protein

CDC37 Protein, Human (sf9, GST)

HY-P75364

50 μg

650 USD

CDC37 Protein, Human (sf9, GST)

proteins

Sf9 insect cells

50 μg

650 USD

The CDC37 protein is a co-chaperone that binds multiple kinases and promotes their interaction with the Hsp90 complex, resulting in stability and enhanced activity. CDC37 Protein, Human (sf9, GST) is the recombinant human-derived CDC37 protein, expressed by Sf9 insect cells , with C-GST labeled tag. The total length of CDC37 Protein, Human (sf9, GST) is 378 a.a., with molecular weight of ~70.7 kDa.

Human

The CDC37 protein serves as a co-chaperone with a pivotal role in facilitating the interaction between numerous kinases and the Hsp90 complex, leading to the stabilization and enhanced activity of these kinases. It functions by inhibiting HSP90AA1 ATPase activity. CDC37 is likely a part of multiple protein complexes, including those containing chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, PPP5C, PTGES3/p23, and client proteins like TSC2, CDK4, AKT, RAF1, and NR3C1. Another complex involving CDC37 comprises chaperones HSP90 and HSP70, co-chaperones PPP5C and TSC1, and client proteins TSC2, CDK4, AKT, RAF1, and NR3C1, but notably lacking STIP1/HOP and PTGES3/p23. CDC37 also forms a distinct complex with Hsp90/HSP90AB1 and CDK6. Its interactions extend to various proteins, including HSP90AA1, AR, CDK4, CDK6, EIF2AK1, RB1, KSR1, and FLCN, FNIP1, and FNIP2. This diverse network of interactions underscores the versatility of CDC37 in regulating the stability and activity of a wide array of kinases and client proteins.

Hsp90 co-chaperone Cdc37; CDC37; CDC37A

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

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 100 mM NaCl, 0.5 mM GSH, 0.5 mM PMSF, 10% Glycerol, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.