Analytical Data
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Gene name
HLA-DQA2
- Application
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Alternative Names
DX alpha chainHLA class II histocompatibility antigen, DQ(6) alpha chainHLA-DQA1MHC class II DQA2
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01906
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Expression Region
24-214aa
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Molecular Weight
25.6 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
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Protein Description
HLA-DQA2 is a crucial component of the human major histocompatibility complex (MHC) class II molecules, which play a vital role in the immune system by presenting peptide antigens to CD4+ T cells. Understanding the structure and function of HLA-DQA2 is essential for insights into immune recognition and responses, particularly in the context of autoimmune diseases, allergies, and transplant rejection. Research on recombinant HLA-DQA2 proteins has garnered interest due to their potential applications in immunotherapy, vaccine development, and understanding disease susceptibility linked to genetic variations in MHC genes. The production of recombinant HLA-DQA2 allows for detailed studies of its interactions with peptides and T cell receptors, enhancing our understanding of antigen presentation mechanisms. Furthermore, elucidating the x-ray crystallographic structure of HLA-DQA2 in complex with specific peptides can provide crucial information regarding binding preferences and the subsequent immune response. This research is particularly relevant in studying population genetics, as variations in HLA-DQA2 can influence the prevalence of certain diseases across different ethnic groups. Overall, the investigation of HLA-DQA2 and its recombinant proteins is pivotal in advancing our knowledge of the immune system and developing novel therapeutic strategies against various diseases.
