|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 (PubMed:2557822, PubMed:2153297, PubMed:1645757). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369).|
|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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