protein

SAG Protein, Human (P.pastoris, His)

HY-P71781

5 μg;10 μg;50 μg

173;294;823 USD

SAG Protein, Human (P.pastoris, His)

proteins

P. pastoris

5 μg;10 μg;50 μg

173;294;823 USD

SAG proteins play a crucial role in phototransduction, regulating signal transduction by binding to light-activated and phosphorylated rhodopsin (RHO). It terminates RHO signaling by competitively interacting with G proteins at the same binding site on RHO. SAG Protein, Human (P.pastoris, His) is the recombinant human-derived SAG protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of SAG Protein, Human (P.pastoris, His) is 405 a.a., with molecular weight of ~47.1 kDa.

Human

The SAG protein exhibits a crucial regulatory role in phototransduction by binding to photoactivated and phosphorylated rhodopsin (RHO), thereby terminating RHO signaling via G-proteins. Through competitive interaction with G-proteins for the same binding site on RHO, SAG effectively modulates signal transduction in a manner consistent with similar proteins. Moreover, SAG may contribute to preventing light-dependent degeneration of retinal photoreceptor cells, as suggested by research findings. Structurally, SAG can exist as a monomer, homodimer, or homotetramer, highlighting its versatile oligomeric states. Furthermore, SAG engages in specific interactions with RHO, specifically binding to the phosphorylated C-terminus, elucidating its intricate involvement in the molecular dynamics of photoreceptor cells.

48kDa protein; Arrestin 1; Arrestin; ARRS_HUMAN; S antigen; S arrestin; S-AG; S-arrestin; SAG

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized after extensive dialysis against solution in 20 mM Tris-HC1, 0.5 M NaCl, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.