MMP17 Antibody (aa409-423)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, E |
---|---|
Primary Accession | Q9ULZ9 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 67kDa |
Dilution | ELISA (1:1000), IHC-P (3-5 µg/ml), |
Gene ID | 4326 |
---|---|
Other Names | Matrix metalloproteinase-17, MMP-17, 3.4.24.-, Membrane-type matrix metalloproteinase 4, MT-MMP 4, MTMMP4, Membrane-type-4 matrix metalloproteinase, MT4-MMP, MT4MMP, MMP17, MT4MMP |
Target/Specificity | Amino acids 409 to 423 of human MMP17 |
Reconstitution & Storage | Long term: -20°C; Short term: +4°C. Avoid repeat freeze-thaw cycles. |
Precautions | MMP17 Antibody (aa409-423) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | MMP17 |
---|---|
Synonyms | MT4MMP |
Function | Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. |
Cellular Location | [Isoform Long]: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side. Secreted, extracellular space, extracellular matrix |
Tissue Location | Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non- transformed cell types |
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Background
Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.
References
Kajita M.,et al.FEBS Lett. 457:353-356(1999).
Seiki M.,et al.Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
Puente X.S.,et al.Cancer Res. 56:944-949(1996).
Scherer S.E.,et al.Nature 440:346-351(2006).
Wang Y.,et al.J. Biol. Chem. 274:33043-33049(1999).
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