Neprilysin is a glycosylated zinc endopeptidase whose physiological targets include bradykinin, glucagon, GLP-1, and neuropeptides. Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1.
Product Details
| Alternative Name: | NEP, Neutral endopeptidase 24.11, Enkephalinase, CALLA, Common acute lymphoblastic leukemia antigen, CD10 |
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| Sequence: | NEP from human cDNA, transcript variant 1, aa 53-750 (D53 - W750; Identical to GeneBank accession NM_000902) is fused at the N-terminus to a His-tag. |
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| MW: | 80.7 kDa (calculated) / ~85 kDa (glycosylated form on SDS-PAGE) |
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| Source: | Produced in Sf9 insect cells. Produced in a baculovirus expression system. |
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| EC: | 3.4.24.11 |
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| UniProt ID: | P08473 |
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| Formulation: | Liquid. In 50mM TRIS, pH 8.0, containing 300mM sodium chloride and 20% glycerol. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Purity Detail: | Purified as the glycosylated soluble form. |
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| Application Notes: | Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Stable on ice for at least 1h. Do not freeze in dilute form. |
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| Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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| Scientific Background: | Neprilysin is an integral plasma membrane (or secreted soluble) protease that has has a broad expression pattern, but is most abundant in the kidney. Due to its involvement in cancer, Alzheimer’s and Parkinson’s diseases, hypertension, diabetes, and pain, it is an important research target. |
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| Regulatory Status: | RUO - Research Use Only |
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SDS-PAGE Analysis: Lane1: MWM; Lane 2: 1.0 μg of purified Neprilysin protein.
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Product Literature References
Neprilysins regulate muscle contraction and heart function via cleavage of SERCA-inhibitory micropeptides: R. Schiemann, et al.; Nat. Commun.
13, 4420 (2022),
Abstract;
Identification of peptide products from enzymatic degradation of amyloid beta: M. Rogeberg, et al.; Biochimie
105, 216 (2014),
Abstract;
General Literature References
Enkephalinase inhibitors: potential agents for the management of pain: V. Thanawala, et al.; Curr. Drug Targets
9, 887 (2008),
Abstract;
Metals in Alzheimer's and Parkinson's Diseases: K.J. Barnham & A.I. Bush; Curr. Opin. Chem. Biol.
12, 222 (2008),
Abstract;
Structural studies of a bifunctional inhibitor of neprilysin and DPPIV: C. Oefner, et al.; Acta Crystallogr. D Biol. Crystallogr.
63, 975 (2007),
Abstract;
Towards triple vasopeptidase inhibitors for the treatment of cardiovascular diseases: P. Daull, et al.; J. Cardiovasc. Pharmacol.
50, 247 (2007),
Abstract;
Angiotensin converting enzyme (ACE) and neprilysin hydrolyze neuropeptides: a brief history, the beginning and follow-ups to early studies: R.A. Skidgel & E.G. Erdös; Peptides
25, 521 (2004),
Abstract;
Full Text
Neutral endopeptidase 24.11 is important for the degradation of both endogenous and exogenous glucagon in anesthetized pigs: R. Trebbien, et al.; Am. J. Physiol. Endocrinol. Metab.
287, E431 (2004),
Abstract;
Full Text
Neutral endopeptidase protein expression and prognosis in localized prostate cancer.: I. Osman et al.; Clin. Cancer Res.
10, 4096 (2004),
Abstract;
Full Text
The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function: A.J. Turner, et al.; BioEssays
23, 261 (2001),
Abstract;
Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology: B.P. Roques, et al.; Pharmacol. Rev.
45, 87 (1993),
Abstract;
Purification and characterization of the neutral endopeptidase from human kidney: M. Ishida, et al.; J. Biochem.
94, 17 (1983),
Abstract;
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