Where to get CDC42 + PAK6 complex?

Description of CDC42 + PAK6 complex
Serine/threonine-protein kinase PAK 6 is an enzyme that in humans is encoded by the PAK6 gene.
PAK6 encodes a protein that shares a high degree of sequence similarity with p21-activated kinase (PAK) family members. The proteins of this family are Rac/Cdc42-associated Ste20-like Ser/Thr protein kinases, characterized by a highly conserved amino-terminal Cdc42/Rac interactive binding (CRIB) domain and a carboxyl-terminal kinase domain. PAK kinases are implicated in the regulation of a number of cellular processes, including cytoskeleton rearrangement, apoptosis and the MAP kinase signaling pathway. The protein encoded by this gene was found to interact with androgen receptor (AR), which is a steroid hormone-dependent transcription factor that is important for male sexual differentiation and development. The p21-activated protein kinase 6 gene was found to be highly expressed in testis and prostate tissues and the encoded protein was shown to cotranslocate into the nucleus with AR in response to androgen.
Six members of the p21-activated kinase (PAK) family of protein kinases have been identified to date. PAK’s are serine/threonine kinases and can be classified into two groups named group I (PAK 1-3), and group II (PAK6) based on their sequence homology and regulatory properties. In addition to the C-terminal Ste20-like catalytic domain, PAK kinases contain a Cdc42/Rac-interactive binding (CRIB) domain. PAK family members have been implicated in the regulation of multiple cellular functions, including actin reorganization, apoptotic signaling, cell motility, gene transcription, cell transformation and steroid hormone receptor signalling.
The binding of activated GTP-bound Cdc42 or Rac to group I PAKs dramatically stimulates their ability to phosphorylate exogenous substrates. In contrast, the group II PAK kinase PAK4 and PAK5 are active in the absence of GTPases and their enzymatic activity is not further stimulated by binding of activated GTPase. The reason for this difference in regulation is most likely due to the lack of an inhibitory switch domain in group II PAK’s which releases the active site upon binding of GTPases. However, GTPase binding has been shown to mediate kinase relocalization. For example upon binding of Cdc42, PAK4 relocalizes to the Golgi, and PAK5 shuttles from the microtubule network to actin-rich structures.
Here we present the crystal structure of activated cdc42 in complex with the CRIB domain of PAK6, the complex when formed is believed to coordinate the cellular relocalizarion of the kinase.
More about: CDC42 + PAK6 complex sale
Read more: Proteases Enzyme