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PTK substrate II (Poly(Ala,Glu,Lys,Tyr)6:2:5:1), 10 mg  

PTK substrate II (Poly(Ala,Glu,Lys,Tyr)6:2:5:1), 10 mg

PTK substrate II (Poly(Ala,Glu,Lys,Tyr)6:2:5:1)

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295,00 €

Background: PTK substrate II (Poly(Ala,Glu,Lys,Tyr)6:2:5:1) is a synthetic random polymers of tyrosine containing glutamic acid, alanine, and lysine in various proportion serves as substrates for tyrosine-specific protein kinases. The structural features of tyrosine containing polymers makes them useful for further study the substrate specificity of the family of tyrosine kinases and in search of new (hormone-sensitive) tyrosine kinase activities whose native substrates are still unknown or present at too low concentrations. Several synthetic random polymers serve as superior substrates for tyrosine phosphorylating kinases although various protein kinases show different responses to different polymers.  Some polymers with ordered sequences serve as potential inhibitors of tyrosine-specific protein kinases.

Molecular Weight:               20,000-30,000 Da
Shipment conditions:          Room temperature
Long Term Storage:            -20°C (AVOID FREEZE/THAW CYCLES)
Appearance:                      Lyophilized white solid
Handling:                            soluble in water (50 mg/ml)

PLEASE NOTE: This product is designed for research purposes and can only be delivered to academic and business customers.  

Product specific literature:

Sahal D, Ramachandran J, Fujita-Yamaguchi Y.(1988) “Specificity of tyrosine protein kinases of the structurally related receptors for insulin and insulin-like growth factor I: Tyr-containing synthetic polymers as specific inhibitors or substrates.” Arch Biochem Biophys.;260(1):416-26.

Braun S, Raymond WE, Racker E.(1984) “Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases”. J Biol Chem.;259(4):2051-4.

Zick Y, Grunberger G, Rees-Jones RW, Comi RJ.(1985) “Use of tyrosine-containing polymers to characterize the substrate specificity of insulin and other hormone-stimulated tyrosine kinases.” Eur J Biochem. 148(1):177-82.

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