MME Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | P08473 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | polyclonal |
Calculated MW | H=86;M=86;Rat=86 KDa |
Isotype | Rabbit IgG |
Antigen Source | HUMAN |
Gene ID | 4311 |
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Antigen Region | 99-132 aa |
Other Names | Neprilysin, Atriopeptidase, Common acute lymphocytic leukemia antigen, CALLA, Enkephalinase, Neutral endopeptidase 2411, NEP, Neutral endopeptidase, Skin fibroblast elastase, SFE, CD10, MME, EPN |
Dilution | WB~~1:1000 |
Target/Specificity | This MME antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 99-132 amino acids from the N-terminal region of human MME. |
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 | MME Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | MME {ECO:0000303|PubMed:27588448, ECO:0000312|HGNC:HGNC:7154} |
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Function | Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:6208535, PubMed:6349683, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991, PubMed:6349683). Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (PubMed:6208535). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675, PubMed:6349683). Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) (PubMed:16254193, PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). |
Cellular Location | Cell membrane; Single-pass type II membrane protein |
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Background
Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV- inducible elastase activity toward skin preelastic and elastic fibers.
References
Letarte M.,et al.J. Exp. Med. 168:1247-1253(1988).
Shipp M.A.,et al.Proc. Natl. Acad. Sci. U.S.A. 85:4819-4823(1988).
D'Adamio L.,et al.Proc. Natl. Acad. Sci. U.S.A. 86:7103-7107(1989).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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