Mouse ENPEP / Aminopeptidase A Protein (His Tag)

Produkt-Information von ENPEP / Aminopeptidase A Protein

QC Testing von ENPEP / Aminopeptidase A Protein

Purity	> 91 % as determined by SDS-PAGE	SDS-PAGE: ENPEP / Aminopeptidase A protein
Bio-activity	Measured by its ability to cleave the fluorogenic peptide substrate, Glu-7-amido-4-methyl coumarin. The specific activity is > 200 pmoles/min/μg.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	His
Molecular Mass	The recombinant mouse ENPEP consists of  921 amino acids and predicts a molecular mass of 106 KDa. It migrates as an approximately 113 KDa band in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from a 0.2μm filtered solution of 20mM Tris, 500mM NaCl, pH7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von ENPEP / Aminopeptidase A Protein

Verwandte Produkte & Themen von ENPEP / Aminopeptidase A Protein

Enzyme>>Other>> ENPEP / aminopeptidase A

Beschreibung von ENPEP / Aminopeptidase A Protein

ENPEP, also known as aminopeptidase A, is a member of the peptidase M1 family. Peptidase M1 family proteins locate in 6 components and are expressed in 26 plant structures. They function in metallopeptidase activity and zinc ion binding. They are also involved in response to cadmium ion and proteolysis. 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 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 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.

References

1. Speth RC. et al., 2008, Heart Fail Rev. 13 (3): 299-309.
2. Rose JE. et al., 2010, Mol Med. 16 (7-8): 247-53.
3. Pérez I. et al., 2009, Head Neck. 31 (10): 1335-40.

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