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ERAP1 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, IF, E |
|---|---|
| Primary Accession | Q9NZ08 |
| Other Accession | NP_057526, 94818901 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | Predicted: 104 kDa Observed: 105kDa |
| Application Notes | ERAP1 antibody can be used for detection of ERAP1 by Western blot at 1 - 2 µg/ml. |
| Gene ID | 51752 |
|---|---|
| Target/Specificity | ERAP1; ERAP1 antibody is human and mouse reactive. At least two isoforms of ERAP1 are known to exist; this antibody will detect both isoforms. ERAP1 antibody is predicted to not cross-react with ERAP2. |
| Reconstitution & Storage | ERAP1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. |
| Precautions | ERAP1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| 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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Provided below are standard protocols that you may find useful for product applications.
Background
The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1), a member of the peptidase M1 family, plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides (1,2). It is also designated as adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1) (3). ERAP1 is localized to the lumen of the ER and induced by interferon. It may be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (3,4).
References
Hattori A, Kitatani K, Matsumoto H, et al. Characterization of recombinant human adipocytederived leucine aminopeptidase expressed in Chinese hamster ovary cells. J. Biochem. 2000; 128:755-62.
Saric T, Chang SC, Hattori A, et al. An IFN-gamma induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat. Immunol. 2002; 3:1169-76.
Cui X, Hawari F, Alsaaty S, et al. Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding. J. Clin. Invest. 2002; 110:515-26.
Akada T, Yamazaki T, Miyashita H, et al. Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) is involved in the activation of endothelial integrins. J. Cell Physiol. 2002; 193: 253-62.
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