Item#: 485-10 ALKALINE PHOSPHATASE, Human Lyophilized

Product Name: ALKALINE PHOSPHATASE, Human Lyophilized
Unit Definition: One unit will convert one micromole of p-nitrophenyl phosphate to p-nitrophenol and phosphate per minute at 37�aC in the presence of AMP (2-amino-2-methyl-1-propanol) at pH 10.35
Synonyms: ALP
Protein: Typically >0.1 mg protein/mg
Activity: Typically >10 u/mg @ 37 C
Source: Human Placenta
Cat. No: 485-10
Storage: -20 C
CAS No: 9001-78-9
Expiration: 1 year
EC No: 3.1.3.1
Form: Lyophilized
Price/Unit Qty
$550.00/100units
$250.00/50units

Print This Page       View MSDS sheet

HUMAN (ALP) BULK QUANTITIES of human placenta(l) alkaline phosphatase (ALP)from 1000-25000 unit single lot sizes. Custom buffers for alkaline phosphatase (ALP)available. Custom fills for alkaline phosphatase (ALP)available.

We also offer these Alkaline Phosphatase products:
485-11 HIGH PURITY Alkaline Phosphatase Human
486-10 Alkaline Phosphatase Human
490-20 Alkaline Phosphatase Porcine
480-20 Alkaline Phosphatase Calf

Human Alkaline Phosphatase (ALP, Alk Phos) from human placenta UNIT DEFINITION: One unit will convert one micromole of p-nitrophenyl phosphate to p-nitrophenol and phosphate per minute at 37C in the presence of AMP(2-amino-2-methyl-1-propanol) at pH 10.35

Alkaline phosphatase (ALP) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups in the 5- and 3- positions from many types of molecules, including nucleotides, proteins, and alkaloids. In human(s), alkaline phosphatase is present in all tissues throughout the entire body, but is particularly concentrated in liver, bile duct, kidney, bone, and the placenta. The optimal pH for the enzyme activity is pH=10 in standard conditions.

Alkaline Phosphatase research: Alkaline phosphatase (ALP)(ALK PHOS)from placenta is characteristic for its stability compared with the other types of mammalian isoenzymes. Phosphatase Ref: Fishman, W. H. 1990. Alkaline phosphatase isozymes: recent process. Clin. Biochem. 23:99-104/phosphatase/alkaline
Loading...