Recombinant human CD272/BTLA protein (Active)
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Recombinant human CD272/BTLA protein (Active) is a Human Fragment protein, in the 31 to 157 aa range, expressed in CHO cells, with >98%, < 0.6 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.
View Alternative Names
CD272, B- and T-lymphocyte attenuator, B- and T-lymphocyte-associated protein, BTLA
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
BTLA functions as a negative regulator of immune responses by delivering inhibitory signals to immune cells upon binding to its ligand HVEM (Herpesvirus entry mediator). It forms a part of an immunological checkpoint complex that modulates lymphocyte activity to prevent overactivation and autoimmunity. This mechanism helps maintain a balance between immune defense and tolerance contributing to self-tolerance.
Pathways
The BTLA/CD272 protein engages with pathways involved in immune checkpoints and T-cell receptor signaling. It interacts with proteins like HVEM and collaborates with receptors such as PD-1 and CTLA-4. These interactions play a role in the downregulation of T-cell responses which is essential in various immune processes. The signaling pathways influenced by BTLA/CD272 are integral in moderating immune responses cooperation and adaptation.
Specifications
Form
Lyophilized
General info
Function
Inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed : 12796776, PubMed : 14652006, PubMed : 15568026, PubMed : 18193050). May interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14 (PubMed : 19915044). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (PubMed : 19915044).
Post-translational modifications
Phosphorylated on Tyr residues by TNFRSF14 and by antigen receptors cross-linking, both inducing association with PTPN6 and PTPN11.. N-glycosylated.
Target data
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