ERAP1 Antibody
Rabbit mAb
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC |
---|---|
Primary Accession | Q9NZ08 |
Reactivity | Rat |
Clonality | Monoclonal |
Other Names | ALAP; Aminopeptidase PILS; APPILS; Arts1; Endoplasmic reticulum aminopeptidase 1; ERAAP; ERAAP1; Erap1; PILSA; PILSAP; |
Isotype | Rabbit IgG |
Host | Rabbit |
Calculated MW | 107235 Da |
Dilution | WB 1:500~1:2000 IHC 1:50~1:200 |
---|---|
Purification | Affinity-chromatography |
Immunogen | A synthesized peptide derived from human ERAP1 |
Description | 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. |
Storage Condition and Buffer | Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle. |
Name | ERAP1 |
---|---|
Synonyms | APPILS, ARTS1, KIAA0525 |
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. |
Cellular Location | Endoplasmic reticulum membrane; Single-pass type II membrane protein |
Tissue Location | Ubiquitous. |

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