|Calculated MW||54007 Da|
|Other Names||Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, 22 kDa interstitial collagenase, 27 kDa interstitial collagenase, MMP1, CLG|
|Target/Specificity||A synthetic peptide corresponding to residues on the N-term of human MMP-1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MMP-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
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Provided below are standard protocols that you may find useful for product applications.
Human interstitial collagenase (matrix metalloproteinase-1, MMP-1), an enzyme whose only known physiologic substrate has heretofore been believed to be the extracellular matrix molecule, collagen. Data indicate that matrix metalloproteinase-1 displays an expanded substrate repertoire that supports the existence of a new interface between connective tissue turnover and serine proteinase inhibitors (1). It has been shown that the MMP-1 functions as a protease agonist of Protease-activated receptors (PAR1) cleaving the receptor at the proper site to generate PAR1-dependent Ca2+ signals and migration. These results demonstrate that MMP-1 in the stromal-tumor microenvironment can alter the behavior of cancer cells through PAR1 to promote cell migration and invasion (2). It has also been suggested that increased levels of MMP-1 due to tobacco smoking plays a major role in the aging process of skin since MMP-1 degrades collagen, which accounts for at least 70% of the dry weight of dermis. Significantly more MMP-1 has been detected in the skin of smokers than non-smokers whereas no difference was seen for the tissue inhibitor of metalloproteinases 1 (TIMP-1) (3).
1. Desrochers PE, et al. J Clin Invest 87(6):2258-65, 1991.
2. Boire A, et al. Cell 120(3):303-13, 2005.
3. Lahmann C, et al. Lancet 357(9260):935-6, 2001.
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