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MMP10 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P09238 |
|---|---|
| Other Accession | NP_002416 |
| Clone Names | 2090305 |
| Gene ID | 4319 |
|---|---|
| Other Names | Stromelysin-2, SL-2, Matrix metalloproteinase-10, MMP-10, Transin-2, MMP10, STMY2 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6194a was selected from the C-term region of human MMP10 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | MMP10 |
|---|---|
| Synonyms | STMY2 |
| Function | Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase. |
| Cellular Location | Secreted, extracellular space, extracellular matrix |
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Provided below are standard protocols that you may find useful for product applications.
Background
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. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP10 degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
References
Nagase, H., et al., J. Biol. Chem. 274(31):21491-21494 (1999).Pendas, A.M., et al., Genomics 37(2):266-268 (1996).Jung, J.Y., et al., Ann. Genet. 33(1):21-23 (1990).Sirum, K.L., et al., Biochemistry 28(22):8691-8698 (1989).Muller, D., et al., Biochem. J. 253(1):187-192 (1988).
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