The primer mix has been verified to generate satisfactory qPCR data on Roche Applied-science LightCycler® 480 Ⅱ.
Storage & Shipping
Shipping:
Lyophilized qPCR primer mix is shipped at ambiente temperatura
Storage:
The lyophilized product is stable for one year from date of receipt when stored at -20℃.
The suspended product is stable for six months from date of receipt when stored at -20℃.
***Sino biological qEASY qPCR primer pairs are used for SYBR Green-based real-time RT-PCR, The primers are designed by using SBI's proprietary primer design algorithm. Our primer collection covers the entire human genomes. It can be widely applied in the quantitative analysis of gene expression.***
Features and Advantages
Unique Primer Design
To avoid genomic DNA amplification, at least one primer is designed crosses the junction of exons according to the conserved region of a specific gene with all variants.
Strict Validation Process
Confirmed in positive organizations; screened the primer with high specificity and high sensitivity.
Uniform PCR conditions, Saving time and cost
~100% amplification curve, ensuring the accuracy of the RNA quantitative
Human MMP7 qPCR Primer Pair: Synonyms
MMP-7 qPCR Primer Pairs, Human; MPSL1 qPCR Primer Pairs, Human; PUMP-1 qPCR Primer Pairs, Human
MMP7 Background Information
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological and pathological processes such as morphogenesis, differentiation, angiogenesis, tissue remodeling, and tumor invasion. MMPs are synthesized as pro-enzymes and converted to the active form by extracellular proteinases. MMP7 also referred to as matrilysin, is the smallest member of the MMP family and differs from other MMP members in that it lacks the C-terminal hemopexin-like domain. MMP7 is produced primarily by mucosal epithelia and is capable of degrading various ECM proteins including proteoglycans, fibronectin, elastin, and casein. This enzyme serves essential functions in both innate defense and wound healing, and appears to be one of the most important MMPs in human colon cancers. It has been reported that MMP7 contributes to tumor malignancy probably by cleaving cell surface proteins such as Fas ligand, degradation of IgG, or inducing E-cadherin-mediated cell aggregation. Besides, matrilysin is also identified as a mediator of pulmonary fibrosis and a potential therapeutic target.
Muller D., et al.,(1988), The collagenase gene family in humans consists of at least four members. Biochem. J. 253:187-192.
Marti H.P., et al., (1992), Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1.Biochem. J. 285:899-905.
Gaire M., et al.,(1994), Structure and expression of the human gene for the matrix metalloproteinase matrilysin.J. Biol. Chem. 269:2032-2040.
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