Phosphorylase|Targetmol

Phosphorylase

Phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor.They include allosteric enzymes that catalyze the production of glucose-1-phosphate from a glucan such as glycogen, starch or maltodextrin.

Cat No.	product name
T0626	Uric Acid	Uric acid is an oxidation product of oxypurines such as XANTHINE and HYPOXANTHINE. It is the final oxidation product of purine catabolism in humans and primates...
T3855	Tracheloside	Tracheloside significantly decreases the activity of alkaline phosphatase (IC50: 0.31 μg/ml), a level of inhibition comparable to that of tamoxifen (IC50: 0.43...
T3938	L(+)-Homoarginine hydrochloride	L-Homoarginine is a specific inhibitor of liver-type alkaline phosphatase.
T6353	(-)-p-Bromotetramisole Oxalate	p-Bromotetramisole Oxalate is a potent and non-specific alkaline phosphatase inhibitor.
T8103	H-HoArg-OH	H-HoArg-OH, a homologue arginine, is a strong inhibitor of human bone and liver alkaline phosphatase.
T8155	Maltoheptaose	Maltoheptaose is an activator of phosphorylase B for the preparation of heptulose-2-phosphate.

Cat No.

product name

T0626

Uric Acid

Uric acid is an oxidation product of oxypurines such as XANTHINE and HYPOXANTHINE. It is the final oxidation product of purine catabolism in humans and primates...

T3855

Tracheloside

Tracheloside significantly decreases the activity of alkaline phosphatase (IC50: 0.31 μg/ml), a level of inhibition comparable to that of tamoxifen (IC50: 0.43...

T3938

L(+)-Homoarginine hydrochloride

L-Homoarginine is a specific inhibitor of liver-type alkaline phosphatase.

T6353

(-)-p-Bromotetramisole Oxalate

p-Bromotetramisole Oxalate is a potent and non-specific alkaline phosphatase inhibitor.

T8103

H-HoArg-OH

H-HoArg-OH, a homologue arginine, is a strong inhibitor of human bone and liver alkaline phosphatase.

T8155

Maltoheptaose

Maltoheptaose is an activator of phosphorylase B for the preparation of heptulose-2-phosphate.

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