Analytical Data
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Gene name
BTN2A1-BTN3A1
- Application
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Alternative Names
CD277
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Species
Human
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Source
Yeast
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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
O00481
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Expression Region
30-254aa
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Molecular Weight
26.2 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
Related Products
Protein Description
BTN2A1 and BTN3A1 are members of the B7 family of immune regulatory proteins that play crucial roles in modulating T cell responses and maintaining immune homeostasis. BTN2A1, also known as butyrophilin 2A1, is involved in presenting lipid antigens to T cells, while BTN3A1 is recognized for its role in presenting non-peptide antigens. Recent research highlights their significance in cancer immunotherapy and autoimmunity, as they affect T cell activation and differentiation. The generation of recombinant BTN2A1-BTN3A1 proteins allows for detailed studies of their interactions and functional mechanisms. Understanding these interactions could lead to novel therapeutic strategies that enhance immune responses against tumors or modulate autoimmunity. Additionally, the exploration of BTN2A1-BTN3A1 complexes may unveil new pathways for T cell activation, offering insights into the development of effective vaccines. The recombination techniques employed to produce these proteins enable researchers to investigate their structure-function relationships and establish their importance in immune signaling pathways. This research not only expands our comprehension of immune regulation but also opens avenues for innovative treatments that harness the power of the immune system in various diseases.
