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Validated All-in-One™ qPCR Primer for COL3A1(NM_000090.3) Search again
Product ID:
HQP002478
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
EDS4A, EDSVASC, PMGEDSV
Gene Description:
collagen type III alpha 1 chain
Target Gene Accession:
NM_000090.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes the pro-alpha1 chains of type III collagen, a fibrillar collagen that is found in extensible connective tissues such as skin, lung, uterus, intestine and the vascular system, frequently in association with type I collagen.
Gene References into function
- mutational analysis in Ehlers-Danlos syndrome type IV
- keratinocyte growth factor (KGF), a key stimulator of epithelial cell proliferation during wound healing, preferentially binds to collagens I, III, and VI.
- COL3A1 mutations appear not to be a major cause of isolated spontaneous cervical artery dissections
- variants in the COL3A1 gene modulate the risk of coronary artery disease and could also modulate the response to antithrombotic therapy
- collagen type III was up-regulated by high glucose, but not by TGF-beta1 in renal fibroblasts
- Proportion of collagen III relative to collagen I increased significantly up to 6 weeks after initial injury and remained elevated up to 6 months, at which time the proportion of collagen III was 70% above baseline values
- Although connective tissue growth factor alone had no effect on collagen secretion, combined stimulation with IGF-I enhanced collagen accumulation.
- fibroblasts from Ehlers-Danlos syndrome patients, with mutations in COL5A1 and COL3A1, synthesize aberrant types V and III collagen and show defective organization of these proteins into the extracellular matrix and reduction of alpha(2)beta(1) integrin
- Association between COL3A1 collagen gene exon 31 and risk of floppy mitral valve/mitral valve prolapse among the Chinese population of Taiwan
- The lower collagen content in the endopelvic fascia and skin of women with SUI is not due to reduced collagen synthesis or selective reduction in synthesis of either collagen I or collagen III.
- Predicted rates of AA substitution for Gly are compared with missense mutations known to cause disease. Any Gly replacement causes disease. The level of triple-helix destabilization determines outcome. More destabilizing mutations were seen than expected
- hnRNP A1 & K ARE positive effectors of collagen synthesis acting at the post-transcriptional level by interaction with the 3'-untranslated region (3'-UTR) of 3A1 mRNAs.
- characterization of the proximal promoter of the COL3A1 gene; segment from -96 to -34 necessary for activation of transcription; multiple proteins depending on cell types, found to form the DNA-protein complex at -79 to -63
- analysis of binding between collagen type III and integrins alpha1beta1 and alpha2beta1
- collagen III, and probably fibronectin, are degraded extracellularly in smooth muscle cells from varicose veins by a mechanism involving MMPs, and maybe MMP3 by a direct or an indirect pathway
- Antisense oligodeoxynuclotides down-regulate collagen type III gene expression.
- demonstrates, for the first time, that BIRC3 (anti-apoptotic protein), COL3A1 (matrix protein synthesis), and CXCL3 (chemokine) were up-regulated in the thrombin-stimulated human umbilical vein endothelial cells
- The expression of precursor proteins and mRNA of type I and type III collagens is increased in usual interstitial pneumonia and sarcoidosis, reflecting mainly active synthesis of these collagens in different areas of the lung.
- Type III collagen was expressed significantly higher in valvular cardiomyopathy.
- data showed the complexity of the regulation of the COL3A1 gene (human alpha1(III) collagen) involving several transcription factors.
- Altered expression of decorin mRNA in the different dermal strata and a decrease in the collagen-to-decorin ratio inflicted by both age and ultraviolet irradiation affect collagen bundle diameter and subsequently the mechanical properties of human skin.
- The results suggest that a high level of decorin mRNA might be associated with the reduced content of collagen type III, resulting in a less flexible form of extracellular matrix in the connective tissue in stress urinary incontinence and prolapse.
- COL3A1 was overexpressed in uterine fibroids.
- Case report of a novel COL3A1 gene mutation in patient with aortic dissected aneurysm and cervical artery dissections.
- High glucose levels downregulate mRNA levels in dermal fibroblast cell cultures.
- Data reveal a more critical role for membrane cholesterol in collagen type III-induced than in VWF-induced Ca(2+) signalling.
- There may be an association between COL3A1 genotype and risk of pelvic organ prolapse
- the human type III collagen Gly991-Gly1032 cystine knot-containing peptide has both 7/2 and 10/3 triple helical symmetries
- COL3A1 exon 31 polymorphism may have a role in determining the risk of pelvic organ prolapse in women