CRKL Protein, Human (His, Strep)

CRKL protein mediates intracellular signal transduction, interacts with tyrosine-phosphorylated EPOR and INPP5D/SHIP1, and plays a role in erythropoietin receptor and phosphoinositide signaling. It also binds to DOCK2 and DOCK5, suggesting regulation of guanine nucleotide exchange factors. CRKL Protein, Human (His, Strep) is the recombinant human-derived CRKL protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of CRKL Protein, Human (His, Strep) is 303 a.a., .

The CRKL protein is implicated in mediating the transduction of intracellular signals, indicating its role in cellular signaling pathways. It interacts with tyrosine-phosphorylated EPOR and INPP5D/SHIP1, suggesting its involvement in pathways associated with erythropoietin receptor signaling and phosphoinositide signaling. Additionally, CRKL interacts with DOCK2 and DOCK5 via its first SH3 domain, highlighting its potential role in modulating guanine nucleotide exchange factors. The protein further engages with phosphorylated CBLB and IRS4, indicating its participation in pathways related to cellular proliferation and insulin receptor signaling. Furthermore, CRKL interacts with BCAR1/CAS and NEDD9/HEF1, suggesting its involvement in signaling cascades associated with cell adhesion and migration. These diverse interactions underscore the versatility of CRKL in transmitting signals within the cell.

Human

E. coli

N-Strep;N-6*His

P46109 (M1-E303)

1399

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

<1 EU/μg, determined by LAL method.