Recombinant human CD10 protein
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(1 Publication)
Recombinant human CD10 protein is a Human Fragment protein, in the 53 to 750 aa range, expressed in Baculovirus infected Sf9 cells, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
CD10, EPN, MME, Neprilysin, Atriopeptidase, Common acute lymphocytic leukemia antigen, Enkephalinase, Neutral endopeptidase 24.11, Skin fibroblast elastase, CALLA, NEP, Neutral endopeptidase, SFE
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human CD10 protein (AB157051)
SDS-PAGE Analysis of 1.0 μg of purified ab157051.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CD10 regulates peptide signaling by inactivating various bioactive peptides such as enkephalins atrial natriuretic peptide and bradykinin. It does not function as part of a complex but rather as a standalone entity. The ability of CD10 to hydrolyze peptides influences signal transmission across cellular membranes impacting cellular communication and signal termination within different systems.
Pathways
Neprilysin plays an essential role in hydrolyzing signaling peptides in several critical pathways. It is especially significant in the natriuretic peptide system and the renin-angiotensin system maintaining blood pressure and fluid balance. Within these pathways CD10 modifies peptides working alongside proteins like atrial natriuretic peptide synthase and angiotensin-converting enzyme ensuring systemic homeostasis and cardiovascular health.
Specifications
Form
Liquid
Additional notes
ab157051 has been purified in the glycosylated soluble form.
General info
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).
Sequence similarities
Belongs to the peptidase M13 family.
Post-translational modifications
Myristoylation is a determinant of membrane targeting.. Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity.
Target data
Publications (1)
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Advanced science (Weinheim, Baden-Wurttemberg, Germany) 8:e2101848 PubMed34363355
2021
Applications
Unspecified application
Species
Unspecified reactive species
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