|Other Names||Matrix metalloproteinase-26, MMP-26, 3424-, Endometase, Matrilysin-2, MMP26|
|Target/Specificity||The synthetic peptide sequence is selected from aa 111-125 of HUMAN MMP26|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
|Tissue Location||Expressed specifically in uterus and placenta. Is also widely expressed in malignant tumors from different sources as well as in diverse tumor cell lines|
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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. The encoded protein degrades type IV collagen, fibronectin, fibrinogen, casein, vitronectin, alpha 1-antitrypsin, alpha 2-macroglobulin, and insulin-like growth factor-binding protein 1, and activates MMP9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.
de Amorim, R.F., et al. Acta Odontol. Scand. 68(4):228-231(2010)
Ban, J.Y., et al. Life Sci. 86 (19-20), 756-759 (2010) :
Deng, Y., et al. Oncol. Rep. 23(1):69-78(2010)
Johnatty, S.E., et al. PLoS Genet. 6 (7), E1001016 (2010) :
Liu, J., et al. Reprod. Biol. Endocrinol. 8, 5 (2010) :
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