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MMP20 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | O60882 |
| Other Accession | O18767, NP_004762.2 |
| Reactivity | Human |
| Predicted | Bovine |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 54387 Da |
| Antigen Region | 399-428 aa |
| Gene ID | 9313 |
|---|---|
| Other Names | Matrix metalloproteinase-20, MMP-20, 3424-, Enamel metalloproteinase, Enamelysin, MMP20 |
| Target/Specificity | This MMP20 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 399-428 amino acids from the C-terminal region of human MMP20. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | MMP20 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MMP20 |
|---|---|
| Function | Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site. |
| Cellular Location | Secreted, extracellular space, extracellular matrix |
| Tissue Location | Expressed specifically in the enamel organ. |
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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 MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene degrades amelogenin, the major protein component of dental enamel matrix, and so the protein is thought to play a role in tooth enamel formation. A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. This gene is part of a cluster of MMP genes that localizes to chromosome 11q22.3.
References
Bailey, S.D., et al. Diabetes Care (2010) In press :
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Wojciechowski, R., et al. Invest. Ophthalmol. Vis. Sci. (2010) In press :
Lee, S.K., et al. J. Dent. Res. 89(1):46-50(2010)
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
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