|Application ||WB, IHC-P, IF|
|Calculated MW||H=54 KDa|
|Antigen Region||30-59 aa|
|Other Names||MMP3; STMY1; Stromelysin-1; Matrix metalloproteinase-3; Transin-1|
|Target/Specificity||This MMP3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 30-59 amino acids from the N-terminal region of human MMP3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MMP3 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
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Provided below are standard protocols that you may find useful for product applications.
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. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
Fallah, S., et al. J. Physiol. Biochem. 66(4):359-364(2010)
Romero, R., et al. Am. J. Obstet. Gynecol. 203 (4), 361 (2010) :
Nikopensius, T., et al. Birth Defects Res. Part A Clin. Mol. Teratol. 88(9):748-756(2010)
Skorupski, P., et al. Ginekol. Pol. 81(8):594-599(2010)
Yeh, Y.C., et al. BMC Microbiol. 10, 218 (2010) :
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