MMP14 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | P50281 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 63 KDa |
Antigen Region | 481 - 540 aa |
Gene ID | 4323 |
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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 | KLH conjugated synthetic peptide derived from human MMP14 |
Dilution | WB~~ 1:1000 |
Format | 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50% |
Storage | Store at -20 °C.Stable for 12 months from date of receipt |
Name | MMP14 |
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Function | Endopeptidase that degrades various components of the extracellular matrix such as collagen (PubMed:8015608). Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). Activates progelatinase A/MMP2, thereby acting as a positive regulator of cell growth and migration (PubMed:22065321, PubMed:8015608). Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (PubMed:12714657, PubMed:22065321). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (PubMed:20837484). Acts as a regulator of Notch signaling by mediating cleavage and inhibition of DLL1 (PubMed:21572390). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (PubMed:22330140). Acts as a negative regulator of the GDF15-GFRAL aversive response by mediating cleavage and inactivation of GFRAL (PubMed:35177851). |
Cellular Location | Cell membrane; Single-pass type I membrane protein. Melanosome. Cytoplasm Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Forms a complex with BST2 and localizes to the cytoplasm (PubMed:17081065) |
Tissue Location | Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors. |
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Background
Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15.
References
Sato H.,et al.Nature 370:61-65(1994).
Takino T.,et al.Gene 155:293-298(1995).
Okada A.,et al.Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995).
Will H.,et al.Eur. J. Biochem. 231:602-608(1995).
Luo G.-X.,et al.Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
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