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Rabbit Anti-ERAP1 (C-terminus) Recombinant Antibody (EPR6069) (CBMAB-E1622-FY)

This product is rabbit antibody that recognizes ERAP1. The antibody EPR6069 can be used for immunoassay techniques such as: WB, IHC-P, ICC.
See all ERAP1 antibodies

Summary

Host Animal
Rabbit
Specificity
Mouse, Rat, Human
Clone
EPR6069
Antibody Isotype
IgG
Application
WB, IHC-P, ICC

Basic Information

Immunogen
A synthetic peptide corresponding to residues on the C-terminus in human ERAP1 was used as an immunogen
Specificity
Mouse, Rat, Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
49% PBS, 50% glycerol, 0.05% BSA
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
C-terminus

Target

Full Name
Endoplasmic Reticulum Aminopeptidase 1
Introduction
The protein encoded by this gene is an aminopeptidase involved in trimming HLA class I-binding precursors so that they can be presented on MHC class I molecules. The encoded protein acts as a monomer or as a heterodimer with ERAP2. This protein may also be involved in blood pressure regulation by inactivation of angiotensin II. Three transcript variants encoding two different isoforms have been found for this gene.
Entrez Gene ID
Human51752
Mouse80898
Rat80897
UniProt ID
HumanQ9NZ08
MouseQ9EQH2
RatQ9JJ22
Alternative Names
Endoplasmic Reticulum Aminopeptidase 1; Puromycin-Insensitive Leucyl-Specific Aminopeptidase; Adipocyte-Derived Leucine Aminopeptidase; Type 1 Tumor Necrosis Factor Receptor Shedding Aminopeptidase Regulator; Aminopeptidase Regulator Of TNFR1 Shedding; Aminopeptidase PILS; PILS-AP; APPILS; ARTS-1; A-LAP; ARTS1; Endoplasmic Reticulum Aminopeptidase Associated With Antigen Processing; Endoplasmic Reticulum Aminopeptidase 1 Delta-Exon-11 Isoform
Research Area
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.
Biological Process
Adaptive immune response Source: UniProtKB-KW
Angiogenesis Source: HGNC-UCL
Antigen processing and presentation of endogenous peptide antigen via MHC class I Source: HGNC-UCL
Antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
Fat cell differentiation Source: UniProtKB
Membrane protein ectodomain proteolysis Source: UniProtKB
Peptide catabolic process Source: GO_Central
Positive regulation of angiogenesis Source: Ensembl
Proteolysis Source: GO_Central
Regulation of blood pressure Source: GO_Central
Regulation of innate immune response Source: UniProtKB
Response to bacterium Source: BHF-UCL
Signal transduction Source: GO_Central
Cellular Location
Endoplasmic reticulum membrane
Topology
Cytoplasmic: 1
Helical: 2-21
Lumenal: 22-941
PTM
N-glycosylated.

Arakawa, A., Reeves, E., Vollmer, S., Arakawa, Y., He, M., Galinski, A., ... & Prinz, J. C. (2021). ERAP1 controls the autoimmune response against melanocytes in psoriasis by generating the melanocyte autoantigen and regulating its amount for HLA-C* 06: 02 presentation. The Journal of Immunology, 207(9), 2235-2244.

Maben, Z., Arya, R., Georgiadis, D., Stratikos, E., & Stern, L. J. (2021). Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism. Nature communications, 12(1), 1-15.

Reeves, E., Islam, Y., & James, E. (2020). ERAP1: A potential therapeutic target for a myriad of diseases. Expert Opinion on Therapeutic Targets, 24(6), 535-544.

Babaie, F., Hosseinzadeh, R., Ebrazeh, M., Seyfizadeh, N., Aslani, S., Salimi, S., ... & Mohammadi, H. (2020). The roles of ERAP1 and ERAP2 in autoimmunity and cancer immunity: New insights and perspective. Molecular immunology, 121, 7-19.

Bufalieri, F., Infante, P., Bernardi, F., Caimano, M., Romania, P., Moretti, M., ... & Di Marcotullio, L. (2019). ERAP1 promotes Hedgehog-dependent tumorigenesis by controlling USP47-mediated degradation of βTrCP. Nature communications, 10(1), 1-15.

Compagnone, M., Cifaldi, L., & Fruci, D. (2019). Regulation of ERAP1 and ERAP2 genes and their disfunction in human cancer. Human immunology, 80(5), 318-324.

Admon, A. (2019). ERAP1 shapes just part of the immunopeptidome. Human immunology, 80(5), 296-301.

Yao, Y., Liu, N., Zhou, Z., & Shi, L. (2019). Influence of ERAP1 and ERAP2 gene polymorphisms on disease susceptibility in different populations. Human immunology, 80(5), 325-334.

Reeves, E., & James, E. (2018). The role of polymorphic ERAP1 in autoinflammatory disease. Bioscience reports, 38(4).

López de Castro, J. A. (2018). How ERAP1 and ERAP2 shape the peptidomes of disease-associated MHC-I proteins. Frontiers in Immunology, 9, 2463.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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