Analytical Data
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Gene name
CD1A-B2M Heterodimer
- Application
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Alternative Names
CD1-A; CD1; FCB6; HTA1; R4; T6; T-cell surface antigen T6/Leu-6; hTa1 thymocyte antigen
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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
P06126
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Expression Region
Asn17~Val300
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Molecular Weight
35&28kDa
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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 CD1C-B2M heterodimer is a key component in the immune system, playing a crucial role in the presentation of lipid antigens to T cells. CD1C, a member of the CD1 family, is responsible for presenting glycolipid antigens derived from various sources, including pathogens and self-lipids, to invariant natural killer T (iNKT) cells. The heterodimerization with β2-microglobulin (B2M) is essential for the proper folding, stability, and surface expression of the CD1C molecule. Understanding the structure and function of the CD1C-B2M heterodimer is vital for elucidating its role in immune responses and potential applications in immunotherapy. Recombinant protein studies have enabled the exploration of this heterodimer's antigen presentation capabilities, providing insights into its interactions with T cell receptors. This research holds promise for developing novel therapeutic strategies targeting lipid antigens in various diseases, including cancer and infectious diseases, thereby enhancing our understanding of the complexities of immune recognition and response.
