Analytical Data
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Gene name
ERAP2
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简介
ERAP2 protein, a key aminopeptidase, plays a pivotal role in peptide trimming, crucial for generating peptides binding to HLA class I molecules. By selectively hydrolyzing basic residues like Arginine (Arg) and Lysine (Lys), ERAP2 precisely customizes longer precursor peptides, ensuring optimal length for effective presentation on MHC class I molecules. ERAP2 Protein, Human (HEK293, His) is the recombinant human-derived ERAP2 protein, expressed by HEK293 , with N-10*His labeled tag.
- Application
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Alternative Names
Endoplasmic reticulum aminopeptidase 2; L-RAP; ERAP2; LRAP
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Species
Human
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Source
HEK293
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Tag
N-10*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q6P179-1
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Expression Region
A56-T960
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AA Sequence
ATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
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Protein Length
Partial
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Molecular Weight
115-125 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ERAP2 (Endoplasmic Reticulum Aminopeptidase 2) is a critical enzyme involved in the processing of peptides for presentation on major histocompatibility complex (MHC) class I molecules, playing a significant role in the adaptive immune response. Its function is essential for the generation of a diverse repertoire of MHC class I ligands, which are pivotal for T cell recognition and activation. Studies have indicated that variations in the ERAP2 gene are associated with susceptibility to various autoimmune diseases and infections, underscoring its importance in immune regulation. The recombinant expression of ERAP2 allows for the detailed characterization of its enzymatic activity, substrate specificity, and structural properties, enabling researchers to understand its role in immune modulation better. Additionally, recombinant ERAP2 can be utilized for in vitro assays to evaluate potential therapeutic interventions targeting peptide processing pathways. A deeper understanding of ERAP2's mechanisms may lead to the development of novel therapies for autoimmune diseases and improved vaccine designs, highlighting its significance in both immunology and therapeutic research.











