Anti-Matrix Metalloproteinase-3 (MMP-3, stromelysin-1) [LF-182] Antibody
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This rabbit IgG polyclonal antibody was generated against peptide and is specific for human matrix metalloproteinase-3 (MMP-3, stromelysin-1).
Highlights:
- Recognizes human MMP-3 stromelysin-1- Epitope EPGFPKQIAEDFPGIDSKIDA
- Suitable for Immunohistochemistry and Western Blot applications
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. This protein is capable of degrading several extracellular molecules and a number of bioactive molecules.
From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research/NIH.
This rabbit IgG polyclonal antibody was generated against peptide and is specific for human matrix metalloproteinase-3 (MMP-3, stromelysin-1).
Highlights:
- Recognizes human MMP-3 stromelysin-1- Epitope EPGFPKQIAEDFPGIDSKIDA
- Suitable for Immunohistochemistry and Western Blot applications
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. This protein is capable of degrading several extracellular molecules and a number of bioactive molecules.
From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research/NIH.
This product is for sale to Nonprofit customers only. For profit customers, please Contact Us for more information.
| Product Type: | Antibody |
| Antigen: | stromelysin-1, human |
| Accession ID: | P082543.2 |
| Molecular Weight: | 53977 Da |
| Clonality: | Polyclonal |
| Clone Name: | LF-182 |
| Reactivity: | Human |
| Immunogen: | Peptide |
| Species Immunized: | Rabbit |
| Epitope: | EPGFPKQIAEDFPGIDSKIDA |
| Buffer: | Whole serum |
| Tested Applications: | WB 1:1000, IHC 1:200 |
| Storage: | -80C |
| Shipped: | Cold Packs (Domestic, Overnight); Dry Ice (International) |
- Ogbureke KU, Fisher LW. Expression of SIBLINGs and their partner MMPs in salivary glands. J Dent Res. 2004 Sep;83(9):664-70.
- Ogbureke KU, Fisher LW. Renal expression of SIBLING proteins and their partner matrix metalloproteinases (MMPs). Kidney Int. 2005 Jul;68(1):155-66.
- Ogbureke KU, Nikitakis NG, Warburton G, Ord RA, Sauk JJ, Waller JL, Fisher LW. Up-regulation of SIBLING proteins and correlation with cognate MMP expression in oral cancer. Oral Oncol. 2007 Oct;43(9):920-32.
- Ogbureke KU, Fisher LW. SIBLING expression patterns in duct epithelia reflect the degree of metabolic activity. J Histochem Cytochem. 2007 Apr;55(4):403-9.
- Ogbureke KU, Weinberger PM, Looney SW, Li L, Fisher LW. Expressions of matrix metalloproteinase-9 (MMP-9), dentin sialophosphoprotein (DSPP), and osteopontin (OPN) at histologically negative surgical margins may predict recurrence of oral squamous cell carcinoma. Oncotarget. 2012 Mar;3(3):286-98.
- Anunobi CC, Koli K, Saxena G, Banjo AA, Ogbureke KU. Expression of the SIBLINGs and their MMP partners in human benign and malignant prostate neoplasms. Oncotarget. 2016 Jul 26;7(30):48038-48049.
- Karadag A, Fedarko NS, Fisher LW. Dentin matrix protein 1 enhances invasion potential of colon cancer cells by bridging matrix metalloproteinase-9 to integrins and CD44. Cancer Res. 2005 Dec 15;65(24):11545-52.
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