ERAP2 Antibody

Product Specifications

Background

The endoplasmic reticulum (ER) aminopeptidase 2 (ERAP2), a member of the peptidase M1 family, like the related protein ERAP1, plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides (1,2) . Like ERAP1, ERAP2 is localized to the lumen of the ER and is thought to associate with ERAP1 as a heterodimer (1) . Both ERAP1 and ERAP2 have been linked to several human diseases ranging from infections to autoimmunity and cancer, and may play a role in the innate immune response (reviewed in 3) .

NCBI Gene ID

64167

Swiss Prot

Q6P179

Accession Number

NP_071745

Host

Rabbit

Reactivity

Human

Clonality

Polyclonal

Conjugation

Unconjugated

Type

Primary Antibodies

Field of Research

Innate Immunity

Purification

ERAP2 Antibody is affinity chromatography purified via peptide column.

Positive Control

Cat. No. 1316 - Human Ovary Tissue Lysate

Concentration

1 mg/mL

Homology

Predicted species reactivity based on immunogen sequence: Bovine: (75%)

Buffer

ERAP2 Antibody is supplied in PBS containing 0.02% sodium azide.

Modification

None

Shipping Conditions

Blue Ice

Storage Conditions

ERAP2 antibody can be stored at 4˚ C for three months and -20˚ C, stable for up to one year.

Fragment

IgG

Specificity

ERAP2 antibody is human reactive. Multiple isoforms of ERAP2 are known to exist. ERAP2 antibody is predicted to not cross-react with ERAP1.

Symbol

ERAP2

NCBI Official Name

Endoplasmic reticulum aminopeptidase 2

NCBI Organism

Homo sapiens

Background Reference 01

Saveanu L, Carroll O, Lindo V, et al. Concerted peptide trimming by EARP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum. Nat. Immunol. 2005; 6:689-97.

Background Reference 02

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.

Background Reference 03

Cifaldi L, Romania P, Lorenzi S, et al. Role of endoplasmic reticulum aminopeptidases in health and disease: from infection to cancer. Int. J. Mol. Sci. 2012; 13:8338-52