protein

FKBP12 Protein, Mouse (His)

HY-P76346

2 μg;5 μg;10 μg;50 μg;100 μg

30;50;72;140;200 USD

FKBP12 Protein, Mouse (His)

proteins

E. coli

2 μg;5 μg;10 μg;50 μg;100 μg

30;50;72;140;200 USD

The FKBP12 protein is multifunctional and critical in TGF-β signaling by maintaining TGFBR1 in an inactive conformation, thereby preventing receptor activation in the absence of ligand. It recruits SMAD7 to ACVR1B, blocks the binding of SMAD2 and SMAD3 to the activin receptor complex, and thereby inhibits activin signaling. FKBP12 Protein, Mouse (His) is the recombinant mouse-derived FKBP12 protein, expressed by E. coli , with N-His labeled tag. The total length of FKBP12 Protein, Mouse (His) is 107 a.a., with molecular weight of ~13 KDa.

Mouse

FKBP12, a multifunctional protein, plays a crucial role in maintaining the inactive conformation of TGFBR1, the serine/threonine kinase receptor for TGF-beta, thereby preventing receptor activation in the absence of ligand. This regulatory function contributes to the precise control of TGF-beta signaling. Additionally, FKBP12 recruits SMAD7 to ACVR1B, impeding the association of SMAD2 and SMAD3 with the activin receptor complex and effectively blocking activin signaling. Beyond its role in TGF-beta and activin pathways, FKBP12 exhibits versatility by potentially modulating the activity of the RYR1 calcium channel. Acting as a peptidyl-prolyl cis-trans isomerase (PPIase), FKBP12 accelerates protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This diverse array of functions underscores FKBP12's significance in cellular processes and highlights its involvement in various signaling pathways.

Peptidyl-prolyl cis-trans isomerase FKBP1A; FKBP-12; Calstabin-1; FKBP-1A; FKBP1

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.