Human ENPEP / Aminopeptidase A Recombinant Protein (His Tag)(Discontinued)
Fig 1: Human ENPEP / Aminopeptidase A Recombinant Protein (His Tag)
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| Amount : | 20 µg |
| Purification : | > 90 % as determined by SDS-PAGE |
| Content : | Formulation Supplied as sterile 20 mM, Tris 500 mM NaCl, 10 % glycerol, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. |
| Storage condition : | Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| AA sequence : | Arg41-Gly957 |
| Alternative Name : | APA Protein, CD249 Protein, ENPEP Protein, gp160 Protein, |
Source : Baculovirus-Insect Cells
ENPEP, also known as aminopeptidase A, is a member of the peptidase M1 family. Members of this family are involved in response to cadmium ion and proteolysis. They located in 6 components and are expressed in 26 plant structures. ENPEP is expressed by epithelial cells of the proximal tubule cells and the glomerulus of the nephron. It also can be detected in a variety of other tissues. ENPEP probably plays a role in regulating growth and differentiation of early B-lineage cells. It also may play a role in the catabolic pathway of the renin-angiotensin system. ENPEP is a zinc-dependent membrane-bound aminopeptidase that catalyzes the cleavage of glutamatic and aspartatic amino acid residues from the N-terminus of polypeptides. It degrades vasoconstricting angiotensin II into angiotensin III and therefore helps to regulate blood pressure.
ENPEP, also known as aminopeptidase A, is a member of the peptidase M1 family. Members of this family are involved in response to cadmium ion and proteolysis. They located in 6 components and are expressed in 26 plant structures. ENPEP is expressed by epithelial cells of the proximal tubule cells and the glomerulus of the nephron. It also can be detected in a variety of other tissues. ENPEP probably plays a role in regulating growth and differentiation of early B-lineage cells. It also may play a role in the catabolic pathway of the renin-angiotensin system. ENPEP is a zinc-dependent membrane-bound aminopeptidase that catalyzes the cleavage of glutamatic and aspartatic amino acid residues from the N-terminus of polypeptides. It degrades vasoconstricting angiotensin II into angiotensin III and therefore helps to regulate blood pressure.
Measured by its ability to cleave the fluorogenic peptide substrate, Glu-7-amido-4-methyl coumarin (Glu-AMC). The specific activity is >2000 pmoles/min/µg.
Endotoxin :< 1.0 EU per µg of the protein as determined by the LAL method
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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