kinases protein kinase inhibitors signaling activators kinase substrates antibodies bioluminescence assays
Recombinant human Neprilysin /CD10 Protein, Tag free, 2x500µg  

Recombinant human Neprilysin /CD10 Protein, Tag free, 2x500µg

Recombinant Human Neprilysin / CD10 / MME Protein, Tyr 52 - Trp 750, produced in human 293 cells (HEK293), Tag free

Recombinant Human Protein, MME, CALLA, CD10, NEP, SFE, Neprilysin, metalloportease

More details


Availability: within 7 days

2 200,00 €

Cluster of differentiation 10 (CD10), membrane metallo-endopeptidase, neutral endopeptidase (NEP), Neprilysin, and common acute lymphoblastic leukemia antigen (CALLA), is a 90-110-kDa type II transmembrane glycoprotein normally expressed by a variety of tissues, including epithelial cells of the prostate, kidney, intestine, endometrium, adrenal glands, and lung. This zinc-dependent metalloprotease enzyme cleaves peptide bonds on the amino side of hydrophobic residues and inactivates a variety of physiologically active secreted peptides. CD20 is thought to be the rate-limiting degrading enzyme of amyloid β peptide (Aβ) whose abnormal misfolding and aggregation in neural tissue has been implicated in the development of Alzheimer\'s disease (AD). CD10 is also identified as the common acute lymphoblastic leukemia antigen (CALLA) present on leukemic cells of pre-B phenotype, and thus serves as the most important biomarker in the diagnosis of human acute lymphocytic leukemia (ALL). [1-4]

Recombinant Human Neprilysin /CD10 Protein (rhCD10 / MME) Tyr 52 - Trp 750 (Accession # NP_000893.2) was produced in human 293 cells (HEK293).

Molecular Characterization
Human Neprilysin, with Gly-Pro at the N- terminus, has a calculated MW of 80.0 kDa. The predicted N-terminus is Tyr 52. The reducing (R) protein migrates as 80-100 kDa due to glycosylation.

Less than 1.0 EU per μg of the rhCD10 / MME by the LAL method.

>95% as determined by SDS-PAGE.

Lyophilized from 0.22 μm filtered solution in 20 mM Tris, 100 mM NaCl, pH8.0 . Normally trehalose is added as protectant before lyophilization.

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).


(1) Pardossi-Piquard, et al. 2006, Journal of Neurochemistry 97 (4): 1052–6.
(2) Goodman, O.B. et al., 2006, J. Biol. Chem. 281: 33597-33605.
(3) Cohen, A.J. 1996, Cancer. Res. 56: 831-839.
(4) Shipp M A,. et al., Proc Natl Acad Sci U S A., 86(1): 297-301.