Endoplasmic reticulum aminopeptidase 1 (Erap1), partial Recombinant Protein | Erap1 recombinant protein

Recombinant Mouse Endoplasmic reticulum aminopeptidase 1 (Erap1), partial

Cat. Num. AAA1361542

• Gene Names: Erap1; Arts1; ERAAP; PILSA; PILSAP
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Endoplasmic reticulum aminopeptidase 1 (Erap1); partial; Recombinant Mouse Endoplasmic reticulum aminopeptidase 1 (Erap1); Endoplasmic reticulum aminopeptidase 1; EC=3.4.11.-; ARTS-1; Adipocyte-derived leucine aminopeptidase; A-LAP; Aminopeptidase PILS; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; VEGF-induced aminopeptidase; Erap1 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 731-930aa; Partial
• Sequence: PCVQRAERYFREWKSSNGNMSIPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCTSKDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLRENWNKLVQKFELGSSSIAHMVMGTTDQFSTRARLEEVKGFFSSLKENGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKEKPELL
• Sequence Length: 930

• Species: Mus musculus (Mouse)
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

SDS-PAGE

Related Product Information for Erap1 recombinant protein

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).

Product Categories/Family for Erap1 recombinant protein

Immunology

NCBI and Uniprot Product Information

• NCBI GI #: 13507656
• NCBI GeneID: 80898
• NCBI Accession #: NP_109636.1
• NCBI GenBank Nucleotide #: NM_030711.4
• UniProt Accession #: Q9EQH2; Q6GTP5; Q9ET63
• Molecular Weight: 28.3 kDa
• NCBI Official Full Name: endoplasmic reticulum aminopeptidase 1
• NCBI Official Synonym Full Names: endoplasmic reticulum aminopeptidase 1
• NCBI Official Symbol: Erap1
• NCBI Official Synonym Symbols: Arts1; ERAAP; PILSA; PILSAP
• NCBI Protein Information: endoplasmic reticulum aminopeptidase 1; A-LAP; ARTS-1; PILS-AP; aminopeptidase PILS; VEGF-induced aminopeptidase; adipocyte-derived leucine aminopeptidase; puromycin-insensitive leucyl-specific aminopeptidase; type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
• UniProt Protein Name: Endoplasmic reticulum aminopeptidase 1
• Protein Family: Endoplasmic reticulum aminopeptidase
• UniProt Gene Name: Erap1
• UniProt Synonym Gene Names: Appils; Arts1; A-LAP; PILS-AP
• UniProt Entry Name: ERAP1_MOUSE

Uniprot Description

ARTS1: 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. Belongs to the peptidase M1 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.4.11.-; Membrane protein, integral; Protease

Cellular Component: extracellular space; intracellular membrane-bound organelle; membrane; endoplasmic reticulum lumen; endoplasmic reticulum; cytoplasm; integral to membrane; extracellular region

Molecular Function: peptidase activity; interleukin-6 receptor binding; metalloexopeptidase activity; metallopeptidase activity; hydrolase activity; zinc ion binding; metal ion binding; aminopeptidase activity; tumor necrosis factor receptor binding

Biological Process: positive regulation of angiogenesis; immune system process; membrane protein ectodomain proteolysis; proteolysis