Analytical Data
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Gene name
TRBV19
- Application
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Alternative Names
TRBV19
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A075B6N1
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Expression Region
22-114 aa
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AA Sequence
GITQSPKYLFRKEGQNVTLSCEQNLNHDAMYWYRQDPGQGLRLIYYSQIVNDFQKGDIAEGYSVSREKKESFPLTVTSAQKNPTAFYLCASSI
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Molecular Weight
16.7 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
TRBV19, or T-cell receptor beta variable gene segment 19, plays a crucial role in the adaptive immune response by allowing T-cells to recognize and bind to various antigens. Research into TRBV19 recombinant proteins has garnered increasing interest in recent years due to their potential applications in immunotherapy and vaccine development. In particular, TRBV19 has been implicated in the immune response to certain viral infections, including HIV, and it displays unique features that may enhance its effectiveness in targeting specific pathogens. Understanding the structure and function of TRBV19 recombinant proteins can provide valuable insight into T-cell receptor dynamics and the overall immune landscape. This research is particularly relevant in the context of developing personalized medicine approaches, where leveraging individual T-cell repertoires may improve therapeutic outcomes. Furthermore, the engineering of TRBV19 proteins may lead to novel strategies for harnessing immune responses against tumors, ultimately enhancing the efficacy of cancer immunotherapies. As scientists continue to explore the intricacies of TRBV19 and its derivatives, there is potential for significant advancements in both basic immunology and clinical applications, paving the way for innovative strategies to combat infectious diseases and cancer.
