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P4252

Sigma-Aldrich

Phosphatase, Alkaline from Escherichia coli

ammonium sulfate suspension, 30-90 units/mg protein (modified Warburg-Christian, in glycine buffer)

Synonym(s):

Orthophosphoric-monoester phosphohydrolase (alkaline optimum)

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About This Item

CAS Number:
9001-78-9
Enzyme Commission number:
3.1.3.1 (BRENDA, IUBMB)
EC Number:
232-631-4
MDL number:
MFCD00131849
UNSPSC Code:
12352204
eCl@ss:
42010105
NACRES:
NA.54

biological source

Escherichia coli

Quality Level

300

form

ammonium sulfate suspension

specific activity

30-90 units/mg protein (modified Warburg-Christian, in glycine buffer)

storage temp.

2-8°C

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Application

Alkaline phosphatase is used for conjugation to antibodies and other proteins for ELISA, Western blotting, and histochemical detection. It may be used for protein labeling when high sensitivity is required. Product P4252 has been used for bulk digestion of tRNA . Product P4252 is provided in the ratio of 30-90 units/mg of protein.
Alkaline phosphatase is used for conjugation to antibodies and other proteins for ELISA, Western blotting, and histochemical detection. It may be used for protein labeling when high sensitivity is required. Product P4252 is an ammonium sulfate suspension in glycine buffer.

Biochem/physiol Actions

Alkaline phosphatase, from Escherichia coli, is a dimeric, non-glycosylated protein which mainly reside in the periplasmic space. Three known isoforms exist. The enzyme requires zinc, and is activated by magnesium. E. coli akaline phosphatase has a broad specificity for phosphate esters.
Alkaline phosphatase, from Escherichia coli, is a dimeric, non-glycosylated protein which mainly reside in the periplasmic space. Three known isoforms exist. The enzyme requires zinc, and is activated by magnesium. E. coli akaline phosphatase has a broad specificity for phosphate esters.

Caution

Presence of 0.1% SDS in the alkaline phosphatase assays will inhibit any nuclease contamination in the sample.

Unit Definition

One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 10.4 at 37 °C.

Physical form

Suspension in 2.5 M (NH4)2SO4

Analysis Note

The activity at pH 8.0 at 25 °C is approximately the same as at pH 10.4 at 37 °C.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Tamaha Yamaguchi et al.
Frontiers in microbiology, 11, 570081-570081 (2021-02-09)
The labile fraction of dissolved organic phosphorus (DOP) - predominantly consisting of phosphoric esters - is an important microbial P source in the subtropical oligotrophic ocean. However, unlike phosphate, knowledge for labile DOP is still limited due to the scarcity
The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA
Basma El Yacoubi, Benjamin Lyons, et al.
RNA, 37, 2894-2909 (2009)
E. coli Alkaline Phosphatase
1.Reid, T., and Wilson
The Enzymes, 4, 373-373 (1971)
Alkaline phosphatase from Thermotoga neapolitana.
A Savchenko et al.
Methods in enzymology, 331, 298-305 (2001-03-27)
R A Anderson et al.
Proceedings of the National Academy of Sciences of the United States of America, 72(1), 394-397 (1975-01-01)
To facilitate the study of individual metal binding sites of polymeric metalloproteins, conversion of exchange-labile Co(II) in E. coli alkaline phosphatase (EC 3.1.3.1) to exchange-inert Co(III) was examined. Oxidation of Co(II) alkaline phosphatase with hydrogen peroxide results in a single
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How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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