|Other Names||Matrix metalloproteinase-26, MMP-26, 3424-, Endometase, Matrilysin-2, MMP26|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6207a was selected from the N-term region of human MMP26 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 may hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. It is also able to activates progelatinase B. MMP26 is expressed specifically in uterus and placenta. Is also widely expressed in malignant tumors from different sources as well as in diverse tumor cell lines.
de Coignac, A.B., et al., Eur. J. Biochem. 267(11):3323-3329 (2000).Uria, J.A., et al., Cancer Res. 60(17):4745-4751 (2000).Park, H.I., et al., J. Biol. Chem. 275(27):20540-20544 (2000).
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