P4252
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)
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
42010105
EC Number:
232-631-4
NACRES:
NA.54
MDL number:
Specific activity:
30-90 units/mg protein (modified Warburg-Christian, in glycine buffer)
Biological source:
Escherichia coli
Product Name
Phosphatase, Alkaline from Escherichia coli, ammonium sulfate suspension, 30-90 units/mg protein (modified Warburg-Christian, in glycine buffer)
biological source
Escherichia coli
form
ammonium sulfate suspension
specific activity
30-90 units/mg protein (modified Warburg-Christian, in glycine buffer)
storage temp.
2-8°C
Quality Level
Looking for similar products? Visit Product Comparison Guide
Related Categories
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 is an ammonium sulfate suspension in glycine buffer.
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.
Analysis Note
The activity at pH 8.0 at 25 °C is approximately the same as at pH 10.4 at 37 °C.
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.
Disclaimer
Presence of 0.1% SDS in the alkaline phosphatase assays will inhibit any nuclease contamination in the sample.
Other Notes
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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
E. coli Alkaline Phosphatase
1.Reid, T., and Wilson
The Enzymes, 4, 373-373 (1971)
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)
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
Alkaline phosphatase from Thermotoga neapolitana.
A Savchenko et al.
Methods in enzymology, 331, 298-305 (2001-03-27)
Jessica Leismann et al.
EMBO reports, 21(7), e49443-e49443 (2020-05-01)
RNA modifications have recently emerged as an important layer of gene regulation. N6-methyladenosine (m6 A) is the most prominent modification on eukaryotic messenger RNA and has also been found on noncoding RNA, including ribosomal and small nuclear RNA. Recently, several
Related Content
QC Methods
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service