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Neprilysin (human), (recombinant) (His-tag)

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BML-SE532-0010 10 µg 503.00 USD
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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
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.
MW:80.7 kDa (calculated) / ~85 kDa (glycosylated form on SDS-PAGE)
Source:Produced in Sf9 insect cells. Produced in a baculovirus expression system.
UniProt ID:P08473
Formulation:Liquid. In 50mM TRIS, pH 8.0, containing 300mM sodium chloride and 20% glycerol.
Purity:≥95% (SDS-PAGE)
Purity Detail:Purified as the glycosylated soluble form.
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Stable on ice for at least 1h. Do not freeze in dilute form.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
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.
Regulatory Status:RUO - Research Use Only
Neprilysin (human), (recombinant) (His-tag) SDS-PAGE
SDS-PAGE Analysis: Lane1: MWM; Lane 2:  1.0 μg of purified Neprilysin protein.
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Neprilysin (human), (recombinant) (His-tag) SDS-PAGE

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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