Analytical Data
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Gene name
HLA-DRA1*01:01&HLA-DRB1*04:01 Monomer
- Application
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Alternative Names
MHCDRa; HLADRa; Major Histocompatibility Complex Class II DR Alpha
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Species
Rabbit
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q30847
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Expression Region
Ala26~Cys221
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Molecular Weight
31kDa
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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
The study of HLA-DRA1*01:01 and HLA-DRB1*04:01 monomer recombinant proteins is rooted in the understanding of human immune response, particularly in relation to autoimmune diseases, transplant rejection, and infectious diseases. HLA (Human Leukocyte Antigen) molecules play a crucial role in the presentation of peptide antigens to T cells, influencing adaptive immune responses. HLA-DRB1*04:01 is associated with several autoimmune conditions, such as rheumatoid arthritis and multiple sclerosis, making it a significant target for research. By generating monomeric forms of these HLA class II proteins, researchers aim to study their structural dynamics, binding affinities, and interactions with various peptides. This approach helps elucidate the molecular mechanisms that underlie antigen presentation and T cell activation. Furthermore, these recombinant proteins can facilitate the development of diagnostic tools and therapeutic strategies aimed at modulating immune responses in disease contexts. Understanding the precise mechanisms of HLA-DR interactions not only advances immunological research but also has the potential to improve clinical outcomes in transplantation and autoimmune disease management.
