Biotin
Carbon-Nitrogen Ligases
Biotinidase
Streptavidin
Avidin
Fatty Acid Synthase, Type II
The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.
Cell Membrane
Methylmalonyl-CoA Decarboxylase
Holocarboxylase Synthetase Deficiency
The neonatal form of MULTIPLE CARBOXYLASE DEFICIENCY that is caused by a defect or deficiency in holocarboxylase synthetase. HLCS is the enzyme that covalently links biotin to the biotin dependent carboxylases (propionyl-CoA-carboxylase, pyruvate carboxylase, and beta-methylcrotonyl-CoA carboxylase).
Protein Transport
Carboxyl and Carbamoyl Transferases
Carbon-Carbon Ligases
Acetyl-CoA Carboxylase
Epigenetic Repression
Amino Acid Sequence
Multiple Carboxylase Deficiency
A deficiency in the activities of biotin-dependent enzymes (propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, and PYRUVATE CARBOXYLASE) due to one of two defects in BIOTIN metabolism. The neonatal form is due to HOLOCARBOXYLASE SYNTHETASE DEFICIENCY. The late-onset form is due to BIOTINIDASE DEFICIENCY.
Molecular Sequence Data
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.
Carbonic Anhydrase I
Endocytosis
Membrane Proteins
Histones
Succinimides
Pyruvate Carboxylase
Symporters
Recombinant Fusion Proteins
Protein Binding
Biological Transport
HEK293 Cells
Repressor Proteins
Cell Polarity
Transfection
Glycosylation
Protein Processing, Post-Translational
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Protein Structure, Tertiary
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.
Microscopy, Confocal
Cricetinae
Blotting, Western
Dogs
Cells, Cultured
Immunoprecipitation
Staining and Labeling
Pyrococcus horikoshii
Mass Spectrometry
Glutamate Plasma Membrane Transport Proteins
A family of plasma membrane neurotransmitter transporter proteins that couple the uptake of GLUTAMATE with the import of SODIUM ions and PROTONS and the export of POTASSIUM ions. In the CENTRAL NERVOUS SYSTEM they regulate neurotransmission through synaptic reuptake of the excitatory neurotransmitter glutamate. Outside the central nervous system they function as signal mediators and regulators of glutamate metabolism.
Kidney Tubules, Collecting
CHO Cells
Membrane Transport Proteins
Carrier Proteins
Solute Carrier Family 12, Member 1
Epithelial Sodium Channels
Propionibacterium
A genus of gram-positive, rod-shaped bacteria whose cells occur singly, in pairs or short chains, in V or Y configurations, or in clumps resembling letters of the Chinese alphabet. Its organisms are found in cheese and dairy products as well as on human skin and can occasionally cause soft tissue infections.
Magnetospirillum
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Microscopy, Fluorescence
Mutation
Binding Sites
Epithelial Cells
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Carboxy-Lyases
Jurkat Cells
Mutagenesis, Site-Directed
Cystic Fibrosis Transmembrane Conductance Regulator
Opossums
Dopamine Plasma Membrane Transport Proteins
Kidney
Caco-2 Cells
Brefeldin A
Immunoblotting
Chromatography, Affinity
A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug resistance protein MdfA. (1/1806)
The nature of the broad substrate specificity phenomenon, as manifested by multidrug resistance proteins, is not yet understood. In the Escherichia coli multidrug transporter, MdfA, the hydrophobicity profile and PhoA fusion analysis have so far identified only one membrane-embedded charged amino acid residue (E26). In order to determine whether this negatively charged residue may play a role in multidrug recognition, we evaluated the expression and function of MdfA constructs mutated at this position. Replacing E26 with the positively charged residue lysine abolished the multidrug resistance activity against positively charged drugs, but retained chloramphenicol efflux and resistance. In contrast, when the negative charge was preserved in a mutant with aspartate instead of E26, chloramphenicol recognition and transport were drastically inhibited; however, the mutant exhibited almost wild-type multidrug resistance activity against lipophilic cations. These results suggest that although the negative charge at position 26 is not essential for active transport, it dictates the multidrug resistance character of MdfA. We show that such a negative charge is also found in other drug resistance transporters, and its possible significance regarding multidrug resistance is discussed. (+info)Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. (2/1806)
The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-dependent enzyme that catalyzes the first committed step of fatty acid biosynthesis. In its functional cycle, this protein engages in heterologous protein-protein interactions with three distinct partners, depending on its state of post-translational modification. Apo-BCCP interacts specifically with the biotin holoenzyme synthetase, BirA, which results in the post-translational attachment of biotin to a single lysine residue on BCCP. Holo-BCCP then interacts with the biotin carboxylase subunit of acetyl-CoA carboxylase, which leads to the addition of the carboxylate group of bicarbonate to biotin. Finally, the carboxy-biotinylated form of BCCP interacts with transcarboxylase in the transfer of the carboxylate to acetyl-CoA to form malonyl-CoA. The determinants of protein-protein interaction specificity in this system are unknown. The NMR solution structure of the unbiotinylated form of an 87 residue C-terminal domain fragment (residue 70-156) of BCCP (holoBCCP87) and the crystal structure of the biotinylated form of a C-terminal fragment (residue 77-156) of BCCP from Escherichia coli acetyl-CoA carboxylase have previously been determined. Comparative analysis of these structures provided evidence for small, localized conformational changes in the biotin-binding region upon biotinylation of the protein. These structural changes may be important for regulating specific protein-protein interactions. Since the dynamic properties of proteins are correlated with local structural environments, we have determined the relaxation parameters of the backbone 15N nuclear spins of holoBCCP87, and compared these with the data obtained for the apo protein. The results indicate that upon biotinylation, the inherent mobility of the biotin-binding region and the protruding thumb, with which the biotin group interacts in the holo protein, are significantly reduced. (+info)Streptavidin facilitates internalization and pulmonary targeting of an anti-endothelial cell antibody (platelet-endothelial cell adhesion molecule 1): a strategy for vascular immunotargeting of drugs. (3/1806)
Conjugation of drugs with antibodies to surface endothelial antigens is a potential strategy for drug delivery to endothelium. We studied antibodies to platelet-endothelial adhesion molecule 1 (PECAM-1, a stably expressed endothelial antigen) as carriers for vascular immunotargeting. Although 125I-labeled anti-PECAM bound to endothelial cells in culture, the antibody was poorly internalized by the cells and accumulated poorly after intravenous administration in mice and rats. However, conjugation of biotinylated anti-PECAM (b-anti-PECAM) with streptavidin (SA) markedly stimulated uptake and internalization of anti-PECAM by endothelial cells and by cells expressing PECAM. In addition, conjugation with streptavidin markedly stimulated uptake of 125I-labeled b-anti-PECAM in perfused rat lungs and in the lungs of intact animals after either intravenous or intraarterial injection. The antioxidant enzyme catalase conjugated with b-anti-PECAM/SA bound to endothelial cells in culture, entered the cells, escaped intracellular degradation, and protected the cells against H2O2-induced injury. Anti-PECAM/SA/125I-catalase accumulated in the lungs after intravenous injection or in the perfused rat lungs and protected these lungs against H2O2-induced injury. Thus, modification of a poor carrier antibody with biotin and SA provides an approach for facilitation of antibody-mediated drug targeting. Anti-PECAM/SA is a promising candidate for vascular immunotargeting of bioactive drugs. (+info)Molecular biology of biotin attachment to proteins. (4/1806)
Enzymatic attachment of biotin to proteins requires the interaction of a distinct domain of the acceptor protein (the "biotin domain") with the enzyme, biotin protein ligase, that catalyzes this essential and rare post-translational modification. Both biotin domains and biotin protein ligases are very strongly conserved throughout biology. This review concerns the protein structures and mechanisms involved in the covalent attachment of biotin to proteins. (+info)Human biotinidase isn't just for recycling biotin. (5/1806)
For years, the major role of biotin has been as the coenzyme for four carboxylases in humans. Although there has been evidence that biotin might have other functions, none has been firmly established. The discovery that human serum biotinidase has biotinyl-transferase activity, in addition to biotinidase hydrolase activity, presents new possibilities for the role of biotinidase in biotin metabolism. Specific transfer of biotin to histones by biotinidase provides a possible explanation for why biotin is found in the nucleus and the nature of its role in the regulation of protein transcription. Future studies will help to determine the functions of biotinidase in biotin metabolism and in disease states. (+info)Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion. (6/1806)
The effect of phosphatidyinositol-specific phospholipase C (PI-PLC) on mouse sperm-egg interaction was investigated in this study to determine if glycosyl-phosphatidylinositol (GPI)-anchored proteins are involved in mammalian fertilization. When both sperm and zona-intact oocytes were pretreated with a highly purified preparation of PI-PLC and coincubated, there was no significant effect on sperm-zona pellucida binding; however, fertilization was reduced from 59.6% (control group) to 2.8% (treatment group). A similar reduction in fertilization rates was found when zona-intact oocytes were treated with PI-PLC and washed prior to incubation with untreated sperm. The effect of PI-PLC on sperm binding and fusion with zona-free oocytes was then investigated. Treatment of sperm with PI-PLC had no significant effect on sperm-egg binding or fusion. However, treatment of eggs with PI-PLC significantly reduced sperm-egg binding and fusion from 6.2 bound and 2.1 fused sperm per egg in the control group to 2.1 bound and 0.02 fused sperm per egg in the treatment group. This decrease in sperm-egg binding and fusion depended on the dose of PI-PLC employed, with a maximal inhibitory effect on binding and fusion at 5 and 1 U/ml, respectively. PI-PLC-treated oocytes could be artificially activated by calcium ionophore, demonstrating that the oocytes were functionally viable following treatment. Furthermore, treatment of oocytes with PI-PLC did not reduce the immunoreactivity of the non-GPI-anchored egg surface integrin, alpha6beta1. Taken together, these observations support the hypothesis that PI-PLC affects fertilization by specifically releasing GPI-anchored proteins from the oolemma. In order to identify the oolemmal GPI-anchored proteins involved in fertilization, egg surface proteins were labeled with sulfo-NHS biotin, treated with PI-PLC, and analyzed by two-dimensional gel electrophoresis followed by avidin blotting. A prominent high-molecular-weight protein cluster (approximately 70 kDa, pI 5) and a lower molecular weight (approximately 35-45 kDa, pI 5.5) protein cluster were released from the oolemmal surface as a result of PI-PLC treatment. It is likely that these GPI-anchored egg surface proteins are required for sperm-egg binding and fusion. (+info)Critical relationship between glycosylation of recombinant lutropin receptor ectodomain and its secretion from baculovirus-infected insect cells. (7/1806)
The lutropin receptor ectodomain overexpressed under the control of the powerful polyhedrin promoter in baculovirus-infected Sf9 insect cells, is mainly found in an inactive, intracellularly-aggregated form. It is secreted in an active form under the control of the P10 promoter, a somewhat weaker and earlier promoter, at the price of a lower production. The apparent molecular masses of the two species encoded by the same cDNA are 48 kDa and 60-68 kDa, respectively. The relationship between the extent and type of glycosylation and the extracellular targeting for the recombinant lutropin receptor ectodomains was investigated precisely with endoglycosidases, lectins of various specificities, and a glycosylation inhibitor, and tested with monoclonal and polyclonal antibodies. The results indicate that the strong polyhedrin promoter probably overwhelms the processing capacity of the ER in Sf9 cells, so that only a high-mannose precursor is expressed in large amounts. Only a minute amount of protein is secreted, which has been processed by Sf9 exoglycosidases/glycosyltransferases and bears complex/hybrid oligosaccharides. The weaker P10 promoter allows secretion of a mature and active receptor ectodomain, bearing complex glycosylation. An important O-linked glycosylation is also added post-translationally on this species. In particular, beta-galactose and sialic acid residues were specifically detected in the secreted species, evidence of the induction of the corresponding glycosyltransferases or of their genes. These results suggest that Sf9 cells should eventually be engineered with chaperones and glycosyltransferases in order to improve the production of demanding glycoproteins such as the porcine lutropin ectodomain, so as to open the way to resolution of the three-dimensional structures of these receptors. (+info)Characterization of the internalization pathways for the cystic fibrosis transmembrane conductance regulator. (8/1806)
Mutations in the gene encoding the cystic fibrosis (CF) transmembrane conductance regulator (CFTR) chloride channel give rise to the most common lethal genetic disease of Caucasian populations, CF. Although the function of CFTR is primarily related to the regulation of apical membrane chloride permeability, biochemical, immunocytochemical, and functional studies indicate that CFTR is also present in endosomal and trans Golgi compartments. The molecular pathways by which CFTR is internalized into intracellular compartments are not fully understood. To define the pathways for CFTR internalization, we investigated the association of CFTR with two specialized domains of the plasma membrane, clathrin-coated pits and caveolae. Internalization of CFTR was monitored after cell surface biotinylation and quantitation of cell surface CFTR levels after elution of cell lysates from a monomeric avidin column. Cell surface levels of CFTR were determined after disruption of caveolae or clathrin-coated vesicle formation. Biochemical assays revealed that disrupting the formation of clathrin-coated vesicles inhibited the internalization of CFTR from the plasma membrane, resulting in a threefold increase in the steady-state levels of cell surface CFTR. In contrast, the levels of cell surface CFTR after disruption of caveolae were not different from those in control cells. In addition, although our studies show the presence of caveolin at the apical membrane domain of human airway epithelial cells, we were unable to detect CFTR in purified caveolae. These results suggest that CFTR is constitutively internalized from the apical plasma membrane via clathrin-coated pits and that CFTR is excluded from caveolae. (+info)
Carboxyl Biotinylation Reagents | Thermo Fisher Scientific
Biotinylation Reagents
citations
Use of In Vivo Biotinylation for Chromatin Immunoprecipitation - Current Protocols
Active Biotinylated Proteins - Protein Assay Formats: R&D Systems
Biotinylated Protein Kinase Product List | Protein Products | Products & Services | Carna Biosciences, Inc.
Biotinylated proteins | NUProtein Co., Ltd
Recombinant Human VEGF 165, Biotinylated Protein BT293-010: R&D Systems
One-Step Antibody Biotinylation Kit | Buffers and beads | Kits and support reagents | MACS Flow Cytometry | Products | Miltenyi...
One-Step Antibody Biotinylation Kit - Buffers and beads - Kits and support reagents - MACS Flow Cytometry - Products - Miltenyi...
Protein Biotinylation - Current Protocols
Protein Biotinylation - Current Protocols
Identification of stretch-induced biotinylation at cadherin junctions - UC Davis
Plus it
Brain Slice Biotinylation: An Ex Vivo Approach to Measure Region-specific Plasma Membrane Protein Trafficking in Adult Neurons ...
British Pound</strong>
US Dollar</strong>
Product Information Request - SuperSignal West Pico <u>COMPLETE</U> Biotinylated Protein Detection Kit from Pierce...
MicroRNA-135a regulates NHE9 to inhibit proliferation and migration of glioblastoma cells
Cardiac transcription factors in HL-1 cells: genome binding profiling | Stem Cell Commons
Sulfosuccinimidyl biotin (Sulfo-NHS-Biotin)
Signature Fragment Ions of Biotinylated Peptides<...
Miscellaneous Reagents - Biotin Labeling Reagents | Click Chemistry Tools
CCL2 promotes P2X4 receptor trafficking to the cell surface of microglia<...
Gentaur Molecular :MarkerGene \ MarkerGeneTM Biotin X Antibody Protein Labeling Kit, For efficient biotinylation of antibodies...
mouse on mouse antibodies
Peptide biotinylation
Transcend™ Non-Radioactive Translation Detection Systems
Detach cells and stop stimulation simultaneously- How? - Cell Biology
Plus it
Recombinant Human Fibronectin ED-B domain (C-Avi-His)(biotinylation) | Bon Opus Biosciences
LANCE Ultra Europium-anti-di-methyl-Histone H3 Lysine 36 (H3K36me2) Antibody, 10 µg | PerkinElmer
LANCE Ultra Europium-anti-methyl-Histone H4 Arginine 3 (H4R3me) Antibody, 100 µg | PerkinElmer
LANCE Ultra Europium-anti-methyl-Histone H3 Lysine 4 (H3K4me1-2), 10 µg | PerkinElmer
Anti-GST Tag, Biotinylated
Gentaur Molecular :Kamiya \ TLR9, biotinylated 5G5 \ MC-192
Custom Reagent Labeling - Alpha | PerkinElmer
Ultrasensitive immuno-detection using viral nanoparticles with modular assembly using genetically-directed biotinylation<...
Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme | Plant Physiology
Biotin - New World Encyclopedia
Best Chromatin IP antibody?(tag) - DNA Methylation, Histone and Chromatin Study
MHC multimer - Wikipedia
Biotinyl-S6 Phosphate Acceptor Peptide H-6098 | Bachem
Recombinant Human ERBB2, His-tagged, Biotinylated ERBB2-182H - Creative BioMart
Biotin protein ligase of is the 35. or that the presence | High-Throughput Screen for the Chemical Inhibitors
Metabolic biotinylation of the adenoviral capsid: Avidin-based applications and studies of ligand-targeted gene delivery
Biotin
BirA Biotin Ligase, MBP-tag, Recombinant - Amid Biosciences | Protein Engineering Company
BirA Biotin Ligase, MBP-tag, Recombinant | Amid Biosciences - Amid Biosciences | Protein Engineering Company
Peroxidase Streptavidin, R.T.U. (Ready-to-Use) | Vector Labs
RCSB PDB
for 1A6X
streptavidin streptavidin Gentaur Molecular Products
The Definitive Guide to biotin for weight loss
streptavidin recombinant streptavidin Gentaur Molecular Products
biotin-polyA-tailed DNA-capped citrate-stabilized gold nanoparticles-coated streptavidin-coated magnetic beads
LANCE Ultra Europium-anti-acetyl-p53 Lysine 382 (p53K382ac) Antibody, 10 µg | PerkinElmer
Plus it
RCSB PDB
for 4GJV
Recombinant Human ITGAV & ITGB6 Protein, His-Avi-tagged, Biotinylated ITGAV & ITGB6-760H - Creative BioMart
Plus it
Thermo Scientific™ Pierce™ Premium Grade Sulfo-NHS-LC-Biotin 1g Thermo Scientific™ Pierce™ Premium Grade Sulfo-NHS-LC-Biotin
Fluorophore Avidin/Streptavidin | Vector Labs
MojoSort Streptavidin Nanobeads
NRDC Gene - GeneCards | NRDC Protein | NRDC Antibody
HVEM Protein, Human, Recombinant (hFc & AVI Tag), Biotinylated | SinoBiological
DiagNano™ Streptavidin, QD 655 nm conjugate - Creative Diagnostics
More than Connections: Developing Village Clean Energy Plans | NRDC
TreeHuggerTV: NRDC Does Bonnaroo | TreeHugger
Biotinylation
NHS-coupling gives biotinylation of any primary amines in the protein). Enzymatic biotinylation results in biotinylation of a ... Chemical biotinylation utilises various conjugation chemistries to yield nonspecific biotinylation of amines, carboxylates, ... In contrast to chemical biotinylation methods, enzymatic biotinylation allows biotin to be linked at exactly one residue ... Photoactivatable biotinylation reagents can also be used to activate biotinylation at specific times in an experiment or during ...
ELISpot
Biotinylation basically creates a strong affinity between the biotin on the cytokine-specific antibody and the streptavidin on ... "Biotinylation". ThermoFisher Scientific. Retrieved 6 December 2018. "BCIP/NBT-plus SDS Summary" (PDF). MABTECH. Retrieved 6 ...
Chemical biology
Fouda AE, Pflum MK (August 2015). "A Cell-Permeable ATP Analogue for Kinase-Catalyzed Biotinylation". Angewandte Chemie. 54 (33 ... Senevirathne C, Embogama DM, Anthony TA, Fouda AE, Pflum MK (January 2016). "The generality of kinase-catalyzed biotinylation ...
Protein folding
Minde DP, Ramakrishna M, Lilley KS (2018). "Biotinylation by proximity labelling favours unfolded proteins". bioRxiv. doi: ...
Citrullination
Citrulline residues can be chemically modified with butanedione or by biotinylation prior to analysis, leading to a different ... Tutturen, Astrid E. V.; Holm, Anders; Fleckenstein, Burkhard (2013-11-01). "Specific biotinylation and sensitive enrichment of ...
Proximity labeling
"Biotinylation by antibody recognition - A method for proximity labeling". Nature Methods. 15 (2): 127-133. doi:10.1038/nmeth. ... "β-Actin mRNA interactome mapping by proximity biotinylation". Proceedings of the National Academy of Sciences. 116 (26): 12863- ...
Holocarboxylase synthetase
Biotinylation Siegel L, Foote JL, Coon MJ (March 1965). "The enzymatic synthesis of propionyl coenzyme A holocarboxylase from d ...
Luciferase
... can act as an ATP sensor protein through biotinylation. Biotinylation will immobilize luciferase on the cell-surface ...
Chromatin immunoprecipitation
2004). "Use of protein biotinylation in vivo for chromatin immunoprecipitation". Analytical Biochemistry. 325 (1): 68-76. doi: ... or in vivo biotinylation can be used instead of antibodies to the native protein of interest. The DNA associated with the ...
Cofactor transferase family
Chapman-Smith A, Cronan JE (September 1999). "The enzymatic biotinylation of proteins: a post-translational modification of ...
Holoprotein
Chapman-Smith A, Cronan JE (1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional ...
Enzyme
ISBN 978-1-118-91840-1. Chapman-Smith A, Cronan JE (September 1999). "The enzymatic biotinylation of proteins: a post- ...
Bioconjugation
Immunofluorescence Biomolecular engineering Biotinylation SpyTag/SpyCatcher Unnatural amino acids Bioconjugate Chemistry ...
Immunostaining
Protein biotinylation in vivo was proposed to alleviate the problems caused by frequent incompatibility of antibody staining ... Viens, A.; Harper, F.; Pichard, E.; Comisso, M.; Pierron, G.; Ogryzko, V. (2008). "Use of Protein Biotinylation in Vivo for ...
Avidin
Streptavidin Biotinylation Helppolainen SH, Nurminen KP, Määttä JA, Halling KK, Slotte JP, Huhtala T, et al. (August 2007). " ...
Biotin
Biotinylation of histone proteins in nuclear chromatin plays a role in chromatin stability and gene expression. The US National ... Biotinylation of histone proteins in nuclear chromatin is a posttranslational modification that plays a role in chromatin ... Biotin deficiency Biotin sulfoxide Biotinidase deficiency Biotinylation Multiple carboxylase deficiency NeutrAvidin Photobiotin ... the chemically modified biotin reagents are bound to the targeted compounds in a solution via a process called biotinylation. ...
Adhesome
The advent of proximity biotinylation by birA* has facilitated the first proteomics-based studies of the cadherin adhesome. ...
Nanopore sequencing
One idea is to attach the exonuclease to the nanopore, perhaps through biotinylation to the beta barrel hemolysin. The central ...
Magnetoelastic filaments
... biotinylation or glucose decomposition. Typically, the primary building blocks of these nanostructures are individual ...
Post-translational modification
biotinylation: covalent attachment of a biotin moiety using a biotinylation reagent, typically for the purpose of labeling a ...
Terminal amine isotopic labeling of substrates
Subtiligase biotinylation of N-termini uses enzymatic labeling of N-terminal peptides, but does not use lysine blocking ... Lysine guanidination followed by biotinylation of N-termini uses a chemical to block lysine residues and tag free N-termini. ... Acetylation of amines followed by tryptic digestion and biotinylation of free N-terminal peptides uses chemical (acetylation) ...
Olfactomedin 4
"Identification of new accessible tumor antigens in human colon cancer by ex vivo protein biotinylation and comparative mass ...
Chem-seq
Limitations For Chem-seq to be feasible, the small molecule under study must be amenable to biotinylation without disruption of ...
Photobiotin
Biotinylation of DNA and RNA with photoactivatable biotin is easier and less expensive than enzymatic methods since the DNA and ...
Dideoxynucleotide
The dye nucleotide to be used will likely occur by treatment with a phosphorylation enzyme and biotinylation and reaction of ...
Mir-153 microRNA precursor family
... thereby increasing the abundance of histone H4 biotinylation marks in HEK-293 human kidney cells". The Journal of Nutritional ...
Protein tag
The tag is recognized by a repertoire of single-domain antibodies AviTag, a peptide allowing biotinylation by the enzyme BirA ... such as biotinylation by biotin ligase) or chemical modification (such as coupling to other proteins through SpyCatcher or ...
List of MeSH codes (E05)
... biotinylation MeSH E05.393.525.100 - blotting, northern MeSH E05.393.525.150 - blotting, southern MeSH E05.393.525.225 - ...
Eastern blot
... biotinylation, formylation, geranylgeranylation, glutamylation, glycosylation, glycylation, hydroxylation, isoprenylation, ...
Alice Y. Ting
In addition, Ting and her lab developed monovalent streptavidin, site-specific biotinylation in mammalian cells, small ...
antibody biotinylation kit
In vivo identification of GTPase interactors by mitochondrial relocalization and proximity biotinylation - preLights
Identification of BPIFA1/SPLUNC1 as an epithelium-derived smooth muscle relaxing factor | Nature Communications
Surface biotinylation. Human ASMCs were treated with or without BPIFA1 for 4 h. Cells were then washed with prechilled PBS++ ( ... 4c). Surface biotinylation/immunoblot and confocal microscopy demonstrated that plasma membrane Orai1 levels decreased by ∼50% ... d) Human ASMCs were incubated with 10 μM BPIFA1 for 4 h, followed by surface biotinylation and immunoblot using indicated ...
What is Biotinylation? | Biopharma PEG
Biotinylation, also known as biotin labeling, is the process of covalently attaching biotin to proteins, nucleic acids, or ... What is Biotinylation?. Release date:2020/6/4 11:07:10. Biotinylation, also known as biotin labeling, is the process of ... Biotinylation is fast, specific, and due to the small size of biotin (MW=244.31 g/mol), it is unlikely to interfere with the ... There are many biotinylation reagents that can utilize a variety of possible labeling methods. Due to the strong affinity ...
IJMS | Free Full-Text | Functional Consequences of the SCN5A-p.Y1977N Mutation within the PY Ubiquitylation Motif: Discrepancy...
4.2.5. Cell Surface Biotinylation Assay. HEK293 cells were transiently transfected with SCN5A WT or YN cDNAs 48 h prior to ... Using cell surface biotinylation assays, we next investigated cell surface expression of WT and YN Nav1.5 in the presence and ... Following cell surface biotinylation, HEK293 cells were washed three times with cold Glycine solution 200 mM in PBS, plus once ... Western blot of a representative cell surface biotinylation assay in HEK293 cells transiently expressing Nav1.5 WT or YN with ...
MAGICLINK™ Site Specific Biotinylation Kit (1x1 mg) | BroadPharm
Biotinylation reagents Dye Antibody Labeling Kit Biotin Antibody Labeling Kit Protein Crosslinking Kit Enzyme, Antibody, ... With site specific biotinylation chemistry, biotin linkers are inserted to thiol-bridge locations and do not affect antibody- ... MagicLink™ Site Specific Biotinylation Kits provide optimized reagents for biotinylating antibodies. Biotin is a small, ... MAGICLINK™ Site Specific Biotinylation Kit (1x1 mg). div.hero { background-image: url(/web/images/home-slides/bg.webp); ...
Frontiers | SUMOylation of the Kv4.2 Ternary Complex Increases Surface Expression and Current Amplitude by Reducing...
Biotinylation of Cell Surface Proteins. NeutrAvidin resin (300 μL) (Thermo Fisher cat no. 29201) was placed in a Pierce Snap ... Immediately following biotinylation on ice, cells on this plate were treated with MESNA to remove all biotin from surface ... Immediately following biotinylation on ice, cells on this plate were lysed and biotinylated proteins were isolated using ... To do this, we performed cell surface biotinylation assays on HEK cells expressing the TC components with or without co- ...
Biotin | Linus Pauling Institute | Oregon State University
Contents Summary Function Biotinylation Deficiency Signs and symptoms Risk factors Inborn metabolic disorders Markers of status ... Several sites of biotinylation have been identified in histones H2A, H3, and H4 (5). Amongst them, histone H4 biotinylation at ... Biotinylation. Biotin functions as a covalently bound cofactor required for the biological activity of the five known mammalian ... In addition, biotinylation marks co-localize with well-known gene repression marks like methylated lysine 9 in histone H3 ( ...
Phospholipid biotinylation of polydimethylsiloxane (PDMS) for protein immobilization. | Lab Chip;6(3): 369-73, 2006 Mar. |...
Dominant negative mutation in oxalate transporter SLC26A6 associated with enteric hyperoxaluria and nephrolithiasis | Journal...
Arterial smooth muscle cell PKD2 (TRPP1) channels regulate systemic blood pressure | eLife
Arterial biotinylation. Request a detailed protocol Procedures used were similar to those previously described (Tsiokas et al ... using arterial biotinylation we show that ~85% of PKD2 protein is located in the plasma membrane in both mesenteric and ... Arterial biotinylation revealed that surface PKD2 protein in mesenteric and hindlimb arteries of hypertensive mice were also ~ ...
Amine Biotinylation Reagents and Kits(胺生物素化试剂和试剂盒)
Reviews and Minireviews
Proximity-dependent biotinylation approaches such as BioID and APEX overcome classical limitations of biochemical purification ... Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches. Molecular & Cellular Proteomics ... and discuss current and emerging applications of these enzymes for proximity dependent biotinylation. We provide guidelines for ... enzyme selection and experimental design for performing and interpreting proximity-dependent biotinylation experiments. ...
Plus it
Biotinylation. Biotinylation experiments were performed essentially as described (Qian et al., 1997; Davis et al., 1998). ... The biotinylation solution was removed by three washes in PBS/Ca/Mg plus 100 mm glycine and quenched in this solution by ... GABA uptake and biotinylation assays for mGAT1-GFP partitioning. A, Scatchard plot of [3H]GABA uptake for all three mGAT1-GFP ... Surface biotinylation defined the fraction of transporters on the surface versus those in the nearby cytoplasm. The data show ...
Biotinylation as a Way of Modulating the Structure and Function of Arc1p(1/3)
- National Central University
Biotinylation as a Way of Modulating the Structure and Function of Arc1p(1/3). *王, 健家 (PI) ... Biotinylation of Arc1p is highly specific and occurs only at K86 within the SSKD motif of its N domain. This covalent ... The proposal presented herein elaborates a three-year project, in which we aim to study the effect of biotinylation on Arc1p5s ... Specific aims include (1) elucidating the effect of biotinylation on Arc1p5s structural and function, and (2) delineating the ...
Synthesis and biological evaluation of biotin conjugates of (±)-(4bS,8aR,10aS)-10a-ethynyl-4b,8,8-trimethyl-3,7-dioxo-3,4b,7,8...
Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2<...
Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2. ... Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2. ... Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2. ... T1 - Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for ...
SUSD5 sushi domain containing 5 [Homo sapiens (human)] - Gene - NCBI
Buffers and beads | MACS® Flow Cytometry Kits and support reagents | 中国
Custom Peptide Synthesis
BTD gene: MedlinePlus Genetics
Recombinant Rat Ccl19 protein, His-tagged Ccl19-723R - Creative BioMart
Piotr ZIOLKOWSKI | Associate Professor | PhD | Adam Mickiewicz University, Poznań | UAM | Laboratory of Genome Biology, http:/...
Efficacy of Affibody-Based Ultrasound Molecular Imaging of Vascular B7-H3 for Breast Cancer Detection | Clinical Cancer...
Biotinylated Human Neuropilin-1 / NRP1 / CD304 Protein, His, Avitag™ | NR1-H82E3
Ralph Weissleder, MD, PhD - DF/HCC
NT5DC1 Mouse Monoclonal Antibody [Clone ID: OTI1E11] - CF501589 | OriGene
Development of a sensitive trial-ready poly(GP) CSF biomarker assay for C9orf72-associated frontotemporal dementia and...
Biotin7
- Biotinylation , also known as biotin labeling , is the process of covalently attaching biotin to proteins, nucleic acids, or other molecules. (biochempeg.com)
- Biotinylation is fast, specific, and due to the small size of biotin (MW=244.31 g/mol), it is unlikely to interfere with the natural function of the molecule. (biochempeg.com)
- It requires that the biotinylation reagent be hydrophilic to prevent it from passing through the hydrophobic cell membrane, thereby limiting the biotin labeling to the cell surface. (biochempeg.com)
- With site specific biotinylation chemistry, biotin linkers are inserted to thiol-bridge locations and do not affect antibody-antigen binding (Fig.1). (broadpharm.com)
- The term "biotinylation" refers to the covalent addition of biotin to any molecules, including apocarboxylases and histones. (oregonstate.edu)
- Because of the charged sulfonate group, these compounds do not penetrate the plasma membrane , thus sulfo-NHS-esters of biotin are recommended for use as cell surface biotinylation reagents. (glpbio.cn)
- It might also have the ability to attach biotin to certain proteins through a process called biotinylation. (medlineplus.gov)
Reagents6
- There are many biotinylation reagents that can utilize a variety of possible labeling methods. (biochempeg.com)
- The spacer arms composed of PEG can make the biotinylation reagents with uncharged reactive groups soluble, or the biotinylated reagents with charged reactive groups more soluble. (biochempeg.com)
- Biochempeg provides advanced biotinylation reagents, PEG-Biotins for improved biostability and bioavailability, hydrazine chemistry and click chemistry biotins, UV-traceable biotins. (biochempeg.com)
- MagicLink™ Site Specific Biotinylation Kits provide optimized reagents for biotinylating antibodies. (broadpharm.com)
- Amine-reactive biotinylation reagents can be divided into two groups based on water solubility: NHS-esters and sulfo-NHS-esters. (glpbio.cn)
- Generate reliable hapten labelled probes with our biotinylation and DNP reagents. (biosearchtech.com)
Protein7
- Proteins have hydrophobic and hydrophilic regions based on amino acid side chains and protein conformation, and these regions can promote or limit biotinylation based on the solubility of the reagent. (biochempeg.com)
- In addition, based on the solubility of the reagent, the hydrophobicity of the target protein microenvironment can prevent or allow biotinylation. (biochempeg.com)
- Therefore, the choice of the appropriate biotinylation reagent depends on the target amino acid and the microenvironment of the protein or macromolecule. (biochempeg.com)
- Phospholipid biotinylation of polydimethylsiloxane (PDMS) for protein immobilization. (bvsalud.org)
- A Surface Biotinylation Strategy for Reproducible Plasma Membrane Protein Purification and Tracking of Genetic and Drug-Induced Alterations. (mpg.de)
- To address this problem an in vivo proximity capturing workflow was developed, consisting of proximity biotinylation followed by protein cross-linking (XL-BioID). (biorxiv.org)
- Biotinylation as well mainly because prior purification of detection antibodies were carried out using biotinylation and protein A/G purification packages according to manufacturers Gemcitabine HCl inhibitor database recommendations (Pierce Biotechnology, Rockford, IL, USA). (ecologicalsgardens.com)
Proteins2
- Following biotinylation, proteins are isolated by streptavidin affinity capture and analysed by mass spectrometry. (biologists.com)
- Within the nucleus, biotinylation of DNA-associated proteins called histones may help determine whether certain genes are turned on or off. (medlineplus.gov)
Reactive1
- The solubility of the biotinylation reagent is based on the solubility of the reactive moiety, the spacer arm, or a combination of both. (biochempeg.com)
Proximity2
- A proximity-dependent biotinylation map of a human cell. (nih.gov)
- Biotinylation by antibody recognition-a method for proximity labeling. (ndriresource.org)
Reaction1
- One reaction corresponds to biotinylation of 10 µg pure antibody. (miltenyibiotec.com)
Substrates1
- We present here an in vitro method that combines biotinylation and mass spectrometry (MS) to identify substrates deacetylated by sirtuins. (nyu.edu)
Amino1
- HCS catalyzes the post-translational biotinylation of the epsilon amino group of a lysine residue at the active site of each apocarboxylase, converting the inactive apocarboxylase into a fully active holocarboxylase ( Figure 1a ). (oregonstate.edu)
Cell1
- Proteomic analysis of the lymphocyte plasma membrane using cell surface biotinylation and solution-phase isoelectric focusing. (ox.ac.uk)
Immobilization1
- Fibronectin was prepared for immobilization by undergoing buffer exchange and biotinylation with the Pierce biotinylation kit (2). (biopharminternational.com)
Method1
- For example, surface biotinylation is a common method for studying the expression or endosomal trafficking of surface molecules. (biochempeg.com)
Function2
- The proposal presented herein elaborates a three-year project, in which we aim to study the effect of biotinylation on Arc1p5s structure and function in particular and the biological significance of this type of post-translational modification in general. (ncu.edu.tw)
- Specific aims include (1) elucidating the effect of biotinylation on Arc1p5s structural and function, and (2) delineating the mechanism of Arc1p biotinylation by Bpl1p. (ncu.edu.tw)
Specific1
- Biotinylation of Arc1p is highly specific and occurs only at K86 within the SSKD motif of its N domain. (ncu.edu.tw)