P4377
Phosphatase, Alkaline from Escherichia coli
ammonium sulfate suspension, ~10 units/mg protein (modified Warburg-Christian)
Synonym(s):
Orthophosphoric-monoester phosphohydrolase (alkaline optimum)
form
ammonium sulfate suspension
specific activity
~10 units/mg protein (modified Warburg-Christian)
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 P4377 has been used for cell digestion during measurement of photoreactivating enzyme
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.
Physical form
Suspension in 2.5 M (NH4)2SO4 solution
Preparation Note
Salt fractionated
Other Notes
One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 10.4 at 37 °C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
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
Regulatory Information
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B M Sutherland et al.
Journal of bacteriology, 138(2), 333-338 (1979-05-01)
Sutherland et al. mapped a phr gene in Escherichia coli at 17 min and found that induction of an E. coli strain lysogenic for a lambda phage carrying this gene increased photoreactivating enzyme levels 2,000-fold. Recently, Smith and Youngs and
Naomi Ofer et al.
The Journal of biological chemistry, 288(16), 11287-11293 (2013-03-09)
Protein degradation via prokaryotic ubiquitin-like protein (Pup) tagging is conserved in bacteria belonging to the phyla Actinobacteria and Nitrospira. The physiological role of this novel proteolytic pathway is not yet clear, although in Mycobacterium tuberculosis, the world's most threatening bacterial
Lars Hansen et al.
American journal of human genetics, 92(4), 575-583 (2013-04-09)
PGAP2 encodes a protein involved in remodeling the glycosylphosphatidylinositol (GPI) anchor in the Golgi apparatus. After synthesis in the endoplasmic reticulum (ER), GPI anchors are transferred to the proteins and are remodeled while transported through the Golgi to the cell
C Cavallo et al.
Journal of biological regulators and homeostatic agents, 27(1), 165-175 (2013-03-16)
Bone marrow is one of the best characterized stem cell microenvironments that contains Mesenchymal Stem Cells (MSCs), a rare population of non-hematopoietic stromal cells. MSCs have been indicated as a new option for regenerative medicine because of their ability to
Peter M Krawitz et al.
American journal of human genetics, 92(4), 584-589 (2013-04-09)
Recently, mutations in genes involved in the biosynthesis of the glycosylphosphatidylinositol (GPI) anchor have been identified in a new subclass of congenital disorders of glycosylation (CDGs) with a distinct spectrum of clinical features. To date, mutations have been identified in
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