A lectin found in ENDOPLASMIC RETICULUM membranes that binds to specific N-linked OLIGOSACCHARIDES found on newly synthesized proteins. It may play role in PROTEIN FOLDING or retention and degradation of misfolded proteins in the endoplasmic reticulum.
A multifunctional protein that is found primarily within membrane-bound organelles. In the ENDOPLASMIC RETICULUM it binds to specific N-linked oligosaccharides found on newly-synthesized proteins and functions as a MOLECULAR CHAPERONE that may play a role in PROTEIN FOLDING or retention and degradation of misfolded proteins. In addition calreticulin is a major storage form for CALCIUM and functions as a calcium-signaling molecule that can regulate intracellular calcium HOMEOSTASIS.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
Complexes of RNA-binding proteins with ribonucleic acids (RNA).
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.
All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.
Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
A group of genetically identical cells all descended from a single common ancestral cell by mitosis in eukaryotes or by binary fission in prokaryotes. Clone cells also include populations of recombinant DNA molecules all carrying the same inserted sequence. (From King & Stansfield, Dictionary of Genetics, 4th ed)
The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.
The production of ANTIBODIES by proliferating and differentiated B-LYMPHOCYTES under stimulation by ANTIGENS.
Antibodies produced by a single clone of cells.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
Any of the ruminant mammals with curved horns in the genus Ovis, family Bovidae. They possess lachrymal grooves and interdigital glands, which are absent in GOATS.
A common name used for the genus Cavia. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research.
Common name for two distinct groups of BIRDS in the order GALLIFORMES: the New World or American quails of the family Odontophoridae and the Old World quails in the genus COTURNIX, family Phasianidae.
Immunoglobulins produced in response to VIRAL ANTIGENS.
Immunoglobulins produced in a response to BACTERIAL ANTIGENS.
Agents that promote the production and release of interferons. They include mitogens, lipopolysaccharides, and the synthetic polymers Poly A-U and Poly I-C. Viruses, bacteria, and protozoa have been also known to induce interferons.
Proteins encoded by the NEF GENES of the HUMAN IMMUNODEFICIENCY VIRUS.
Products of the retroviral NEF GENE. They play a role as accessory proteins that influence the rate of viral infectivity and the destruction of the host immune system. nef gene products were originally found as factors that trans-suppress viral replication and function as negative regulators of transcription. nef stands for negative factor.
An essential amino acid. It is often added to animal feed.
DNA sequences that form the coding region for a protein that down-regulates the expression of human immunodeficiency virus (HIV). nef is short for negative factor.
The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.
A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.
A strain of PRIMATE T-LYMPHOTROPIC VIRUS 1 isolated from mature T4 cells in patients with T-lymphoproliferation malignancies. It causes adult T-cell leukemia (LEUKEMIA-LYMPHOMA, T-CELL, ACUTE, HTLV-I-ASSOCIATED), T-cell lymphoma (LYMPHOMA, T-CELL), and is involved in mycosis fungoides, SEZARY SYNDROME and tropical spastic paraparesis (PARAPARESIS, TROPICAL SPASTIC).
A strain of PRIMATE T-LYMPHOTROPIC VIRUS 2 that can transform normal T-lymphocytes and can replicate in both T- and B-cell lines. The virus is related to but distinct from HTLV-1.
A strain of PRIMATE T-LYMPHOTROPIC VIRUS 2, closely related to the human HTLV-1 virus. The clinical, hematological, and histopathological characteristics of the disease in STLV-infected monkeys are very similar to those of human adult T-cell leukemia. Subgroups include the African green monkey subtype (STLV-I-AGM), for which the nucleotide sequence is 95% homologous with that of HUMAN T-LYMPHOTROPIC VIRUS 1, and the Asian rhesus macaque subtype (STLV-I-MM), for which the nucleotide sequence is 90% homologous with that of HUMAN T-LYMPHOTROPIC VIRUS 1.
Information or data used to ensure the safe handling and disposal of substances in the workplace. Such information includes physical properties (i.e. melting, boiling, flashing points), as well as data on toxicity, health effects, reactivity, storage, disposal, first-aid, protective equipment, and spill-handling procedures.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Elements, compounds, mixtures, or solutions that are considered severely harmful to human health and the environment. They include substances that are toxic, corrosive, flammable, or explosive.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
OXIDOREDUCTASES which mediate vitamin K metabolism by converting inactive vitamin K 2,3-epoxide to active vitamin K.
Large benign, hyperplastic lymph nodes. The more common hyaline vascular subtype is characterized by small hyaline vascular follicles and interfollicular capillary proliferations. Plasma cells are often present and represent another subtype with the plasma cells containing IgM and IMMUNOGLOBULIN A.
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
A species in the genus RHADINOVIRUS, subfamily GAMMAHERPESVIRINAE, isolated from patients with AIDS-related and "classical" Kaposi sarcoma.
A rare neoplasm of large B-cells usually presenting as serious effusions without detectable tumor masses. The most common sites of involvement are the pleural, pericardial, and peritoneal cavities. It is associated with HUMAN HERPESVIRUS 8, most often occurring in the setting of immunodeficiency.
The type species of ROSEOLOVIRUS isolated from patients with AIDS and other LYMPHOPROLIFERATIVE DISORDERS. It infects and replicates in fresh and established lines of hematopoietic cells and cells of neural origin. It also appears to alter NK cell activity. HHV-6; (HBLV) antibodies are elevated in patients with AIDS, Sjogren's syndrome, sarcoidosis, chronic fatigue syndrome, and certain malignancies. HHV-6 is the cause of EXANTHEMA SUBITUM and has been implicated in encephalitis.

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. (1/475)

The role of conformation-based quality control in the early secretory pathway is to eliminate misfolded polypeptides and unassembled multimeric protein complexes from the endoplasmic reticulum, ensuring the deployment of only functional molecules to distal sites. The intracellular fate of terminally misfolded human alpha1-antitrypsin was examined in hepatoma cells to identify the functional role of asparagine-linked oligosaccharide modification in the selection of glycoproteins for degradation by the cytosolic proteasome. Proteasomal degradation required physical interaction with the molecular chaperone calnexin. Altered sedimentation of intracellular complexes following treatment with the specific proteasome inhibitor lactacystin, and in combination with mannosidase inhibition, revealed that the removal of mannose from attached oligosaccharides abrogates the release of misfolded alpha1-antitrypsin from calnexin prior to proteasomal degradation. Intracellular turnover was arrested with kifunensine, implicating the participation of endoplasmic reticulum mannosidase I in the disposal process. Accelerated degradation occurred in a mannosidase-independent manner and was arrested by lactacystin, in response to the posttranslational inhibition of glucosidase II, demonstrating that the attenuated removal of glucose from attached oligosaccharides functions as the underlying rate-limiting step in the proteasome-mediated pathway. A model is proposed in which the removal of mannose from multiple attached oligosaccharides directs calnexin in the selection of misfolded alpha1-antitrypsin for degradation by the proteasome.  (+info)

Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. (2/475)

To analyze the role of glucose trimming and reglucosylation in the binding of substrate proteins to calnexin in the endoplasmic reticulum (ER) of living cells, we made use of the thermosensitive vesicular stomatitis virus tsO45 glycoprotein (G protein). At nonpermissive temperature the G protein failed to fold completely and remained bound to calnexin. When the cells were shifted to permissive temperature, complete folding occurred accompanied by glucosidase-mediated elimination of calnexin-G protein complexes. If release from calnexin was blocked during the temperature shift by inhibiting the glucosidases, folding occurred, albeit at a reduced rate. In contrast, when unfolded by a shift from permissive to nonpermissive temperature, the G protein was reglucosylated rapidly and became capable of rebinding to calnexin. The rate at which calnexin binding occurred showed a 20-min delay that was explained by accumulation of the G protein in calnexin-free exit sites of the ER. These contained the glucosyltransferase responsible for reglucosylation of misfolded glycoproteins but had little or no calnexin. After unfolding and reglucosylation, the G proteins moved slowly from these structures back to the ER where they reassociated with the chaperone. Taken together, these results in live cells fully supported the lectin-only model of calnexin function. The ER exit sites emerged as a potentially important location for components of the quality control system.  (+info)

Surface expression and functional competence of CD3-independent TCR zeta-chains in immature thymocytes. (3/475)

In recombinase-deficient (RAG-2-/-) mice, double-negative thymocytes can be stimulated to proliferate and differentiate by anti-CD3 Abs. CD3 molecules are expressed on the surface of these cells in association with calnexin. In this study, we show that zeta-chains can be recovered as phosphorylated proteins in association with phosphorylated ZAP-70 from anti-CD3-stimulated RAG-2-/- thymocytes, even though they are not demonstrably associated with the CD3/calnexin complex. The lack of a physical association of zeta dimers with the CD3 complex in RAG-2-/- thymocytes and also in a pre-TCR-expressing cell line, as well as the efficient association of zeta dimers with ZAP-70 in the RAG-2-/- thymocytes, suggest that these zeta-chain dimers could contribute to pre-TCR signaling. This idea is supported by the finding that in RAG-2-/- zeta-deficient thymocytes, ZAP-70 and p120cbl were only weakly phosphorylated.  (+info)

Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex. (4/475)

The hepatitis C virus (HCV) genome encodes two membrane-associated envelope glycoproteins (E1 and E2), which are released from the viral polyprotein precursor by host signal peptidase cleavages. These glycoproteins interact to form a noncovalent heterodimeric complex, which is retained in the endoplasmic reticulum. HCV glycoproteins, E1 and E2, are heavily modified by N-linked glycosylation. A recent study has revealed that upon partial deglycosylation with endoglycosidase H only four of the five potential glycosylation sites of HCV glycoprotein E1 are utilized. In this work, the unused glycosylation site on the E1 glycoprotein was identified and the influence of N-linked glycosylation on the formation of the HCV glycoprotein complex was studied by expressing a panel of E1 glycosylation mutants in HepG2 cells. Each of the five potential N-linked glycosylation sites, located at amino acid positions 196, 209, 234, 305 and 325, respectively, on the HCV polyprotein, was mutated separately as well as in combination with the other sites. Expression of the mutated E1 proteins in HepG2 cells indicated that the fifth glycosylation site is not used for the addition of N-linked oligosaccharides and the Pro immediately following the sequon (Asn-Trp-Ser) precludes core glycosylation. The effect of each mutation on the formation of noncovalent E1E2 complexes was also analysed. As determined with the use of a conformation-sensitive monoclonal antibody, mutations at positions N2 and N3 had no, or only minor, effects on the assembly of the E1E2 complex, whereas a mutation at position N1 and predominantly at position N4 dramatically reduced the efficiency of the formation of noncovalent E1E2 complexes.  (+info)

Biogenesis of alpha6beta4 integrin in a human colonic adenocarcinoma cell line involvement of calnexin. (5/475)

The heterodimer alpha6beta4 is a major integrin and the main laminin receptor in epithelia. The alpha6 integrin subunit is proteolytically cleaved, probably by furin, and glycosylated during its biosynthesis. In the present work, we have investigated the kinetics of the assembly process of alpha6beta4 heterodimers in the colonic adenocarcinoma cell line HT29-D4. We demonstrate that the association of alpha6 and beta4 precursors occurs within the ER, while the endoproteolytic cleavage of pro-alpha6 occurs later, probably in the trans-Golgi network. When pro-alpha6 was blocked within the ER by treatment with brefeldin A, its maturation processing was completely prevented without any consequence on its association with beta4 subunit. Low temperature (20 degrees C) also blocked pro-alpha6 maturation, like brefeldin A, but in addition impaired the integrin assembly. Calnexin, an ER resident protein chaperone, was found to be associated with both the alpha6 and beta4 subunit precursors. Our data suggest that calnexin might be responsible for the prolonged retention of pro-alpha6 within the ER compartment and for the defect of integrin subunit association observed at low temperature.  (+info)

Interaction of mammalian neprilysin with binding protein and calnexin in Schizosaccharomyces pombe. (6/475)

Neutral endopeptidase (neprilysin or NEP, EC 3.4.24.11) is a zinc metallo-endopeptidase expressed in many eukaryotic cell types and displaying several important physiological roles. In the brain (and central nervous system), this enzyme is involved in the molecular mechanism of pain by its action in the degradation of enkephalin molecules. In the kidney, NEP is implicated in the degradation of regulatory factors involved in the control of arterial pressure, including atrial natriuretic peptide and bradykinin. In this study we assessed the potential of the fission yeast Schizosaccharomyces pombe to overproduce rabbit NEP and secreted NEP (sNEP, a soluble derivative of this integral membrane protein). Both recombinant NEP and sNEP were produced at high levels (5 mg/l) in this system. Enzymic studies revealed that these recombinant proteins were fully active and exhibit kinetic parameters similar to those of the bona fide enzyme. Immunofluorescence microscopy and enzymic assays demonstrated that recombinant NEP is correctly targeted to the cell membrane. Furthermore, co-immunoprecipitation studies showed that folding intermediates of NEP and sNEP, produced in S. pombe, interact in the endoplasmic reticulum (ER) with binding protein (BiP) and calnexin (Cnx1p). The amount of sNEP coprecipitated with both BiP and Cnx1p augmented when cells were subjected to various stresses causing the accumulation of unfolded proteins in the ER. The interactions of NEP with BiP and Cnx1p were, however, more refractive to the same stresses.  (+info)

Biosynthesis of HLA-C heavy chains in melanoma cells with multiple defects in the expression of HLA-A, -B, -C molecules. (7/475)

Recent investigations have shown that malignant transformation may down-regulate the expression of class I HLA molecules, beta2-microglobulin (beta2m) and members of the antigen-processing machinery. In the present study, we HLA-genotyped and identified at a biochemical level the three (HLA-A25, -B8, -Cw7) class I alleles expressed by the previously described [D'Urso CM et al (1992) J Clin Invest 87: 284-292] beta2m-defective human melanoma FO-1 cell line and tested their ability to interact with calnexin, calreticulin and the TAP (transporter associated with antigen processing) complex. All these alleles were found to bind calnexin, but not calreticulin or the poorly expressed TAP complex, both in parental and beta2m-transfected FO-1 cells, demonstrating a complex defect of class I expression in FO-1 cells. In these conditions, Cw7 heavy chains interacted with calnexin more strongly than A25 and B8, and preferentially accumulated in the endoplasmic reticulum, in both a calnexin-associated and a calnexin-free form. In addition, they could be transported to the cell surface at low levels even in the absence of beta2m, without undergoing terminal glycosylation. These results establish a parallel between HLA-C and the murine Db and Ld molecules which have been found to be surface expressed and functional in beta2m-defective cells. They also demonstrate distinctive features of HLA-C molecules. We propose that the accumulation of several assembly intermediates of HLA-C might favour the binding of peptide antigens not readily bound by HLA-A and -B molecules in neoplastic cells with suboptimal class I expression.  (+info)

Molecular chaperones stimulate the functional expression of the cocaine-sensitive serotonin transporter. (8/475)

The serotonin transporter (SERT) is an N-glycosylated integral membrane protein that is predicted to contain 12 transmembrane regions. SERT is the major binding site in the brain for antidepressant drugs, and it also binds amphetamines and cocaine. The ability of various molecular chaperones to interact with a tagged version of SERT (Myc-SERT) was investigated using the baculovirus expression system. Overexpression of Myc-SERT using the baculovirus system led to substantial quantities of inactive transporter, together with small amounts of fully active and, therefore, correctly folded molecules. The high levels of inactive Myc-SERT probably arose because folding was rate-limiting due, perhaps, to insufficient molecular chaperones. Therefore, Myc-SERT was co-expressed with the endoplasmic reticulum (ER) molecular chaperones calnexin, calreticulin and immunoglobulin heavy chain binding protein (BiP), and the foldase, ERp57. The expression of functional Myc-SERT, as determined by an inhibitor binding assay, was enhanced nearly 3-fold by co-expressing calnexin, and to a lesser degree on co-expression of calreticulin and BiP. Co-expression of ERp57 did not increase the functional expression of Myc-SERT. A physical interaction between Myc-SERT-calnexin and Myc-SERT-calreticulin was demonstrated by co-immunoprecipitation. These associations were inhibited in vivo by deoxynojirimycin, an inhibitor of N-glycan precusor trimming that is known to prevent the calnexin/calreticulin-N-glycan interaction. Functional expression of the unglycosylated SERT mutant, SERT-QQ, was also increased on co-expression of calnexin, suggesting that the interaction between calnexin and SERT is not entirely dictated by the N-glycan. SERT is the first member of the neurotransmitter transporter family whose folding has been shown to be assisted by the molecular chaperones calnexin, calreticulin, and BiP.  (+info)

HIV patients are at a greater risk of developing atherosclerosis than non-infected individuals, partly due to the impairment of the ATP-Binding Cassette A1 (ABCA1) cholesterol transporter by the HIV-1 viral protein Nef leading to accumulation of cholesterol inside the cell. While studying the possible mechanism of Nef-mediated disruption of cholesterol efflux, we found that ABCA1 interacts with Nef, but a direct interaction with Nef is dispensable for the inactivation of ABCA1. Using mass spectroscopy we identified calnexin as a protein that associates with both ABCA1 and Nef and provided evidence to show that in the presence of Nef, ABCA1-calnexin interaction is disrupted leading to ABCA1 retention in the ER, subsequent degradation and impairment of cholesterol efflux. However, the molecular interactions taking place remained unknown as Nef is not known to enter the ER lumen and the domain of calnexin involved in binding to substrate proteins is located within the ER lumen. We hypothesized that ...
Calnexin Calnexin Lumenal domain of calnexin from PDB 1JHN. Available structures: 1jhn Identifiers Symbol(s) CANX; CNX; FLJ26570; IP90; P90 External IDs
BACE457 is the splice variant of β-secretase found in the pancreas. Compared with the brain isoform, BACE501, BACE457 lacks 44 residues in the lumenal domain. Although maturation of BACE501 transiently expressed in HEK293 cells was efficient (this study; Sinha et al., 1999; Vassar et al., 1999; Yan et al., 1999), we found that most of the BACE457 expressed under similar conditions was retained in the ER and became a substrate for ERAD.. The fate of BACE457 and of the soluble mutant BACE457Δ was characterized by a lag phase during which the proteins were extensively oxidized and remained protected from premature degradation during nonproductive attempts at folding in association with the molecular chaperone calnexin. Upon release from calnexin, misfolded BACE457 (and to a lesser extent BACE457Δ) transiently entered into disulfide-bonded complexes before degradation from the ER. Because the lumenal portion of the two proteins is identical, it is likely that attachment at the membrane, or the ...
N-Glycans are modified as part of a quality control mechanism during glycoprotein folding in the endoplasmic reticulum (ER). Glucosidase II (GII) plays a critical role by generating monoglucosylated glycans that are recognized by lectin chaperones, calnexin and calreticulin. To understand how the hydrolytic activity of GIIα is enhanced by the mannose 6-phosphate receptor (MPR) homology domain (MRH domain) of its β subunit, we now report a 1.6 Å resolution crystal structure of the MRH domain of GIIβ bound to mannose. A comparison of ligand-bound and unbound structures reveals no major difference in their overall fold, but rather a repositioning of side chains throughout the binding pocket, including Y372. Mutation of Y372 inhibits GII activity, demonstrating an important role for Y372 in regulating GII activity. Comparison of the MRH domains of GIIβ, MPRs, and the ER lectin OS-9 identified conserved residues that are critical for the structural integrity and architecture of the carbohydrate ...
This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jun 2018 ...
Buy our Recombinant Human Calnexin protein. Ab117167 is a protein fragment produced in Escherichia coli and has been validated in SDS-PAGE. Abcam provides free…
Hosted by the Department of BiochemistryMandatory for all Biochemistry Graduate Students David Thomas, PhD FRSC Department of Biochemistry McGill UniversityAbstract Cells have homeostatic mechanisms that monitor the integrity organelles and proteins and repair or degrade faulty components, termed proteostasis. One example that we have intensively studied is the ER quality system, the Calnexin Cycle. Protein trafficking diseases such as cystic fibrosis arise from recognition of mutant proteins by the quality control mechanism and the retention of the mutant but otherwise function protein in the ER. We have identified correctors of the trafficking of ER retained mutant proteins and identified two types of mechanism, pharmacological chaperones that bind the mutant molecules and proteostasis modulators that act on the quality control mechanisms.
Immunofluorescence microscopy. Cells were plated on coverslips in a 24-well plate and were allowed to grow overnight. Cells were fixed for 15 minutes in a freshly prepared solution of 4% paraformaldehyde in PBS (pH 7.4), and then permeabilized in washing buffer (PBS with 0.2% Triton X-100) for 5 minutes at room temperature. After three washes, the primary antibodies, rabbit anti-human TAP-1 (Calbiochem), and mouse anti-human calnexin (Affinity Bioreagents, Golden, CO), which were diluted in 200 μL of dilution buffer (PBS containing 3% bovine serum and 0.2% Triton X-100) were added. After incubation for 1 hour at room temperature, coverslips were washed thrice in washing buffer and then incubated with the secondary antibodies, fluorescein-conjugated donkey anti-rabbit immunoglobulin (Amersham Biosciences, Inc., Piscataway, NJ) for TAP-1 and Texas red dye-linked goat anti-mouse immunoglobulin (Jackson ImmunoResearch Laboratories, Inc., West Grove, PA) for calnexin, for 1 hour at room temperature. ...
Calnexin antibody (calnexin) for FACS, ICC/IF, IHC, IP, WB. Anti-Calnexin pAb (GTX13504) is tested in Human, Mouse, Monkey, Pig, Rat, Guinea pig, Hamster, Quail, Rabbit, Sheep, Xenopus laevis, Bovine, Sheep samples. 100% Ab-Assurance.
These reference sequences exist independently of genome builds. Explain. These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above. ...
Supplementary Materialsijms-17-01152-s001. reversal from the R residues whatsoever three positions inside the theme impaired their colocalization with ER marker calnexin and resulted in considerably improved cell surface area manifestation. Additionally, these data demonstrate an R to glutamic acidity (E) substitution at placement 2 inside the RXR theme isnt functionally permissible. Furthermore, all generated D2L-R mutants … [Read more…]. ...
Rabbit Polyclonal Calnexin antibody C-Term for FM, IHC, ELISA, WB. Order this anti-Calnexin antibody. | Product number ABIN1607882
Plasmid mEmerald-Calnexin-N-14 from Dr. Michael Davidsons lab contains the insert Calnexin. This plasmid is available through Addgene.
CD160, eFluor 660, clone: eBioCNX46-3 (CNX46-3), eBioscience™ 100μg; eFluor 660 CD160, eFluor 660, clone: eBioCNX46-3 (CNX46-3), eBioscience™ Primary...
Quality control of the endoplasmic reticulum plays a critical role in protein folding, modification and modification of a secretory pathway. As endoplasmic reticulum chaperones, calreticulin and calnexin have similar substrate specificity and share several common features. Yet, surprisingly, mice bearing a disruption in the calreticulin gene die from a lesion in cardiac development and develop significant metabolic problems whereas calnexin-deficient mice are born alive with, yet not understood, neurological problems. Studies with calreticulin and calnexin gene knockout mice and calreticulin- and calnexindeficient cell lines indicate that calnexin is unable to compensate for the loss of calreticulin and conversely, calreticulin cannot compensate for the loss of calnexin. Calreticulin or calnexin deficiency or reduction in the level of ERp57 protein (ERp57 heterozygote mice) leads to development of metabolic disorders as documented by sever changes serum lipids and carbohydrates composition in ...
Function: Calreticulin (CALR) is calcium-binding chaperone that promotes folding oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium ...
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Endoplasmic-reticulum-associated protein degradation (ERAD) designates a cellular pathway which targets misfolded proteins of the endoplasmic reticulum for ubiquitination and subsequent degradation by a protein-degrading complex, called the proteasome. The process of ERAD can be divided into three steps: The recognition of misfolded or mutated proteins depends on the detection of substructures within proteins such as exposed hydrophobic regions, unpaired cysteine residues and immature glycans. In mammalian cells for example, there exists a mechanism called glycan processing. In this mechanism, the lectin-type chaperones calnexin/calreticulin (CNX/CRT) provide immature glycoproteins the opportunity to reach their native conformation. They can do this by way of reglucosylating these glycoproteins by an enzyme called UDP-glucose-glycoprotein glucosyltransferase. Terminally misfolded proteins, however, must be extracted from CNX/CRT. This is carried out by members of the EDEM (ER ...
This family of GBPs is widespread in evolution and plays a key role in ER quality control,ref name=Ellgaard 2003a,Ellgaard, L. and Frickel, E. M. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem Biophys 39, 223-247 (2003),/ref,,ref name=Jorgensen 2003,Jorgensen, M. M., Bross, P. and Gregersen, N. Protein quality control in the endoplasmic reticulum. APMIS Suppl 86-91 (2003),/ref,,ref name=Ellgaard 2003,Ellgaard, L. and Helenius, A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4, 181-191 (2003),/ref,,ref name=Helenius 2004,Helenius, A. and Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73, 1019-1049 (2004),/ref,,ref,Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M. and Helenius, A. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol Cell 13, 125-135 (2004),/ref,,ref,Deprez, P., Gautschi, M. and Helenius, A. More ...
In the present study, we demonstrate that SND1 promotes immune escape of tumor cells through inhibition of MHC-I antigen presentation pathway, leading to impaired antitumor CD8+ T cell response in tumor microenvironment. Physiologically, the nascent unfolded HC of MHC-I would be stabilized by the chaperone calnexin before association with the β2m in ER. Here, we revealed that SND1 physically interacted with the nascent HC of MHC-I molecule in tumor cells. Instead of promoting the assembly of MHC-I molecule, SND1 recruits the nascent HC to VIMP/VCP complex for ERAD pathway. As a result, the MHC-I expression on tumor cell membrane is reduced, leading to impaired CD8+ T cell activation in tumor microenvironment.. SND1 is highly expressed in various cancers and is newly identified as a novel oncoprotein. We have previously reported that SND1 plays important physiological roles in a variety of cellular processes (17-19, 33). By using various methodologies, we identified cytoplasmic SND1 as an ...
Anti-Calnexin, C-Terminal (575-593) Rabbit pAb Anti-Calnexin, C-Terminal (575-593), rabbit polyclonal, recognizes the ~90 kDa calnexin protein. It is validated for Western blotting. - Find MSDS or SDS, a COA, data sheets and more information.
How do chaperones operate in cells? For some major chaperones it is clear what they do, though mostly not how they do it. Hsp60, 70 and 100 families carry out folding, unfolding or disaggregation of proteins. Regarding mechanisms of action, we have the clearest picture of the ATP-driven mechanism of the bacterial Hsp60s, and structures of full-length Hsp70 and 90 family members are beginning to give insights into their allosteric mechanisms. Recent advances are giving an improved understanding of the nature of chaperone interactions with their non-native substrate proteins. There have also been significant advances in understanding the engagement of chaperones in preventing the formation of toxic aggregates in degenerative disease and the relationship of protein quality control to complex biological processes such as ageing.. ...
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Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHAAEQQ RAYLEGRCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
PrA contains a distinct determinant for glycan-independent ERAD (ER associated degradation). A mutant of the vacuolar proteinase A (PrA*-Gldelta4) (gr...
1DUZ: The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site.
TY - JOUR. T1 - Evolving Evidence of Calreticulin as a Pharmacological Target in Neurological Disorders. AU - Kotian, Vignesh. AU - Sarmah, Deepaneeta. AU - Kaur, Harpreet. AU - Kesharwani, Radhika. AU - Verma, Geetesh. AU - Mounica, Leela. AU - Veeresh, Pabbala. AU - Kalia, Kiran. AU - Borah, Anupom. AU - Wang, Xin. AU - Dave, Kunjan R. AU - Yavagal, Dileep R. AU - Bhattacharya, Pallab. PY - 2019/1/1. Y1 - 2019/1/1. N2 - Calreticulin (CALR), a lectin-like ER chaperone, was initially known only for its housekeeping function, but today it is recognized for many versatile roles in different compartments of a cell. Apart from canonical roles in protein folding and calcium homeostasis, it performs a variety of noncanonical roles, mostly in CNS development. In the past, studies have linked Calreticulin with various other biological components which are detrimental in deciding the fate of neurons. Many neurological disorders that differ in their etiology are commonly associated with aberrant levels of ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Protein folding in the endoplasmic reticulum (ER) is error prone, and ER quality control (ERQC) processes ensure that only correctly folded proteins are exported from the ER. Glycoproteins can be retained in the ER by ERQC, and this retention contributes to multiple human diseases, termed ER storage diseases. UDP-glucose:glycoprotein glucosyltransferase (UGGT1) acts as a central component of glycoprotein ERQC, monoglucosylating deglucosylated N-glycans of incompletely folded glycoproteins and promoting subsequent reassociation with the lectin-like chaperones calreticulin and calnexin. The extent to which UGGT1 influences glycoprotein folding, however, has only been investigated for a few selected substrates. Using mouse embryonic fibroblasts lacking UGGT1 or those with UGGT1 complementation, we investigated the effect of monoglucosylation on the soluble/insoluble distribution of two misfolded alpha 1-antitrypsin (AAT) variants responsible for AAT deficiency disease: null Hong Kong (NHK) and Z ...
TY - JOUR. T1 - Assembly and retention of CD1b heavy chains in the endoplasmic reticulum. AU - Sugita, Masahiko. AU - Porcelli, Steven A.. AU - Brenner, Michael B.. PY - 1997/12/1. Y1 - 1997/12/1. N2 - The endoplasmic reticulum (ER) is the site for assembly of MHC class I molecules. Newly synthesized class I heavy chains bind calnexin, an ER-resident molecular chaperone, and dissociate from calnexin following association with β2-microglobulin (β2m). The class I heavy chain:β2m complex then is stabilized by binding endogenous peptides transported to the ER through the TAP molecules. Thus, both β2m and TAP are required for class I Ag presentation. Human CD1b is a β2m-associated, non-MHC-encoded glycoprotein that functions in presentation of lipid Ags to T cells. Despite its structural similarities with class I, CD1b-mediated Ag presentation is TAP independent, and CD1b traffics to endocytic compartments for sampling exogenous Ags. Given these distinctive features of CD1b, we set out to ...
Song, H, et al. (2010) Effects of endoplasmic reticulum stress on group VIA phospholipase A2 in beta cells include tyrosine phosphorylation and increased association with calnexin. J. Biol. Chem.. 2010 Oct 29; 285(44):33843-57. PM ID: ...
Materials. Rat α2B-AR in vector pcDNA3, human β2-AR in vector pBC, rat AT1R in vector pCDM8 and human α1B-AR tagged with green fluorescent protein (GFP) at its C terminus were kindly provided by Drs. Stephen M. Lanier, Dr. John D. Hildebrandt (Medical University of South Carolina, Charleston, SC), Kenneth E. Bernstein, and Kenneth P. Minneman (Emory University, Atlanta, GA), respectively. Antibodies against GFP, phospho-ERK1/2, calnexin, and calreticulin were purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA). Anti-ERK antibodies detecting total ERK1/2 expression were from Cell Signaling Technology, Inc. (Danvers, MA). The α2-AR agonist UK14304, rauwolscine, dimethyl sulfoxide (DMSO), and protein G-Sepharose 4B were obtained from Sigma-Aldrich (St. Louis, MO). [3H]RX821002 (specific activity, 41 Ci/mmol), [3H]CGP12177 (51 Ci/mmol), [7-methoxy-3H]prazosin (70 Ci/mmol), and [125I-Sar1, Ile8]angiotensin II (125I-Ang II) (2200 Ci/mmol) were purchased from PerkinElmer Life and ...
9 Mer Peptide (RL9) From Histone H2A.xBeta-2-microglobulinHLA class I histocompatibility antigen, alpha chain GLeukocyte immunoglobulin-like receptor subfamily B member 1
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SIL1 antibody [N1N3] (SIL1 homolog, endoplasmic reticulum chaperone (S. cerevisiae)) for IHC-P, WB. Anti-SIL1 pAb (GTX116755) is tested in Human, Rat samples. 100% Ab-Assurance.
Dear All Please read attached document for details of 4th international CALRETICULIN workshop to be held at Oxford University in April 2000 If you have problems opening the attachment or are worried about viruses look at our homepage on:- http://www.uwcm.ac.uk/uwcm/mb/crt2000.html Yours sincerely, Paul Eggleton. Dept Biochemistry. University of Oxford. UK ...
Viral interleukin-6 (vIL-6) encoded by human herpesvirus 8 (HHV-8) is believed to contribute via mitogenic, survival, and angiogenic activities to HHV-8-associated Kaposis sarcoma, primary effusion lymphoma (PEL), and multicentric Castlemans disease through autocrine or paracrine mechanisms during latency or productive replication. There is direct evidence that vIL-6 promotes latently infected PEL cell viability and proliferation and also viral productive replication in PEL and endothelial cells. These activities are mediated largely through endoplasmic reticulum (ER)-localized vIL-6, which can induce signal transduction via the gp130 signaling receptor, activating mitogen-activated protein kinase (MAPK) and signal transducer and activator of transcription (STAT) signaling, and interactions of vIL-6 with the ER membrane protein vitamin K epoxide reductase complex subunit 1 variant 2 (VKORC1v2). The latter functional axis involves suppression of pro-apoptotic lysosomal protein cathepsin D by ...
Title: Converging Pathways in the Occurrence of Endoplasmic Reticulum (ER) Stress in Huntingtons Disease. VOLUME: 11 ISSUE: 1. Author(s):R. Vidal, B. Caballero, A. Couve and C. Hetz. Affiliation:Institute of Biomedical Sciences, University of Chile. Independencia 1027, Santiago, P.O. BOX 70086, Chile.. Keywords:Huntingtons disease, ER stress, protein misfolding, Unfolded protein response, Huntingtin, endoplasmic reticulum, neurodegenerative disease, cognitive defects, dementia, polyglutamine, spinobulbar muscular atrophy, spinocerebellar ataxias, Machado-Joseph Disease, mutations, protein conformational disorders, aggregation, apoptosis, translocation, homeostasis, PERK signaling, morphogenesis, phenotype, mutant Htt, tunicamycin, vesicular trafficking, autophagy, ERAD, calnexin cycle, chaperones, familial amyotrophic lateral sclerosis, brefeldin A, ER/Golgi trafficking, Parkinsons disease, Synuclein, NMDAR, AMPA receptors, axonal transport, Macroautophagy, autophagosome, Beclin-1, ...
The biogenesis of nascent proteins translocated into the calcium‐rich, oxidizing milieu of the endoplasmic reticulum (ER) lumen is assisted by a group of resident ER proteins that include molecular chaperones and folding enzymes. These specialized ER proteins are constitutively expressed in all cells, where they play a role in monitoring and assisting the maturation of normal proteins (Gething and Sambrook, 1992; Hendrick and Hartl, 1993) and are essential for proper steady‐state operations of the eukaryotic secretory pathway. Expression of mutant secretory pathway proteins or exposure of cells to agents that adversely affect ER protein folding and maturation all result in the accumulation of unfolded proteins in the ER, thereby activating an inter‐organelle signaling pathway linking the ER and nucleus. This response, termed the unfolded protein response (UPR), includes the coordinate transcriptional up‐regulation of ER chaperones and folding enzymes (Lee, 1992).. In yeast, an ER ...
Abstract Introduction: Calreticulin is a multi-functioning protein located in the endoplasmic reticulum. Several functions have been attributed to calreticulin including lectin-like chaperoning, regulation of gene expression, cell adhesion, auto-immunity and calcium homeostasis. As an endoplasmic reticulum chaperone calreticulin regulates the maturation and folding of several trans-membrane proteins. We hypothesized that as an endoplasmic reticular protein it regulates the expression folding and maturation of epidermal growth factor receptor (EGFR). To date no information is available about the role of calreticulin in EGFR expression and folding. Methods: Wild type calreticulin deficient (crt -/-) and mouse lung cancer cells isolated from transgenic mice over expressing calreticulin was used to examine the expression, localization and function of EGFR. Western blot analysis was used to determine the protein expression. Immunocytochemical staining of cells was utilized to determine localization of EGFR
def: A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1. [PMID:12475965 ...
EM (fig. S1, C to H) and biochemical fractionation (fig. S2) experiments show the localization of StAR and GRP78 in the ER, MAM, and mitochondria. Because GRP78 is a highly abundant chaperone at the ER that interacts with StAR, it is likely facilitating its folding and subsequent activity (17). We next knocked down the expression of GRP78 by small interfering RNA (siRNA) in COS-1 cells (Fig. 1C) or adenosine 3′,5′-monophosphate (cAMP)-stimulated MA-10 cells (Fig. 1D) and identified changes in StAR expression by Western blotting. In the absence of GRP78, the expression of StAR was greatly reduced, but the negative control siRNA had no effect, suggesting that GRP78 is responsible for StAR expression. As expected, the absence of GRP78 did not affect the expression of mitochondrial VDAC2 or the ER proteins PACS2 and calnexin (Caln) (Fig. 1, C and D). As shown in Fig. 1E, pregnenolone synthesis in MA-10 cells decreased from 25 ng/ml in control cells to 2 ng/ml in the absence of GRP78. The ...
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Plasmid mEmerald-Calreticulin-C-10 from Dr. Michael Davidsons lab contains the insert Calreticulin. This plasmid is available through Addgene.
HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described. [provided by RefSeq, Jul 2008 ...
HLA-A belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-A alleles have been described. [provided by RefSeq, Jul 2008 ...
ENCODES a protein that exhibits peptide antigen binding (ortholog); INVOLVED IN alpha-beta T cell activation involved in immune response (ortholog); antigen processing and presentation of endogenous peptide antigen via MHC class Ib (ortholog); antigen processing and presentation of exogenous peptide antigen via MHC class Ib (ortholog); FOUND IN external side of plasma membrane (ortholog); MHC class Ib protein complex (ortholog); INTERACTS WITH flavonoids; 1,2-dimethylhydrazine (ortholog); 2,3,7,8-tetrachlorodibenzodioxine (ortholog)
We have identified novel interactions between ER chaperones and foldases using different methods tailored for the ER. The affinity capture and tagged bait experiments detect complexes whereas ER-MYTHS defines binary interactions. Using these methods, we have developed a high quality map that is rich in new interactions between ER lumenal proteins, and we have defined in detail one type of physical and functional interaction.. A remarkable finding was the interaction of six different PDI family members with PPIs. Interaction between PDIs and PPIs that catalyze rate-limiting steps of protein folding could allow their activities to be concentrated simultaneously on a folding substrate protein. Functional PDI-PPI interactions have been investigated in vitro (51, 52), with one study demonstrating that an interaction between bovine PDI and cyclophilin B modestly enhanced the chaperone activity of PDI (53). Although we observed no effect of cyclophilin B on the oxidoreductase activity of ERp72 in ...
Any of a group of proteins in living cells that assist newly synthesized or denatured proteins to fold into their functional three-dimensional structures. The chaperones bind to the protein and prevent improper interactions within the polypeptide chain, so that it assumes the correct folded orientation. This process may require energy in the form of ATP. Other functions include assisting the translocation of proteins across the membranes of cell organelles and binding denatured proteins under stress conditions or in degenerative disease. There are several unrelated families of chaperones, including five classes of heat-shock proteins - HSP25 (small heat-shock proteins), HSP60, HSP70, HSP90, and HSP100 - chaperonins, calnexin, and calreticulin. ...
The ER-resident MHC class I PLC forms a key target for viral immune evasion. When analyzing the subcellular distribution of BNLF2a, we observed strict membrane association and colocalization with TAP and the ER markers calnexin and PDI (Figs. 1⇑, 2⇑, 6⇑D, and 7B), reminiscent of two other TAP inhibitors, HCMV US6 (35, 36) and BHV-1 UL49.5 (33). The latter two represent integral type I membrane proteins with cleavable signal sequences at their N termini for cotranslational membrane insertion, as well as transmembrane domains toward their C termini. In contrast, BNLF2a lacks an obvious N-terminal signal sequence (Fig. 1⇑A). Still, the EBV-encoded TAP inhibitor is membrane associated and, even in the absence of TAP, localizes to the ER (Fig. 6⇑D). In this respect, BNLF2a differs from HSV ICP47, which also lacks a signal sequence but has been detected primarily as a cytosolic protein with small amounts associating with membranes (26, 31). ICP47 is unstructured in aqueous solutions but ...
In this study, we have identified two unique aspects of STIM1 function that are separate but overlapping. We discovered that ERp57, an ER‐resident oxidoreductase, interacts with the ER luminal domain of STIM1 and affects SOC. Although ERp57−/− cells show reduced ER Ca2+ stores, expression of ERp57 in ERp57−/− cells inhibits SOC without restoring Ca2+ stores, supporting a role for ERp57 on SOC by interaction with STIM1 rather than its effects on the size of ER Ca2+ stores. ERp57/STIM1 interaction involves two conserved cysteines (C49 and C56), forming a disulphide bridge upstream from the EF‐hand domain. The mutation of these residues to eliminate the disulphide bond rendered STIM1 incapable of proper punctae translocation. As the conserved C49 and C56 are located in close proximity to the EF‐hand Ca2+ sensor in STIM1, these results indicated that the conformation of the disulphide‐containing region of STIM1 might affect that of the EF hand (and vice versa). Indeed, extensive in ...
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... and calnexin in glycoprotein folding and quality control". Proceedings of the National Academy of Sciences of the United States ... and calnexin (CNX; membrane bound). Favoured by the highly oxidizing environment of the ER, protein disulfide isomerases ...
Bergeron JJ, Brenner MB, Thomas DY, Williams DB (March 1994). "Calnexin: a membrane-bound chaperone of the endoplasmic ... This family includes Calreticulin, Calnexin and Camlegin. Michalak M, Milner RE, Burns K, Opas M (August 1992). "Calreticulin ...
2005). "Calnexin suppresses GD3 synthase-induced apoptosis". FASEB J. 18 (13): 1553-5. doi:10.1096/fj.04-1675fje. PMID 15319364 ...
... and calnexin are also integral proteins in the production of MHC class I Proteins. As newly synthesized MHC class ... Calreticulin and Calnexin's ability to bind carbohydrates associates them with the lectin protein family. In normal cellular ... Both proteins, calnexin and calreticulin, have the function of binding to oligosaccharides containing terminal glucose residues ... Del Bem LE (Feb 2011). "The evolutionary history of calreticulin and calnexin genes in green plants". Genetica. 139 (2): 225-9 ...
Bergeron also discovered calnexin with Dr. David Y. Thomas and uncovered the calnexin code along with Dr. Ari Helenius and Dr. ... Calnexin through additional proteins that together makeup the calnexin cycle will not only guide folding but will also sense if ... When this happens, calnexin will send the incorrectly folded protein to be degraded through other sugar recognizing proteins ... He is a Rhodes Scholar (Class of 1966). He is best known for the discovery of calnexin, endosomal signalling and organellar ...
... calnexin, and Erp57 (PDIA3). Calnexin acts to stabilize the class I MHC α chains prior to β2m binding. Following complete ... assembly of the MHC molecule, calnexin dissociates. The MHC molecule lacking a bound peptide is inherently unstable and ...
2002). "Calnexin deficiency and endoplasmic reticulum stress-induced apoptosis". Biochemistry. 41 (8): 2850-8. doi:10.1021/ ...
Guérin, Reneé; Beauregard, Pascale B.; Leroux, Alexandre; Rokeach, Luis A. (2009). "Calnexin Regulates Apoptosis Induced by ...
Oda Y, Hosokawa N, Wada I, Nagata K (2003). "EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin ... "Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle". Science. 299 (5611): 1397-400. doi:10.1126/ ...
Rubio ME, Wenthold RJ (1999). "Calnexin and the immunoglobulin binding protein (BiP) coimmunoprecipitate with AMPA receptors". ...
Li X, Su RT, Hsu HT, Sze H (January 1998). "The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat ...
This protein localizes to the endoplasmic reticulum (ER) and interacts with lectin chaperones calreticulin and calnexin (CNX) ... and polypeptide binding sites of calnexin and calreticulin". The Journal of Biological Chemistry. 277 (33): 29686-97. doi: ...
Lp(a) has been shown to interact with calnexin, fibronectin, and fibrinogen beta chain. Lipoprotein Apolipoprotein Very-low- ...
He elucidated the molecular features of substrate recognition by endoplasmic reticulum chaperones calreticulin and Calnexin. He ...
Examples include: calmodulin calnexin calreticulin gelsolin Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (2013). "The ...
A molecular chaperone protein called calnexin and an enzyme called ERp57 assist in the folding process. Calnexin holds the HLA- ... Calnexin then dissociates with the complex, now referred to as a peptide loading complex, and is replaced by calreticulin, ...
There are several ER chaperones involved in MHC-I assembly, such as calnexin, calreticulin and tapasin. Peptides are loaded to ...
A chaperone protein (calnexin/calreticulin) binds to the unfolded or partially folded protein to assist protein folding. The ...
"A lymphocyte-specific Ltk tyrosine kinase isoform is retained in the endoplasmic reticulum in association with calnexin". J. ...
In fungal infection, it has been shown an IL-17 producing clone with a TCR specific for calnexin from Blastomyces dermatitidis ... "Calnexin induces expansion of antigen-specific CD4(+) T cells that confer immunity to fungal ascomycetes via conserved epitopes ...
Chen Y; Le Cahérec F; Chuck SL (1998). "Calnexin and other factors that alter translocation affect the rapid binding of ...
PMP22 protein is glycosylated with an N terminus-linked sugar and co-localized with the chaperone protein calnexin in the ER. ... Dickson KM, Bergeron JJ, Shames I, Colby J, Nguyen DT, Chevet E, Thomas DY, Snipes GJ (July 2002). "Association of calnexin ...
Chen Y, Le Cahérec F, Chuck SL (May 1998). "Calnexin and other factors that alter translocation affect the rapid binding of ...
Del Bem LEV (2011). "The evolutionary history of calreticulin and calnexin genes in green plants". Genetica 139 (2): 225-9. ... "Getting In and Out from Calnexin/Calreticulin Cycles". J. Biol. Chem. 283 (16): 10221-5. PMC 2447651. PMID 18303019. doi ...
... and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5 ...
... calnexin and Stim-1. Calcium ion involvement in the countertransport of chloride ions also supports the idea that Best1 is ...
In this mechanism, the lectin-type chaperones calnexin/calreticulin (CNX/CRT) provide immature glycoproteins the opportunity to ...
The lectins, calnexin and calreticulin, have high affinities for monoglucosylated proteins and the ER chaperones that associate ... The main proteins involved in the ER quality control system are UGGT, the ER lectin chaperones (calnexin and calreticulin), and ...
This process is vital since the lectin chaperones calnexin and calreticulin, involved in protein quality, bind to the ...
Chaperone proteins in the endoplasmic reticulum, such as calnexin and calreticulin, bind to the three glucose residues present ...
Mouse models. Calnexin-deficient mice were generated as previously described (18). To inactivate the calnexin gene in the T ... Calnexin-deficient mice are resistant to induction of EAE. To test whether high abundance of calnexin is important to MS ... Transgenic Canx-/- mice expressing full-length calnexin protein. (A) Abundance of calnexin mRNA in fibroblast cell lines ... To generate calnexin rescue mice, WT CD1/C57BL6 mice expressing the transgene were crossed with calnexin-deficient mice, and ...
immunogen = synthetic peptide: T A P P S S P K V T Y K A P V P T G E conj. to KLH, corresponding to aa50-68 of human Calnexin. ...
immunogen = C-terminus peptide (A E E D E I L N R S P R N R K P R R E) of rat calnexin with an added cysteine, conj. to BSA ...
Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting ... Calnexin at the US National Library of Medicine Medical Subject Headings (MeSH) Benyair R, Ron E, Lederkremer GZ (2011). ... Calnexin is a chaperone, characterized by assisting protein folding and quality control, ensuring that only properly folded and ... Calnexin associates with the protein folding enzyme ERp57 to catalyze glycoprotein specific disulfide bond formation and also ...
Rabbit polyclonal Calnexin antibody. Validated in WB, ICC/IF and tested in Mouse, Rat, Dog, Human, Pig, Chinese hamster. Cited ... Primary - Rabbit Anti-Calnexin antibody (ab10286) WB, ICC/IF Protein - Recombinant Human Calnexin protein (ab115706) WB, SDS- ... All lanes : Anti-Calnexin antibody (ab10286) at 1/4000 dilution. Lane 1 : HeLa (Total cell lysate). Lane 2 : HeLa (Membrane ... Anti-Calnexin antibody (ab10286) at 1/1000 dilution + MCF7 cells. Secondary. Goat anti rabbit at 1/10000 dilution. Predicted ...
Rabbit polyclonal Calnexin antibody validated for WB, IP, IHC, Flow Cyt, ICC/IF and tested in Human, Mouse, Rat and Rabbit. ... Anti-Calnexin antibody (ab75801) at 1/2000 dilution ((in TBS with 0.05% TW-20)) + HeLa cell lysate. Secondary. An HRP- ... Myhill N et al. The subcellular distribution of calnexin is mediated by PACS-2. Mol Biol Cell 19:2777-88 (2008). PubMed: ... ab75801 staining Calnexin in HeLa cells by ICC/IF (Immunocytochemistry/immunofluoresence). Cells were fixed with 4% PFA for 20 ...
"Palmitoylated calnexin is a key component of the ribosome-translocon complex.". Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic ... "Palmitoylated calnexin is a key component of the ribosome-translocon complex.". Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic ... "Palmitoylated calnexin is a key component of the ribosome-translocon complex.". Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic ... "Palmitoylated calnexin is a key component of the ribosome-translocon complex.". Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic ...
Michael Davidsons lab contains the insert Calnexin. This plasmid is available through Addgene. ... mPlum-Calnexin-N-14 was a gift from Michael Davidson (Addgene plasmid # 55954 ; http://n2t.net/addgene:55954 ; RRID:Addgene_ ...
... which completely released the protein from calnexin. These observations directly demonstrate that calnexin can act exclusively ... Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, ... Conformation-independent binding of monoglucosylated ribonuclease B to calnexin.. Zapun A1, Petrescu SM, Rudd PM, Dwek RA, ... Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked ...
Mitochondria were closer to the ER in cells without calnexin than in cells with calnexin. This enabled calnexin knockout cells ... We found that calnexin stimulated the ATPase activity of SERCA by maintaining its redox state. This function enabled calnexin ... The ER chaperone calnexin controls mitochondrial positioning and respiration. By Tomás Gutiérrez, Hong Qi, Megan C. Yap, Nasser ... The ER chaperone calnexin controls mitochondrial positioning and respiration. By Tomás Gutiérrez, Hong Qi, Megan C. Yap, Nasser ...
Calreticulin and calnexin are Ca2+-binding chaperones localized in the endoplasmic reticulum of eukaryotes acting in ... Calreticulin Calnexin Chaperones Evolution Green plants Electronic supplementary material. The online version of this article ( ... Calnexin founder gene in land plants was inherited from basal green algae during evolution in a very conservative copy number. ... Crofts AJ, Denecke J (1998) Calreticulin and calnexin in plants. Trends Plants Sci 3:396-399CrossRefGoogle Scholar ...
... products and learn more about Calnexin Mouse, Unlabeled, Clone: 37, BD 150µg; Unlabeled:Life Sciences 150µg; Unlabeled. ... Neither calnexin nor calreticulin contain the calcium-binding motif, known as the "E-F hand" found in the calmodulin family of ... Calnexin is a 90kDa integral membrane protein located primarily in the ER. It contains a long N-terminal calcium-binding domain ... Calnexin associates with several cell surface proteins as they pass through the ER. Since it also forms complexes with other ...
EBI3 augmented IL-23Rα expression via binding to the chaperone molecule calnexin and to IL-23Rα in a peptide-dependent manner, ... Indeed, EBI3 failed to augment the IL-23Rα expression in the absence of endogenous calnexin. Moreover, EBI3 poorly augmented ... EBV-induced gene 3 augments IL-23Rα protein expression through a chaperone calnexin. ... EBV-induced gene 3 augments IL-23Rα protein expression through a chaperone calnexin. ...
Mouse anti-Calnexin, DyLight 350, Clone: IE2.1C12, Novus Biologicals 100 Tests; DyLight 350 Life Sciences:Antibodies:Primary ... Calnexin Monoclonal antibody specifically detects Calnexin in Human samples. It is validated for Western Blot, Flow Cytometry, ... calnexin, CNX, IP90FLJ26570, Major histocompatibility complex class I antigen-binding protein p88, P90. ... Partial recombinant human Calnexin protein (between amino acids 1-300) [UniProt# P27824]. ...
Calnexin is a calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. As a ... Rabbit anti Calnexin Polyclonal Antibody; Description. Calnexin is a calcium-binding protein that interacts with newly ... GenScript Rabbit Anti-Calnexin Polyclonal Antibody detects endogenous levels of human calnexin protein. Sequence homology ... GenScript Rabbit Anti-Calnexin Polyclonal Antibody is developed in rabbit using a KLH-coupled synthetic peptide within residues ...
Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein ... Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with ... Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits ... Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570. ...
... calnexin) for FACS, ICC/IF, IHC, IP, WB. Anti-Calnexin pAb (GTX13504) is tested in Human, Mouse, Monkey, Pig, Rat, Guinea pig, ... calnexin. Background. Calnexin, also referred to as IP90, p88 and p90, is an ~90 kDa integral membrane protein of the ... Calnexin contains a large ER luminal domain (461 amino acids), a transmembrane segment (22 amino acids), and a cytoplasmic tail ... WB: Use at a dilution of 1/2000 (this dilution was sufficient for detection of Calnexin in 20μg of HeLa heat shocked cell ...
Order this anti-Calnexin antibody. , Product number ABIN1607882 ... Rabbit Polyclonal Calnexin antibody C-Term for FM, IHC, ELISA, ... anti-Calnexin antibody (CANX) (C-Term) Calnexin antibody (CANX) (C-Term). Details for Product anti-CANX Antibody No. ... anti-Mammalian Calnexin antibody for Immunoprecipitation Show more 1 anti-Mammalian Calnexin antibody for Immunoprecipitation ... Calnexin (CANX Antibody Abstract) Background Calnexin, also referred to as IP90, p88 and p90, is an ~90 kDa integral membrane ...
Stress relief protein modulation by calnexin. Ann N Y Acad Sci. 1996 Sep 30; 793:479-84. ...
Feb 14, 2020 anti ma2 antibody, calnexin antibody by Lillian Williamson The acute side effects of traditional chemotherapeutic ... To fix the limits, the calnexin immunoglobulin medication conjugates have developed comprising tumor-selective antibody-linked ...
Calnexin antibody for Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)). ... Product Details anti-Calnexin Antibody Target Details Calnexin Application Details Handling References for anti-Calnexin ... Target Details Calnexin Product Details anti-Calnexin Antibody Application Details Handling References for anti-Calnexin ... Product Details anti-Calnexin Antibody Target Details Calnexin Handling References for anti-Calnexin antibody (ABIN152677) ...
Furthermore, calnexin deficiency in mice did not alter the development or function of the immune system. Instead, the loss of ... mice expressing recombinant calnexin (. Canx-/-. -Tg-CanxFL). Data presented are mean ± SEM of 5 independent experiments (20 ... Conversely, mice lacking calnexin exhibited resistance to EAE induction, no evidence of immune cell infiltration into the CNS, ... These findings identify calnexin in brain endothelial cells as a potentially novel target for developing strategies aimed at ...
Roles of calreticulin and calnexin during mucin synthesis in LS180 and HT29/A1 human colonic adenocarcinoma cells Biochem J ( ... We have studied the interaction of ApoB with two lectin-like chaperones of the Endoplasmic Reticulum (ER)Calnexin (CN) and ... Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin Biochem J (August ... Interaction of Newly Synthesized Apolipoprotein B with Calnexin and Calreticulin Requires Glucose Trimming in the Endoplasmic ...
Using structural models of Nef and calnexin, possible Nef-calnexin interaction models were built using docking servers. ... Using calnexin mutants lacking a luminal or cytoplasmic domain, we identified that the C-terminal cytoplasmic domain is ... Using mass spectroscopy we identified calnexin as a protein that associates with both ABCA1 and Nef and provided evidence to ... In conclusion, lysine residues at positions 4 and 7 on Nef were found to be indispensable for interacting with calnexin and ...
Association of p12I with calreticulin and calnexin. (A and B) Coimmunoprecipitation of p12I with calreticulin or calnexin. p12I ... p12I is associated with calreticulin and calnexin.Calreticulin and calnexin, ER resident proteins, bind to a variety of viral ... The fact that p12I colocalizes with calreticulin and calnexin in the ER implied that calreticulin and calnexin, as molecular ... and calreticulin or calnexin. The 16-kDa subunit protein exhibited moderate binding to calnexin but failed to bind calreticulin ...
Effect of ionomycin on interaction of calnexin with vesicular stomatitis virus glycoprotein is cell type-specific. Journal of ...
Rabbit pAb Anti-Calnexin, C-Terminal (575-593), rabbit polyclonal, recognizes the ~90 kDa calnexin protein. It is validated for ... Recognizes the ~90 kDa calnexin protein. Background. Calnexin is an ER transmembrane protein that transiently associates with ... Anti-Calnexin, C-Terminal (575-593), rabbit polyclonal, recognizes the ~90 kDa calnexin protein. It is validated for Western ... More,, Anti-Calnexin, C-Terminal (575-593), rabbit polyclonal, recognizes the ~90 kDa calnexin protein. It is validated for ...
Increased tumour protein levels of calnexin may be of prognostic significance in CRC, and calnexin may represent a potential ... The calnexin gene was silenced using siRNA in HCT116 cells. There were no increased levels of ER stress proteins in tumour ... However, increased calnexin protein levels were predictive of poor clinical outcome in the patient cohort. Data were validated ... The expression levels of ER stress proteins calnexin, calreticulin, GRP78 and GRP94 were determined in n = 23 Stage II and III ...
This report identifies interactions of vIL-6 and VKORC1v2 with calnexin cycle enzymes GlucII and UGGT1, which are involved in ... Human Herpesvirus 8 Interleukin-6 Interacts with Calnexin Cycle Components and Promotes Protein Folding. by Physicians Weekly ... Here, we show that both vIL-6 and VKORC1v2 interact with calnexin cycle proteins UDP-glucose:glycoprotein glucosyltransferase 1 ...
Effects of redox potential and calnexin association on the folding and assembly of the Kb molecule. RMA cells were pulsed for 1 ... Figure 4: Effects of redox potential and calnexin association on the folding and assembly of the Kb molecule. RMA cells were ... Figure 4: Effects of redox potential and calnexin association on the folding and assembly of the Kb molecule. RMA cells were ...
  • Calnexin (CANX) belongs to the calnexin family of molecular chaperones. (prospecbio.com)
  • EAE was induced by MOG 35-55 immunization of WT, Canx +/- (heterozygote), Canx -/- , and Canx -/- mice expressing recombinant calnexin ( Canx -/- -Tg-CanxFL). (jci.org)
  • Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER). (wikipedia.org)
  • Calnexin Monoclonal antibody specifically detects Calnexin in Human samples. (fishersci.com)
  • GenScript Rabbit Anti-Calnexin Polyclonal Antibody is developed in rabbit using a KLH-coupled synthetic peptide within residues 250-300 of human calnexin protein (Swiss Prot: P27824). (genscript.com)
  • GenScript Rabbit Anti-Calnexin Polyclonal Antibody detects endogenous levels of human calnexin protein. (genscript.com)
  • To fix the limits, the calnexin immunoglobulin medication conjugates have developed comprising tumor-selective antibody-linked drugs, together with the potential to significantly broaden the therapeutic selection. (amsamoatourism.com)
  • Western Blot: Calnexin Antibody (AF18) [ABIN152677] - Analysis of 25 ug of HepG2 lysate. (antibodies-online.com)
  • Immunocytochemistry/Immunofluorescence: Calnexin Antibody (AF18) [ABIN152677] - Staining of Calnexin in A549 Cells. (antibodies-online.com)
  • Immunocytochemistry/Immunofluorescence: Calnexin Antibody (AF18) [ABIN152677] - Transfected COS7 cells were blocked in 1% BSA, 5% normal goat serum, and 0.1% Triton X-100 in 1X PBS, and then stained (1:500), followed by a fluorophore-conjugated goat anti-mouse IgG secondary antibody (red). (antibodies-online.com)
  • Immunohistochemistry-Paraffin: Calnexin Antibody (AF18) [ABIN152677] - Both normal and cancer biopsies of deparaffinized Human hepatocarcinoma tissues. (antibodies-online.com)
  • Primary antibody: Anti-Calnexin, C-Terminal (575-593) Rabbit pAb (Cat. (merckmillipore.com)
  • Calnexin is a chaperone, characterized by assisting protein folding and quality control, ensuring that only properly folded and assembled proteins proceed further along the secretory pathway. (wikipedia.org)
  • Calnexin associates with the protein folding enzyme ERp57 to catalyze glycoprotein specific disulfide bond formation and also functions as a chaperone for the folding of MHC class I α-chain in the membrane of the ER. (wikipedia.org)
  • Since it also forms complexes with other resident ER proteins involved in the Ca 2 + -dependent retention of proteins, calnexin may act as a chaperone. (fishersci.com)
  • EBI3 augmented IL-23Rα expression via binding to the chaperone molecule calnexin and to IL-23Rα in a peptide-dependent manner, but not glycan-dependent manner. (jci.org)
  • It has been shown that calnexin is a chaperone that retains incompletely or improperly folded proteins in the ER. (genetex.com)
  • Here, we discovered that calnexin, an ER chaperone, is highly abundant in human brain endothelial cells of MS patients. (jci.org)
  • Here we show that calnexin, a molecular chaperone located in the endoplasmic reticulum (ER), plays an important role in regulating the cytosolic free calcium concentration ([Ca(2+)]c) in Aspergillus nidulans Inactivation of calnexin (ClxA) in A. nidulans caused severe defects in hyphal growth and conidiation under ER stress caused by the ER stress-inducing agent dithiothreitol (DTT) or high temperature. (readbyqxmd.com)
  • Finally, we examined the relationship between the interaction of mouse heavy chain-beta 2m heterodimers with TAP and with the resident ER chaperone, calnexin. (rupress.org)
  • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. (chemeurope.com)
  • The integrin chains beta 1 and alpha 6 associate with the chaperone calnexin prior to integrin assembly. (chemeurope.com)
  • Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). (chemeurope.com)
  • Calnexin (CNX) is a highly conserved endoplasmic reticulum (ER) chaperone protein. (edu.au)
  • RESULTS After acute hyperglycemia and moderate diabetes, more LPL is processed into an active dimeric form, which involves the endoplasmic reticulum chaperone calnexin. (diabetesjournals.org)
  • Cleavage of the terminal mannose on branch A, the only acceptor for the UGT1-catalyzed re-glucosylation, results in the irreversible exclusion of the folding-defective polypeptide from the calnexin chaperone system. (biologists.org)
  • Calreticulin and calnexin possibly share a common origin, and both proteins are present along all green plants lineages. (springer.com)
  • Calnexin associates with several cell surface proteins as they pass through the ER. (fishersci.com)
  • Neither calnexin nor calreticulin contain the calcium-binding motif, known as the "E-F hand" found in the calmodulin family of proteins. (fishersci.com)
  • Integral membrane ER resident proteins, like calnexin, often lack this KDEL sequence but contain positively charged cytosolic residues that ensure ER retention. (genetex.com)
  • However, the molecular interactions taking place remained unknown as Nef is not known to enter the ER lumen and the domain of calnexin involved in binding to substrate proteins is located within the ER lumen. (ahajournals.org)
  • Moreover, using coimmunoprecipitation assays, we identify the direct binding of p12 I with both calreticulin and calnexin, resident ER proteins which regulate calcium storage. (asm.org)
  • The expression levels of ER stress proteins calnexin, calreticulin, GRP78 and GRP94 were determined in n = 23 Stage II and III colon cancer fresh frozen tumour and matched normal tissue samples. (biomedcentral.com)
  • Here, we show that both vIL-6 and VKORC1v2 interact with calnexin cycle proteins UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), catalyzing monoglucosylation of N-glycans, and oppositely-acting glucosidase II (GlucII) and that vIL-6 can promote protein folding. (physiciansweekly.com)
  • Calnexin, protein disulfide isomerase, heat shock proteins and thioredoxin were predominantly affected as the ER proteins in response to calcium, and ER-associated degradation-related proteins of HCP-like superfamily protein were up-regulated under stress exposure and then down-regulated. (readbyqxmd.com)
  • Calnexin might bind selectively to carbohydrates within glycoproteins, or to hydrophobic surfaces of secretory proteins while they form proper disulfide bonds (Wada, I., W.-J. Ou, M.-C. Liu, and G. Scheele, J. Biol. (rupress.org)
  • Confocal microscopic time series with green fluorescent protein (GFP)-tagged calnexin and calreticulin demonstrated the accumulation of both proteins in the phagocytic cup of L. pneumophila -infected host cells. (microbiologyresearch.org)
  • Calnexin belongs among chaperones , which are characterized by their main function of assisting protein folding and quality control, ensuring that only properly folded and assembled proteins proceed further along the secretory pathway. (chemeurope.com)
  • Retention of unassembled components of integral membrane proteins by calnexin. (chemeurope.com)
  • In addition, calnexin T-DNA mutant lines showed no change in transcript abundance of a number of plasmodesmata-related proteins. (edu.au)
  • In yeast, KAR2, which is homologous to Bip, and CNE1, a homologue of calnexin, have been shown to be required for the proteasomal degradation of ER proteins ( 20 , 21 ). (jimmunol.org)
  • Calnexin primarily binds to newly formed monoglucosylated proteins in the ER ( 26 ). (jimmunol.org)
  • Calreticulin and calnexin are Ca 2+ -binding chaperones localized in the endoplasmic reticulum of eukaryotes acting in glycoprotein folding quality control and Ca 2+ homeostasis. (springer.com)
  • The evolutionary histories of calreticulin and calnexin gene families were inferred by comprehensive phylogenetic analyses using 18 completed genomes and ESTs covering the major green plants groups, from green algae to angiosperms. (springer.com)
  • A comprehensive classification in possible groups of orthologs and a catalog of calreticulin and calnexin genes from green plants are provided. (springer.com)
  • Crofts AJ, Denecke J (1998) Calreticulin and calnexin in plants. (springer.com)
  • Calnexin, also referred to as IP90, p88 and p90, is an ~90 kDa integral membrane protein of the endoplasmic reticulum (ER). (genetex.com)
  • Using defined components, the binding of ribonuclease B (RNase B) Man7-Man9 glycoforms to the luminal domain of calnexin was observed in vitro only if RNase B was monoglucosylated. (nih.gov)
  • We hypothesized that Nef interacts with the C-terminal cytoplasmic domain of calnexin and that inhibiting this interaction would rescue ABCA1 function and expression. (ahajournals.org)
  • Lumenal domain of calnexin from PDB 1JHN. (chemeurope.com)
  • Anti-Calnexin, C-Terminal (575-593), rabbit polyclonal, recognizes the ~90 kDa calnexin protein. (merckmillipore.com)
  • We have studied the interaction of ApoB with two lectin-like chaperones of the Endoplasmic Reticulum (ER)'Calnexin (CN) and Calreticulin (CR). (portlandpress.com)
  • Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. (rupress.org)
  • 1994). "The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin. (chemeurope.com)
  • Calnexin transfer DNA (T-DNA) mutant lines exhibited increased transcript abundances of a number of other ER chaperones, including calreticulins, suggesting a degree of redundancy. (edu.au)
  • This assembly relies on processing in the endoplasmic reticulum (ER) and involves multiple steps, including early association with the ER-resident chaperones calnexin/calreticulin and subsequent dimerization facilitated by lipase maturation factor 1 (LMF1) ( 19 - 23 ). (diabetesjournals.org)
  • 1992). "The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene. (chemeurope.com)
  • ATP and calcium ions are cofactors involved in substrate binding for calnexin. (wikipedia.org)
  • Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. (prospecbio.com)
  • ATP and Ca++ are two of the cofactors involved in substrate binding for calnexin. (chemeurope.com)
  • Calnexin is a calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. (genscript.com)
  • Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. (prospecbio.com)
  • Human Herpesvirus 8 Interleukin-6 Interacts with Calnexin Cycle Components and Promotes Protein Folding. (physiciansweekly.com)
  • Here, we show that calnexin, an endoplasmic reticulum integral membrane protein, interacts with the III-IV linker region of the Cav3. (readbyqxmd.com)
  • A prolonged association of calnexin with mutant misfolded PMP22 known to cause Charcot-Marie-Tooth Disease leads to the sequestration, degradation and inability of PMP22 to traffic to the Schwann cell surface for myelination. (wikipedia.org)
  • CNX1 and CNX2 do not appear to have a specific localisation or function at plasmodesmata-rather the association of calnexin with the ER is simply maintained as the ER passes through plasmodesmata. (edu.au)
  • The subcellular distribution of calnexin is mediated by PACS-2. (abcam.com)
  • Calnexin contains a large ER luminal domain (461 amino acids), a transmembrane segment (22 amino acids), and a cytoplasmic tail (89 amino acids). (genetex.com)
  • Using calnexin mutants lacking a luminal or cytoplasmic domain, we identified that the C-terminal cytoplasmic domain is responsible for Nef interaction. (ahajournals.org)
  • Calnexin binds only those N-glycoproteins that have GlcNAc2Man9Glc1 oligosaccharides. (wikipedia.org)
  • Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked glycoproteins in vivo. (nih.gov)
  • The function of calnexin is to retain unfolded or unassembled N-linked glycoproteins in the endoplasmic reticulum. (chemeurope.com)
  • Apart from its carbohydrate-dependent association with nascent glycoproteins ( 29 , 30 ), calnexin also associates with protein aggregates in a carbohydrate-independent manner ( 31 ). (jimmunol.org)
  • Using mass spectroscopy we identified calnexin as a protein that associates with both ABCA1 and Nef and provided evidence to show that in the presence of Nef, ABCA1-calnexin interaction is disrupted leading to ABCA1 retention in the ER, subsequent degradation and impairment of cholesterol efflux. (ahajournals.org)
  • Therefore, both TAP and calnexin may participate in the ER retention of peptide-deficient class I molecules. (rupress.org)
  • The folding sensor UGT1 adds back a terminal glucose to promote re-association of non-native polypeptides released from calnexin, thus prolonging their retention in the ER folding environment. (biologists.org)
  • immunogen = C-terminus peptide (A E E D E I L N R S P R N R K P R R E) of rat calnexin with an added cysteine, conj. (alzforum.org)
  • This report identifies interactions of vIL-6 and VKORC1v2 with calnexin cycle enzymes GlucII and UGGT1, which are involved in glycan processing and nascent protein folding. (physiciansweekly.com)
  • In conclusion, lysine residues at positions 4 and 7 on Nef were found to be indispensable for interacting with calnexin and inactivation of ABCA1. (ahajournals.org)
  • The monoglucosylated oligosaccharides that are recognized by calnexin result from the trimming of two glucose residues by the sequential action of two glucosidases, I and II. (chemeurope.com)
  • Access to the calnexin/calreticulin system requires removal of the two outermost glucose residues displayed on branch A of the N -glycan by the sequential action of glycanases GI and GII. (biologists.org)
  • After repeated rounds of calnexin binding, mutant PMP22 is modified by ubiquitin for degradation by the proteasome as well as a Golgi to ER retrieval pathway to return any misfolded PMP22 that escaped from the ER to the Golgi apparatus. (wikipedia.org)
  • Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. (prospecbio.com)
  • Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. (prospecbio.com)
  • The amino acid sequence of calnexin is highly conserved among species and is similar in sequence to calreticulin, another Ca 2 + -binding protein found in the ER. (fishersci.com)
  • WB: Use at a dilution of 1/2000 (this dilution was sufficient for detection of Calnexin in 20μg of HeLa heat shocked cell lysate). (genetex.com)
  • Calnexin is a 90kDa integral membrane protein located primarily in the ER. (fishersci.com)
  • Calnexin (CNX) is a 90kDa integral protein of the endoplasmic reticulum (ER). (chemeurope.com)
  • Calnexin founder gene in land plants was inherited from basal green algae during evolution in a very conservative copy number. (springer.com)
  • The calnexin gene was silenced using siRNA in HCT116 cells. (biomedcentral.com)
  • Calnexin gene-silencing significantly reduced cell survival and increased cancer cell susceptibility to 5FU chemotherapy. (biomedcentral.com)
  • 1994). "Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. (chemeurope.com)
  • Using structural models of Nef and calnexin, possible Nef-calnexin interaction models were built using docking servers. (ahajournals.org)
  • Effect of ionomycin on interaction of calnexin with vesicular stomatitis virus glycoprotein is cell type-specific. (researchmap.jp)
  • MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. (rupress.org)
  • Upon delivery of peptide to class I molecules in permeabilized cells, dissociation from TAP was observed but the interaction with calnexin was largely maintained. (rupress.org)
  • However, since release from calnexin occurs after dissociation from TAP, it appears that calnexin ultimately determines if a class I molecule is to be exported from the ER. (rupress.org)
  • GII-catalyzed removal of the third glucose residue follows the dissociation of folding substrates from calnexin and is required for release of native polypeptides from the ER and transport to their final destination. (biologists.org)
  • The x-ray crystal structure of calnexin revealed a globular lectin domain and a long hydrophobic arm extending out. (wikipedia.org)
  • These observations directly demonstrate that calnexin can act exclusively as a lectin. (nih.gov)
  • Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases. (prospecbio.com)
  • Synthetic peptide: EEDEILNRSPRNRKPRRE conjugated to KLH, corresponding to amino acids 575-593 of Human Calnexin. (genetex.com)
  • Immunohistochemistry analysis of human spleen tissue stained with Calnexin, pAb at 10µg/ml. (genetex.com)
  • Detection of human calnexin by immunoblotting. (merckmillipore.com)
  • Synthetic peptide within Human Calnexin aa 1-100. (abcam.co.jp)
  • Recognizes ~90-100kD band, corresponding to glycosylated human Calnexin. (biosave.com)
  • Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, which completely released the protein from calnexin. (nih.gov)
  • If the glycoprotein is not properly folded, an enzyme called UGGT (for UDP-glucose:glycoprotein glucosyltransferase) will add the glucose residue back onto the oligosaccharide thus regenerating the glycoprotein's ability to bind to calnexin. (wikipedia.org)
  • Both calnexin and the homologous ER-lumenal protein, calreticulin, bind calcium ions and participate in protein folding. (edu.au)
  • Once a glycoprotein is fully folded, it is no longer recognized by this enzyme, fails to bind calnexin, and can thus leave the ER ( 28 ). (jimmunol.org)
  • Calnexin has been reported to bind unassembled B cell receptor complexes ( 14 , 15 , 32 , 33 ). (jimmunol.org)
  • Objective To explore the temporal and spatial distribution of CCAAT/enhancer-binding protein homologous protein (CHOP) and calnexin (CNX) in the dentate gyrus of mesial temporal lobe epilepsy (mTLE) mouse model. (bvsalud.org)
  • Indeed, EBI3 failed to augment the IL-23Rα expression in the absence of endogenous calnexin. (jci.org)
  • As newly synthesized MHC class I α-chains enter the endoplasmic reticulum, calnexin binds on to them retaining them in a partly folded state. (wikipedia.org)
  • Cycles of de-/re-glucosylation might be protracted until the polypeptide released from calnexin fulfils quality control requirements. (biologists.org)
  • Sequential cleavage of the outermost α1,2-linked glucose residue by GI and of the first α1,3-linked glucose by GII generates the Glc 1 -Man 9 -GlcNAc 2 trimming intermediate that allows the polypeptide to associate with calnexin (and calreticulin) ( Fig. 2 , Step 1). (biologists.org)