protein

SKP1 Protein, Human (Biotinylated, His-Avi)

HY-P76644

5 μg;10 μg;50 μg;100 μg

80;137;382;650 USD

SKP1 Protein, Human (Biotinylated, His-Avi)

proteins

HEK293

5 μg;10 μg;50 μg;100 μg

80;137;382;650 USD

The SKP1 protein is a component of the SCF ubiquitin ligase complex and targets cell cycle progression and signal transduction. SKP1 Protein, Human (Biotinylated, His-Avi) is the recombinant human-derived SKP1 protein, expressed by HEK293 , with C-Avi, N-His labeled tag. The total length of SKP1 Protein, Human (Biotinylated, His-Avi) is 162 a.a., with molecular weight of 23-28 kDa.

Human

SKP1, an indispensable component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, plays a crucial role in orchestrating the ubiquitination of proteins involved in diverse cellular processes, including cell cycle progression, signal transduction, and transcription. Within the SCF complex, SKP1 serves as an essential adapter, bridging the F-box protein to CUL1 and, consequently, facilitating the substrate recognition function of the SCF complex. The specificity of SCF-mediated ubiquitination is contingent on the F-box protein's unique substrate recognition capabilities. Several F-box proteins within the SCF complex, such as BTRC, FBXW11, SKP2, FBXW7, FBXO32, and others, are implicated in directing ubiquitination events targeting key regulatory proteins involved in Wnt signaling, NF-kappa-B activation, G1/S transition regulation, and diverse cellular pathways. This intricate network of interactions highlights SKP1's pivotal role as a molecular adapter in the SCF ubiquitin ligase complex, governing the dynamic regulation of protein modification through ubiquitination.

S-phase kinase-associated protein 1; p19A; OCP-2; p19skp1; EMC19; SKP1A; TCEB1L

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

Lyophilized from a 0.2 μm filtered solution of PBS, 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.