KDR Kinase Enzyme System
Recombinant human KDR (amino acids 789-end) was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. KDR (or kinase insert domain receptor) is a growth factor receptor tyrosine kinase that was originally isolated from human endothelial cells where it plays a pivotal role in endothelial cell proliferation and differentiation. KDR and its mouse homolog Flk1 bind VEGF with high affinity and are implicated in the development of new blood vessels (angiogenesis). The expression levels of VEGF and KDR are highly correlated during the normal development of the ocular vasculature in humans. Induction of angiogenesis is a critical step in tumor progression, and inhibitors of KDR have been demonstrated both to induce tumor regression and reduce metastatic potential in preclinical models. ADP-Glo Kinase Assay is a luminescent kinase assay that measures ADP formed from a kinase reaction; ADP is converted into ATP, which is a substrate in a reaction catalyzed by Ultra-Glo Luciferase that produces light. The luminescent signal positively correlates with ADP amount and kinase activity. The assay is well suited for measuring the effects chemical compounds have on the activity of a broad range of purified kinases, making it ideal for both primary screening as well as kinase selectivity profiling. The ADP-Glo Kinase Assay can be used to monitor the activity of virtually any ADP-generating enzyme (e.g., kinase or ATPase) using up to 1mM ATP. Kinase Enzyme System contains: Kinase: KDR, 10ug (Human, recombinant; amino acids 789-end). MW: ~110kDa. Substrate: Poly (4:1 Glu, Tyr) Peptide. Other: Reaction Buffer, DTT. KDR NCBI Database Entry: www.ncbi.nlm.nih.gov/gene/3791/. Visit www.promega.com/kinase/ to see all Kinase Enzyme Systems.