Analytical Data
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Gene name
TRBC2
- Application
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Alternative Names
TRBC2；TCRBC2；T cell receptor beta constant 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A5B9
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Expression Region
1-129aa
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AA Sequence
DLKNVFPPKVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRAD
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Molecular Weight
16.2 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
TRBC2, or T-cell receptor beta constant region 2, is a crucial component of the T-cell receptor (TCR) complex, which plays a vital role in the adaptive immune response. TCRs are essential for T cells to recognize antigens presented by major histocompatibility complex (MHC) molecules on the surface of cells. The TRBC2 protein, encoded by the TRBC2 gene, contributes to the structural stability and functionality of the TCR. Research on TRBC2 recombinant proteins has gained importance as it facilitates the study of TCR structure and function, the mechanisms of T-cell activation, and the development of immunotherapies for cancer and autoimmune diseases. By expressing TRBC2 as a recombinant protein, scientists can investigate its interactions with various components of the immune system and develop strategies to enhance T-cell responses in therapies. Moreover, recombinant TRBC2 proteins can serve as valuable tools in vaccine development and in creating engineered T cells with specific antigen recognition capabilities, thereby improving therapeutic efficacy in combating infections and malignancies. Overall, the study of TRBC2 recombinant proteins is pivotal in advancing our understanding of T-cell biology and enhancing the efficacy of immunotherapeutic approaches.
