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MMP14 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P50281 |
|---|---|
| Other Accession | NP_004986 |
| Clone Names | 2090309 |
| Gene ID | 4323 |
|---|---|
| Other Names | Matrix metalloproteinase-14, MMP-14, MMP-X1, Membrane-type matrix metalloproteinase 1, MT-MMP 1, MTMMP1, Membrane-type-1 matrix metalloproteinase, MT1-MMP, MT1MMP, MMP14 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6198a was selected from the N-term region of human MMP14 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| 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. |
| Name | MMP14 |
|---|---|
| Function | Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (PubMed:20837484). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (PubMed:12714657). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (PubMed:22330140). |
| Cellular Location | Membrane; Single-pass type I membrane protein. Melanosome. Cytoplasm. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV Forms a complex with BST2 and localizes to the cytoplasm |
| Tissue Location | Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors. |
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Provided below are standard protocols that you may find useful for product applications.
Background
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. MMP14 seems to specifically activate progelatinase A, and may thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. Expression is significant in stromal cells of colon, breast, and head and neck.
References
Will, H., et al., Eur. J. Biochem. 231(3):602-608 (1995).Takino, T., et al., Gene 155(2):293-298 (1995).Okada, A., et al., Proc. Natl. Acad. Sci. U.S.A. 92(7):2730-2734 (1995).Sato, H., et al., Nature 370(6484):61-65 (1994).
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