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Validated All-in-One™ qPCR Primer for MMP10(NM_002425.2) Search again
Powered by BiozBy 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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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
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
Gene References into function
- The catalytic domain of human matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 angstroms resolution.
- Beta-carotene suppresses UVA-induction of MMP-10.
- a tightly regulated expression level of stromelysin-2 is required for limited matrix degradation at the wound site
- Overexpression of MMP-10 is associated with non-small cell lung cancer
- identified significant interactions between MMP10 (nt+180) polymorphisms and gender in abdominal aortic aneurysm
- zinc finger protein 267 as a negative transcriptional regulator of MMP-10 might promote liver fibrogenesis
- Increased levels of MMP-10 is associated with gastric cancer
- Finally, we found that induction of mmp-3 and mmp-10 gene expression by hypomethylation was cell-specific, suggesting that epigenetic changes may predispose cells to express stromelysin genes.
- C-reactive protein augmented MMP-1 and -10 messenger ribonucleic acid expression in vascular endothelial cells. Might provide a link between inflammation and plaque vulnerability.
- The ability of MMP-10 to superactivate procollagenases that are relevant to cartilage degradation suggests that this activation represents an important mechanism by which this MMP contributes to tissue destruction in arthritis.
- Primary colorectal cancers and metastatic liver lesions showed highly significant differences in MMP-1, -10, -11, and TIMP-1.
- MMP-10 protein levels were higher in the lung tumor tissues than in the adjacent normal tissues.
- Knockdown of MMP-10 expression blocks anchorage-independent growth and invasion of NSCLC cells and addition of catalytically active MMP-10 to PKCiota- or Par6alpha-deficient cells restores anchorage-independent growth and invasion
- VEGF stimulates HDAC7 phosphorylation and cytoplasmic accumulation modulating MT-MMP1/MMP10 expression and angiogenesis.