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Recombinant human MME /CD10 Protein, Fc Tag, 50µg  

Recombinant human MME /CD10 Protein, Fc Tag, 50µg

Recombinant Human Neprilysin /CD10 Protein, Tyr52-Trp750, produced in human 293 cells (HEK293), Fc Tag

Synonym
Recombinant Human Protein, MME, CALLA, CD10, CD-10, NEP, SFE, Neprilysin

More details

MME-H526a-050

Availability: within 7 days

336,00 €

Background
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]

Source
Recombinant Human Neprilysin /CD10 Protein,With N-Fc Tag Tyr52-Trp750 (Accession # AAI01659) was produced in human 293 cells (HEK293).

Molecular Characterization
Human CD10, fused with Fc fragment of human IgG1 at the N-terminus, has a calculated MW of 107.3 kDa expressed. The predicted N-terminus is Tyr52. Protein migrates as 120-130 kDa in reduced SDS-PAGE due to glycosylation.

Endotoxin
Less than 1.0 EU endotoxin per μg rhCD10 by the LAL method.

Purity
>95% purity as determined by SDS-PAGE of reduced rhCD10.

Formulation
Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH7.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.

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

Storage
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).

References

(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. 1989, Proc. Natl. Acad. Sci. USA. 86: 297-301.