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TIMP-3 (Tissue Inhibitor of Metalloproteinase-3) Antibody - With BSA and Azide
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, IF, FC |
|---|---|
| Primary Accession | P35625 |
| Other Accession | 7078, 644633, 714168 |
| Reactivity | Human, Mouse, Rat, Bovine, Horse, Dog |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit / IgG |
| Clone Names | |
| Calculated MW | 30kDa |
| Gene ID | 7078 |
|---|---|
| Other Names | Metalloproteinase inhibitor 3, Protein MIG-5, Tissue inhibitor of metalloproteinases 3, TIMP-3, TIMP3 |
| Format | 200ug/ml of Ab purified from rabbit anti-serum by Protein A. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA at 1.0mg/ml. |
| Storage | Store at 2 to 8°C.Antibody is stable for 24 months. |
| Precautions | TIMP-3 (Tissue Inhibitor of Metalloproteinase-3) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TIMP3 |
|---|---|
| Function | Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15. |
| Cellular Location | Secreted, extracellular space, extracellular matrix |
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
TIMP3 (tissue inhibitor of metalloproteinases 3), along with family members TIMP1, TIMP2, and TIMP4, are inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix (ECM). An imbalance between MMPs and the associated TIMPs may play a significant role in the invasive phenotype of malignant tumors. TIMP s inhibit the proteolytic invasiveness of tumor cells and normal placental trophoblast cells. TIMP-3 may be involved in regulating trophoblastic invasion of the uterus as well as in regulating remodeling of the extracellular matrix during the folding of epithelia, and in the formation, branching and expansion of epithelial tubes.
References
Nagase, H. et al. (2006) Cardiovasc Res 69, 562-73. | Visse, R. and Nagase, H. (2003) Circ Res 92, 827-39. |
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