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Cleaved-MMP-17 (Q129) Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | Q9ULZ9 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 66653 Da |
| Gene ID | 4326 |
|---|---|
| Other Names | MMP17; MT4MMP; Matrix metalloproteinase-17; MMP-17; Membrane-type matrix metalloproteinase 4; MT-MMP 4; MTMMP4; Membrane-type-4 matrix metalloproteinase; MT4-MMP; MT4MMP |
| Dilution | WB~~Western Blot: 1/500 - 1/2000. ELISA: 1/10000. Not yet tested in other applications. |
| Format | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% (W/V) sodium azide. |
| Storage Conditions | -20℃ |
| 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 |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
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. 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.
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