TY - JOUR. T1 - Human recombinant tissue transglutaminase ELISA. T2 - An innovative diagnostic assay for celiac disease. AU - Sblattero, D.. AU - Berti, I.. AU - Trevisiol, C.. AU - Marzari, R.. AU - Tommasini, A.. AU - Bradbury, A.. AU - Fasano, A.. AU - Ventura, A.. AU - Not, T.. PY - 2000/5. Y1 - 2000/5. N2 - OBJECTIVE: Tissue transglutaminase is the autoantigen recognized by the sera of celiac patients. An enzyme-linked immunosorbent assay (ELISA) based on guinea-pig tissue transglutaminase was recently used to measure serum tissue transglutaminase antibodies for the diagnosis of celiac disease. We determine the sensitivity and specificity of an ELISA test based on the use of human recombinant transglutaminase, compared with the guinea pig transglutaminase ELISA and IgA antiendomysium antibodies. METHODS: Serum samples were tested from 65 patients with intestinal biopsy proven celiac disease, from 10 patients with Crohns disease, and from 150 healthy blood donors. RESULTS: Human ...
TY - JOUR. T1 - Autoregulation of SafA assembly through recruitment of a protein cross-linking enzyme. AU - Fernandes, Catarina G.. AU - Moran, Charles P.. AU - Henriques, Adriano O.. PY - 2018/7/1. Y1 - 2018/7/1. N2 - The coat of Bacillus subtilis spores is a multiprotein protective structure that also arbitrates many of the environmental interactions of the spore. The coat assembles around the cortex peptidoglycan layer and is differentiated into an inner and an outer layer and a crust. SafA governs assembly of the inner coat, whereas CotE drives outer coat assembly. SafA localizes to the cortex-coat interface. Both SafA and its short form C30 are substrates for Tgl, a coat-associated transglutaminase that cross-links proteins through ε-(γ-glutamyl)lysyl isopeptide bonds. We show that SafA and C30 are distributed between the coat and cortex layers. The deletion of tgl increases the extractability of SafA, mainly from the cortex. Tgl itself is mostly located in the inner coat and cortex. The ...
Tissue transglutaminase (tTG) and microbial transglutaminase (mTG) cross-link gliadins to form complexes that expose immunogenic neo-epitopes to produce tTG and mTG-neo-epitope antibodies. The aim of this study was to test the diagnostic performance of antibodies against non-complexed and complexed forms of transglutaminases, to correlate their activities to the intestinal damage and to explore age group dependency in celiac disease (CD). A total of 296 children with untreated CD and 215 non-celiac disease controls were checked by in-house enzyme-linked immunosorbent assays detecting immunoglobulin (Ig)A, IgG or combined detection of IgA and IgG (check) against tTG, AESKULISA® tTG New Generation (tTG-neo) and mTG-neo (RUO), IgA and IgG antibodies against deamidated gliadin peptide (DGP) and human IgA anti-endomysium antibodies (EMA) using AESKUSLIDES® EMA. Intestinal pathology was graded according the revised Marsh criteria, and age dependencies of the antibody activities were analysed. Using ...
Rabbit anti tissue transglutaminase antibody recognizes tissue transglutaminase, also known as protein-glutamine gamma-glutamyltransferase
Objectives: To determine (i) the prevalence of positive results of anti-tissue transglutaminase (anti-tTG) antibody assays and coeliac disease (CD) in a rural Australian community; and (ii) whether confirmatory testing of a positive assay result with an alternative anti-tTG assay improved the positive predictive value of the test in population screening for CD.. Design: Retrospective analysis in December 2004 of stored serum samples taken in 1994-1995 from 3011 subjects in the Busselton Health Study follow-up. Assays for IgA and IgG anti-tTG antibodies were performed, and positive or equivocal samples were retested with a different commercial anti-tTG assay. Available subjects with one or more positive assay results were interviewed, had serum collected for repeat anti-tTG assays and for HLA-DQ2 and HLA-DQ8 haplotyping and, if appropriate, gastroscopy and duodenal biopsy were performed. In unavailable subjects, HLA-DQ2 and -DQ8 haplotyping was performed on stored sera. Total serum IgA levels ...
Bacterial transglutaminases are increasingly required as industrial reagents for in vitro modification of proteins in different fields such as in food processing as well as for enzymatic site-specific covalent conjugation of therapeutic proteins to polyethylene glycol to get derivatives with improved clinical performances. In this work we studied the production in Escherichia coli of a recombinant transglutaminase from Streptomyces mobaraensis (microbial transglutaminase or MTGase) as enzymatically active chimeric forms using different expression systems under the control of both lac promoter or thermoinducible phage lambda promoter. Thermoinducible and constitutive expression vectors were constructed expressing Met-MTGase with chimeric LacZ1-8PNP1-20 or LacZ1-8 fusion protein under different promoters. After transformed in competent Escherichia coli K12 strains were fermented in batch and fed-bach mode in different mediums in order to select the best conditions of expression. The two most performing
To improve the fermentation production of transglutaminase (TGase) from Streptomyces mobaraensis for applications in the food industry, the atmospheric and room-temperature plasma (ARTP) mutagenesis was applied to breed S. mobaraensis mutants with increased TGase production. After eight rounds of iterative ARTP mutagenesis, four genetically stable mutants, Sm5-V1, Sm6-V13, Sm2-V10, and Sm7-V12, were identified, which showed increased TGase production by 27, 24, 24, and 19%, respectively. The best mutant Sm5-V1 exhibited a maximum TGase activity of 5.85 U/mL during flask fermentation. Compared to the wild-type strain, the transcription levels of the zymogen TGase genes in the mutants increased significantly as indicated by quantitative real-time PCR, while the gene nucleotide sequences of the mutants did not change at all. It was shown that the overexpression of TGase zymogen gene in the mutants contributes to the increase in TGase production. ARTP is a potentially efficient tool for microbial mutation
Human type II transglutaminase (TG2) is an enzyme that exists in two dramatically different conformational states, each with a unique activity. In the open, extended form, the transglutaminase active site is exposed, allowing TG2 to catalyze formation of an isopeptide bond between the sidechain of a peptide-bound glutamine and a primary amine. Upon GTP binding to a separate GTPase active site, TG2 adopts a heavily favored and compact closed conformation, which obstructs the glutaminase active site, and only allows GTPase activity. TG2 has been linked to Huntingtons disease, as well as to many other cellular processes, both physiological and pathological. However, TG2s two conformational states, each with its own activity, have made it difficult to elucidate how this enzyme functions in disease progression. In addition, because TG2 heavily prefers the closed state, attempts to screen for inhibitors that may bind the transglutanimase site exposed in the open conformation, and attempts to obtain ...
A transglutaminase is an enzyme that catalyzes the formation of an isopeptide bond between a free amine group (e.g., protein- or peptide-bound lysine) and the acyl group at the end of the side chain of protein- or peptide-bound glutamine. The reaction also produces a molecule of ammonia. Such an enzyme is classified as EC 2.3.2.13. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). Transglutaminases were first described in 1959. The exact biochemical activity of transglutaminases was discovered in blood coagulation protein factor XIII in 1968. Eight transglutaminases have been characterised. Transglutaminases form extensively cross-linked, generally insoluble protein polymers. These biological polymers are indispensable for an organism to create barriers and stable structures. Examples are blood clots (coagulation factor XIII), as well as skin and hair. The catalytic reaction is generally viewed as being irreversible, and must be closely monitored ...
1KV3: Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity.
1KV3: Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity.
The present invention relates to use of a transglutaminase in the preparation of a medicament for inhibiting angiogenesis. Preferably, the transglutaminase is a human tissue transglutaminase. Advantageously, the medicament is for treating cancer, rheumatoid arthritis, retinopathy and/or psoriasis. Additionally, the invention relates to compositions comprising a transglutaminase in an amount sufficient to inhibit angiogenesis.
For the Tetris game, see Tetris: The Grand Master. Protein-glutamine gamma-glutamyltransferase E is an enzyme that in humans is encoded by the TGM3 gene. Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle. Proximal promoter GRCh38: Ensembl release 89: ENSG00000125780 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000027401 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Wang M, Kim IG, Steinert PM, McBride OW (Mar 1995). "Assignment of the human transglutaminase 2 (TGM2) and ...
Recombinant Transglutaminase 3 (E Polypeptide, Protein-Glutamine-gamma-Glutamyltransferase) (TGM3) Protein. Species: Human. Order product ABIN1047977.
Using immunogold-silver techniques, we have demonstrated that, in rats, type-I (keratinocyte) transglutaminase is expressed primarily in stratified squamous epithelia of the integument, the upper digestive tract, and the lower female genital tract. PMID: 2436965 ...
A 2009 issue of The Journal of Immunology (Novel Role of Tissue Transglutaminase (TG2) in Chronic Inflammatory Diseases) had something to say about this. Transglutaminases are enzymes that allow us to break down wheat protein, otherwise known as Gluten. In people with Celiac Disease (not to mention numerous people who do not have Celiac Disease --- HERE), the body makes anti-Transglutaminase antibodies. In other words, not only is the body attacking Gluten as though it were a foreign invader (HERE), its attacking the enzyme that helps break down Gluten as well. The study mentioned at the top of the page revealed that, "Tissue transglutaminase (TG2) has a critical role in the pathogenesis of chronic inflammatory diseases." Not that I have time to get into it today, but Gluten is arguably the single biggest factor in developing AUTOIMMUNE DISEASES (HERE is a list of A.I. diseases). And how about this for a "fun fact"? The "Modern Pantry" website sells Transglutaminase for kitchen use. Listen to ...
Vascular aging is marked by an increase in vascular stiffness. Tissue-type transglutaminase (tTG) enzymatically forms crosslinks between extracellular matrix proteins and may contribute to this pathobiology. Recently, it has been demonstrated that s-nitrosylation of cysteine residues within the enzyme leads to its inhibition. We hypothesize that tTG is more active in the aging vasculature due to decreased bioavailability of nitric oxide (NO) and impaired S-nitrosylation. tTG activity in aorta measured by the incorporation of biotin labeled pentylamine, a tTG substrate, into crosslinks was markedly increased in old (O) animals compared to young (Y) (3.2 fold increase, n = 6, p = 0.0018). S-nitrosylation of tTG, as determined by the biotin switch assay, was significantly reduced in O vs. Y rat aorta. tTG specific (ϵ-(γ-glutamyl)lysine) crosslinks measured by immunofluorescent staining was significantly increased in O vs Y rat aortic rings. Denitrosylation of tTG in Y rats with DTT increased tTG ...
TY - JOUR. T1 - Retinoic acid-induced tissue transglutaminase and apoptosis in vascular smooth muscle cells. AU - Ou, Hesheng. AU - Haendeler, Judith. AU - Aebly, Michael R.. AU - Kelly, Louise A.. AU - Cholewa, Brian C.. AU - Koike, George. AU - Kwitek-Black, Anne. AU - Jacob, Howard J.. AU - Berk, Bradford C.. AU - Miano, Joseph M.. PY - 2000/11/10. Y1 - 2000/11/10. N2 - Retinoids exert antiproliferative and prodifferentiating effects in vascular smooth muscle cells (SMCs) and reduce neointimal mass in balloon-injured blood vessels. The mechanisms through which retinoids carry out these effects are unknown but likely involve retinoid receptor-mediated changes in gene expression. Here we report the cloning, chromosomal mapping, and biological activity of the retinoid-response gene rat tissue transglutaminase (tTG). Northern blotting studies showed that tTG is rapidly and dose-dependently induced in a protein synthesis-independent manner after stimulation with the natural retinoid all-trans ...
TY - JOUR. T1 - Tissue transglutaminase and the progression of human renal scarring. AU - Johnson, Timothy S.. AU - El-Koraie, Ahmed F.. AU - Skill, N.. AU - Baddour, Nahed M.. AU - El Nahas, A. Meguid. AU - Njloma, Melvin. AU - Adam, Ahmed G.. AU - Griffin, Martin. PY - 2003/8/1. Y1 - 2003/8/1. N2 - Experimental renal scarring indicates that tissue transglutaminase (tTg) may be associated with the accumulation of extracellular matrix (ECM), both indirectly via TGF-β1 activation and directly by the formation of ε(γ-glutamyl) lysine dipeptide bonds within the ECM. The latter potentially accelerates deposition and confers the ECM with resistance to proteolytic digestion. Studied were 136 human renal biopsy samples from a range of chronic renal diseases (CRD) to determine changes in tTg and ε(γ-glutamyl) lysine crosslinking. Immunofluorescence for insoluble tTg showed a 14-fold increase in the kidneys of CRD patients (5.3 ± 0.5 versus 76 ± 54 mV/cm2), which was shown to be active by a ...
Tissue transglutaminase (tTG) belongs to the family of transglutaminase enzymes that catalyze the posttranslational modification of proteins via Ca(2+)-dependent cross-linking reactions. The catalytic action of tTG results in the formation of an isopeptide bond that is of great physiological significance since it is highly resistant to proteolysis and denaturants. Although tTG-mediated cross-linking reactions have been implicated to play a role in diverse biological processes, the precise physiological function of the enzyme remains unclear. Recent data, however, suggest that the protein polymers resulting from tTG-catalyzed reactions may play a role in commitment of cells to undergo apoptosis. On the same token, tTG-mediated formation of insoluble protein aggregates may underlie the markers of numerous pathological conditions, such as the senile plaques in Alzheimers disease and the Lewy bodies in Parkinsons disease. In addition to catalyzing Ca(2+)-dependent cross-linking reactions, tTG can also
Today, we know that we are talking about a family of nine different isoenzymes in the human body. Although transglutaminases have one basic common feature - the formation of high molecular weight aggregates by covalent protein cross-linking - they fulfill a plentitude of other catalytic and physiological functions ...
A hitherto unknown function for transglutaminase (TGase; R-glutaminyl-peptide: amine gamma-glutamyltransferase, EC 2.3.2.13) was found in the conversion of latent transforming growth factor-beta (LTGF-beta) to active TGF-beta by bovine aortic endothelial cells (BAECs). The cell-associated, plasmin-mediated activation of LTGF-beta to TGF-beta induced either by treatment of BAECs with retinoids or by cocultures of BAECs and bovine smooth muscle cells (BSMCs) was blocked by seven different inhibitors of TGase as well as a neutralizing antibody to bovine endothelial cell type II TGase. Control experiments indicated that TGase inhibitors and/or a neutralizing antibody to TGase did not interfere with the direct action of TGF-beta, the release of LTGF-beta from cells, or the activation of LTGF-beta by plasmin or by transient acidification. After treatment with retinoids, BAECs expressed increased levels of TGase coordinate with the generation of TGF-beta, whereas BSMCs and bovine embryonic skin ...
The CPT codes provided are based on AMA guidelines and are for informational purposes only. CPT coding is the sole responsibility of the billing party. Please direct any questions regarding coding to the payer being billed ...
TY - JOUR. T1 - Inactive and highly active, proteolytically processed transglutaminase-5 in epithelial cells. AU - Pietroni, Valentina. AU - Di Giorgi, Sabrina. AU - Paradisi, Andrea. AU - Ahvazi, Bijan. AU - Candi, Eleonora. AU - Melino, Gerry. PY - 2008/12. Y1 - 2008/12. N2 - Transglutaminases (TGs) are Ca2+-dependent enzymes capable of catalyzing transamidation of glutamine residues to form intermolecular isopeptide bonds. These enzymes are involved in various biological phenomena, including blood coagulation, wound healing, cell death, tissue repair, and terminal differentiation of keratinocytes. Among the TG-family members, TG5 is one of the latest identified enzymes and therefore the less characterized at the functional level. In this work, we reported that TG5 is proteolytically processed in the baculovirus expression system and in mammal epithelial cells. Similar to other members of the TG family - TG1, TG3, and factor XIIIa -, TG5 full-length enzyme has very low enzymatic activity, ...
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Transglutaminases (TGases) are ubiquitous enzymes that catalyze selective crosslinking between protein-bound glutamine and lysine residues; the resulting isopeptide bond confers high resistance to proteolysis. Phytophthora sojae, a pathogen of soybean, secretes a Ca(2+)-dependent TGase (GP42) that is activating defense responses in both host and non-host plants. A GP42 fragment of 13 amino acids, termed Pep-13, was shown to be absolutely indispensable for both TGase and elicitor activity. GP42 does not share significant primary sequence similarity with known TGases from mammals or bacteria. This suggests that GP42 has evolved novel structural and catalytic features to support enzymatic activity. We have solved the crystal structure of the catalytically inactive point mutant GP42 (C290S) at 2.95 A resolution and identified residues involved in catalysis by mutational analysis. The protein comprises three domains that assemble into an elongated structure. Although GP42 has no structural homolog, ...
A tissue transglutaminase (TTG) IgA and/or IgG test is used as part of an evaluation for certain autoimmune conditions, most notably celiac disease.
The problem with this response is that the enzyme your body sends to jump on the gluten and grapple it to the ground, is the same type of enzyme that is also present in countless cells and organs of your body!. When your immune system sends the troops in to attack gluten, it assumes that the enzyme now attached to it is also part of the problem (I feel bad for this enzyme - Tissue Transglutaminase or Ttg - it got mixed up in the wrong crowd and its guilty by association!).. This means your immune system thinks that wherever it comes across this enzyme, it should attack.. It may detect this enzyme in your brain, joints, thyroid, liver, heart, skin… are you seeing the potential scope of the problem?. This is where auto-immune diseases take hold: your immune system attacks your own bodys cells because it thinks they are the enemy.. When your own body begins to attack itself, thats bad news… but there are ways to bring peace to your body.. ...
TGM2 Full-Length MS Protein Standard (NP_945189), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene.
Molecular deletion of transglutaminase 2 (TG2) has been shown to improve function and survival in a host of neurological conditions including stroke, Huntingtons disease, and Parkinsons disease. However, unifying schemes by which these cross-linking or polyaminating enzymes participate broadly in neuronal death have yet to be presented. Unexpectedly, we found that in addition to TG2, TG1 gene expression level is significantly induced following stroke in vivo or due to oxidative stress in vitro. Forced expression of TG1 or TG2 proteins is sufficient to induce neuronal death in Rattus norvegicus cortical neurons in vitro. Accordingly, molecular deletion of TG2 alone is insufficient to protect Mus musculus neurons from oxidative death. By contrast, structurally diverse inhibitors used at concentrations that inhibit TG1 and TG2 simultaneously are neuroprotective. These small molecules inhibit increases in neuronal transamidating activity induced by oxidative stress; they also protect neurons ...
2005 (English)In: Journal of Clinical Gastroenterology, ISSN 0192-0790, E-ISSN 1539-2031, Vol. 39, no 1, 80-81 p.80-81 p.Article in journal (Refereed) Published ...
It has been hypothesized that gluten-dependent production of anti-tissue-transglutaminase 2 (anti-TG2) antibodies may occur only at an intestinal level. We have investigated intestinal production of anti-TG2 antibodies in 136 patients with normal serum levels of anti-TG2 antibodies and normal duodenal mucosa. Intestinal deposits of anti-TG2 antibodies were evaluated by immunofluorescence and anti-TG2 antibodies released in organ culture supernatants measured by ELISA. Intestinal antibody libraries were obtained from 10 subjects. Immunohistochemistry for CD25+, CD3+, and TCR-γδ+ was assessed in subjects with positive (n = 32) and negative (n = 31) intestinal anti-TG2 antibodies. Globally 33/136 (24%) seronegative patients produced anti-TG2 autoantibodies at an intestinal level. Antibody libraries analysis confirmed the anti-TG2 antibodies mucosal production in all (n = 8) positive subjects. Lamina propria CD25+ cell count was significantly (p < 0.05) higher in patients with intestinal anti-TG2.
Transglutaminase-2 antibody [Biotin] | P21980 | Tissue transglutaminase (TG2), Transglutaminase C (TG(C)), (TGC), (TGase C), Transglutaminase H (TGase H), Transglutaminase-2 (TGase-2)
Journal of Cerebral Blood Flow & Metabolism: April 10, 2013. Transglutaminases (TGs) are multifunctional, calcium-dependent enzymes that have been recently implicated in stroke pathophysiology. Classically, these enzymes are thought to participate in cell injury and death in chronic neurodegenerative conditions via their ability to catalyze covalent, nondegradable crosslinks between proteins or to incorporate polyamines into protein substrates. Read more. ...
The New England Journal of Medicine diagnostic challenge is aimed at physicians but anyone can play. This patient has skin lesions (click on image for a better view) that are non-tender, non-itchy and slowly growing. What lab test would cinch the diagnosis? 1. 17-hydroxyprogesterone2. Angiotensin-converting enzyme3. Anti-tissue transglutaminase antibody4. Prolactin5. Vitamin B6 The ...
Diabetes causes endothelial dysfunction, which is the initial trigger for vascular complications in diabetic patients. Hyperglycemia initiates a cascade of events that alters protein expression and secretion by endothelial cells. Tissue transglutaminase-2 (tTG2) is an enzyme that under physiologic conditions is sequestered inside the endothelial cell, but under pathologic conditions causing decreased bioavailability of nitric oxide, tTG2 is secreted, activated, and catalyzes irreversible crosslinking of proteins in the extracellular matrix (ECM). Exendin-4 (Ex-4) is a glucagon-like peptide-1 receptor (GLP-1R) agonist, used in the treatment of type 2 diabetes, which has vasculo-protective effects. We hypothesized that hyperglycemic stress would induce secretion of tTG2, and that this effect would be attenuated by Ex-4. Mouse cardiac microvascular endothelial cells (MCECs) were serum-starved and exposed to control (5.5 mM glucose) or hyperglycemic (25 mM glucose) conditions, with or without Ex-4 ...
Transglutaminase 2兔多克隆抗体(ab71099)可与人样本反应并经WB, IHC, ICC/IF实验严格验证。所有产品均提供质保服务,中国75%以上现货。
References for Abcams Anti-Transglutaminase 6 antibody (ab105725). Please let us know if you have used this product in your publication
spu:578380 K05619 transglutaminase 1 [EC:2.3.2.13] , (RefSeq) etg; extracellular transglutaminase (A) MVRRSTRTSRTPSRFGYSARYEPYTVRKASVLVPAAGRRNVPTQPLVIEKAKETVKQLKV TAVDLCSEANKKAHHTDAYEVDQLILRRGQVMDMCVTFDRAYSSAKDTLSLELLMGSRPS VASGSRVPIDLVTRAPPPDDFGLQVVSSSGNKVTMKVHLACDALVGEYQLVVCTAQTKEE DEYRYECEDDIIILFNPWCKKDDVYMENDKWRKEYVMNENGAYFYGTASNIGSSAWYQGQ FEEVALECALYLLKKSRMTSRHRSSPVEICRVLSALVNSQDDDGVLVGNWSGDYSDGVEP TAWNGSISILSQYMKTETPVEYGQCWVFGSLLTTLCRTLGIPCRTITNFESAHDSDANLT LDYHFNEEGDPLEDLNDDSIWNFHVWNDVWFARPDLPEGYGGWQALDSTPQETSHGEFRM GPASLKAIKQGHVYLDYDTKFAFSEVNAETVYWTVPKNARHAPQVITTDPKGVGNHISTK AVLAESRQDITEEYKYKEGSSLERIAVYNASRYVAKNKNFRKDIKQDVEFEVVLADGTMI GKDFSVKVIATNKSSTTRSGSVTLTGSTVFYTGVRKTRVYSSRRTFSMRAGESETETFTV EAADYIPELTEYAGFTFFIMSSVTQTKQVFSIQKDFVLNKPTLELSITEDLMVGQPMRLS VTFTNPLDKAIRNGVFRIEGPDIDGFKADKFRVIQPNEKVTHVVRIVPKRTGNRRFFANF SSDILIALKGSSTFVVGPSA ...
In this study, we demonstrate that the induction of CYP26 in HTBE cells by retinoids correlates closely with the induction of mucous cell differentiation. HTBE cells grown in the absence of retinoids express a squamous phenotype, as characterized by the expression of the squamous cell marker transglutaminase type I and do not express CYP26 mRNA. In the presence of retinoids, cells undergo mucous cell differentiation, as indicated by MUC2 and MUC5AC expression and mucin secretion (Rearick et al., 1987; Rearick and Jetten, 1989; Koo et al., 1999a,b), and do express CYP26 mRNA. This increase in CYP26 mRNA by retinoids therefore parallels the inhibition of the squamous phenotype and the induction of mucous cell differentiation. Interestingly, the induction of CYP26 and mucous cell differentiation was only observed in confluent cell cultures and not in logarithmically growing cells. These results further strengthen the association between CYP26 expression and mucous cell differentiation. Moreover, ...
Transglutaminase 2/TGM2 Antibodies available through Novus Biologicals. Browse our Transglutaminase 2/TGM2 Antibody catalog backed by our Guarantee+.
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.
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.
For BJH Laboratory Use Only. Analyte Stability:. See Analyte Stability Chart. Laboratory Processing Instructions:. Test performed in BJH Core Lab. Processed by automated line and aliquot stored refrigerated for batch analysis. Completed specimens are stored refrigerated for 5 days.. ...
Enzyme immunoassay for the detection of IgA antibodies to tissue transglutaminase (h-tTG) in human serum or plasma. SmartEIA kit is specifically designed for automated analysis using the Agility instrument.
Rabbit polyclonal Transglutaminase 4 antibody validated for WB, ELISA and tested in Human. Immunogen corresponding to synthetic peptide
Transglutaminase 2 (TG2) is ubiquitously expressed enzyme with multiple functions. It belongs to the large TG2 family of eight isozymes including blood coagula...
A transglutaminase é uma enzima que actua como catalisadora de reacções de ligações entre moléculas de proteína. Este tipo de ligações resultantes da acção desta enzima, são de grande estabilidade e ocorrem entre os aminoácidos glutamina e lisina. Sendo assim,...
Enzymes play a major in the manufacture, processing, preparation and treatment of foods and beverages. They aid digestion and help our body absorb key nutrients. We offer all sorts of enzymes, such as amylases, cellulases, pectinases, phytases, transglutaminases and xylanases. Do not hesitate and contact us if you request more information about our enzyme portfolio or the services we offer. ...
This assay is designed for the in-vitro measurement of specific IgG autoantibodies against tissue transglutaminase (tTG) present in human serum, as an...