BTN2A1 Protein, Human (Biotinylated, HEK293, Fc-Avi)

BTN2A1 is a direct Vγ9 TCR ligand. BTN2A1 consists of extracellular domains (IgV and IgC), a transmembrane (TM) domain, a coiled-coil domain (JM), an intracellular B30.2 domain and a C-terminal tail. BTN2A1 is an immune checkpoint targeting Vγ9Vδ2 T cell cytotoxicity against malignant cells^[1][2]. BTN2A1 Protein, Human (Biotinylated, HEK293, Fc-Avi) is the recombinant human-derived BTN2A1 protein, expressed by HEK293 , with C-Avi, C-hFc labeled tag. The total length of BTN2A1 Protein, Human (Biotinylated, HEK293, Fc-Avi) is 220 a.a., with molecular weight of 65-70 kDa.

Butyrophilins are a family of transmembrane (TM) proteins of which 8 (BTN1A1, BTN2A1/2A2, BTN3A1/3A2/3A3, MOG, and BTNL2) are located in the major histocompatibility complex (MHC) class I region of human chromosome 6. They are structurally similar to the B7 family, possessing immunoglobulin (Ig)C-IgV extracellular domains, a single-pass TM domain, a juxtamembrane (JTM) domain, and, in most members, an intracellular B30.2 domain. butyrophilin 2A1 (BTN2A1) is required for BTN3A-mediated Vγ9Vδ2 T cell cytotoxicity against cancer cells, and that expression of the BTN2A1/BTN3A1 complex is sufficient to trigger Vγ9Vδ2 TCR activation^[1].
Although BTN2A1’s intracellular B30.2 domain shares around 50% sequence identity with BTN3A1’s intracellular B30.2 domain, the BTN2A1 B30.2 domain does not bind to HMBPP^[2].

Human

HEK293

C-Avi;C-hFc

Q7KYR7-2 (Q29-A248)

11120  [NCBI]

65-70 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.