Recombinant Mouse Endoplasmic reticulum aminopeptidase 1 (Erap1), partial

Product Description

Recombinant Mouse Endoplasmic reticulum aminopeptidase 1 (Erap1), partial is available at Gentaur for Next week Delivery.

Gene Name: Erap1

Alternative Names : ARTS-1 Adipocyte-derived leucine aminopeptidase

Expression Region : 731-930aa

AA Sequence : PCVQRAERYFREWKSSNGNMSIPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCTSKDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLRENWNKLVQKFELGSSSIAHMVMGTTDQFSTRARLEEVKGFFSSLKENGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKEKPELL

Sequence Info : Partial

Tag Info : N-terminal 10xHis-tagged and C-terminal Myc-tagged

Theoretical MW : 28.3 kDa

Storage Buffer : Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Endotoxin Level : Not tested-

Biological Activity : Not tested

Storage : Short term: -20°C; Long term: -80°C. Minimize freeze and thaw cycles.

Research Area : Immunology

Restriction : For Research Use Only. Not for use in diagnostic procedures, drug use, or for administration to humans or animals.

Relevance : Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity).

Function : Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity).

Involvement in disease :

Subcellular location : Endoplasmic reticulum membrane, Single-pass type II membrane protein

Protein Families : Peptidase M1 family

Tissue Specificity :

Paythway :

Uniprot ID : Q9EQH2