Alkaline phosphatase, placental, human recombinant

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SKU:
P1044-50
€185
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Description

Alkaline phosphatase, placental, human recombinant is available at Gentaur for Next week delivery.

A hydrolase enzyme responsible for removing phosphate groups

Biomolecule/Target: ALPP

Alternates names: ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1

Synonyms: ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1

Background Information: ALPP, also known as alkaline phosphatase, placental, is a family of dimeric metalloenzymes catalyzing the hydrolysis of monoesters of phosphoric acid. Also, this protein catalyzes a transphosphorylation reaction in the presence of large concentrations of phosphate acceptors. It occurs widely in nature, and are found in many organisms from Escherichia coli to man. Most alkaline phosphatases are homodimeric enzymes and each catalytic site contains three metal ions (two Zn and one Mg), that are necessary for enzymatic activity. Recombinant human ALPP, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.

Reconstitution Instructions: N/A

NCBI Gene Symbol: ALPP

Gene ID: 250

NCBI Accession: P05187

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Additional Information

Size:
50 μg
Country of Manufacturing Origin:
USA
Country of Animal Origin:
USA
Gene Source:
Human
Recombinant:
Yes
Source:
Baculovirus
Purity by SDS-PAGE:
> 95%
Assay:
SDS-PAGE
Purity:
N/A
Assay 2:
N/A
Endotoxin Level:
< 1.0 EU per/μg
Activity (Specifications/test method):
Measured by its ablity to hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
Biological activity:
Specific activity is > 2,500 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
Results:
> 2,500 units/mg
Molecular Weight:
53.9 kDa
Storage Temperature:
-20°C
Shelf Life:
12 months
Concentration:
N/A
Appearance:
Liquid
Handling:
Centrifuge the vial prior to opening.
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