|Other Names||Matrix metalloproteinase-27, MMP-27, 3424-, MMP27|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6208a was selected from the C-term region of human MMP27 . 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||Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens.|
|Cellular Location||Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Retained in the endoplasmic reticulum.|
|Tissue Location||Expressed in B-cells (PubMed:14506071). Expressed in a subset of endometrial macrophages related to menstruation and in ovarian and peritoneal endometriotic lesions (at protein level)(PubMed:24810263).|
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Provided below are standard protocols that you may find useful for product applications.
Matrix Metalloproteases (MMPs) are zinc-dependent endopeptidases that break down the extracellular matrix, and thus play important roles in many physiological processes including embryonic development, wound healing, reproduction, tissue remodeling, arthritis, cancer and cardiovascular disease. Although most MMPs are secreted, the membrane-type MMPs (MT-MMPs) are anchored to the cell membrane by a transmembrane and intracytoplasmic domain. MMP activities are regulated at several levels, including cleavage of proenzyme forms and suppression via tissue inhibitors of metalloproteinases (TIMPs). The 513 amino acid human MMP27 protein is located primarily in extracellular spaces in the extracellular matrix, and maps to chromosome 11q24.
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