P9614
Lambda protein phosphatase
liquid, Bacteriophage Lambda, recombinant, expressed in E. coli
Synonym(e):
Lambda-PPase
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About This Item
Empfohlene Produkte
Rekombinant
expressed in E. coli
Qualitätsniveau
Form
liquid
Mol-Gew.
25 kDa
Konzentration
≥400000 units/mL
Versandbedingung
dry ice
Lagertemp.
−70°C
Allgemeine Beschreibung
Lambda protein phosphatase is a recombinant protein expressed in Escherichia coli. It requires Mn2+ or Ni2+ as activators.
Biochem./physiol. Wirkung
Lambda protein phosphatase has been used to dephosphorylate HeLa cell extracts.
Can be used to release phosphate groups from serine, threonine or tyrosine residues in proteins. Also active on phosphorylated histidine residues.
Einheitendefinition
One unit will hydrolyze 1 nanomole of p-nitrophenyl phosphate per min at pH 7.5 at 30 deg C.
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.
Zhuo S
The Journal of Biological Chemistry, 268(24), 17754-17761 (1993)
Proliferating cell nuclear antigen-dependent rapid recruitment of Cdt1 and CRL4Cdt2 at DNA-damaged sites after UV irradiation in HeLa cells.
Ishii T
The Journal of Biological Chemistry, 285(53), 41993-42000 (2010)
P T Cohen et al.
The Biochemical journal, 260(3), 931-934 (1989-06-15)
Infection of Escherichia coli with phage lambda gt10 resulted in the appearance of a protein phosphatase with activity towards 32P-labelled casein. Activity reached a maximum near the point of cell lysis and declined thereafter. The phosphatase was stimulated 30-fold by
Kyoko Chiba et al.
Molecular biology of the cell, 28(26), 3857-3869 (2017-11-03)
In neurons, amyloid β-protein precursor (APP) is transported by binding to kinesin-1, mediated by JNK-interacting protein 1b (JIP1b), which generates the enhanced fast velocity (EFV) and efficient high frequency (EHF) of APP anterograde transport. Previously, we showed that EFV requires
Delphine Pflieger et al.
Molecular & cellular proteomics : MCP, 7(2), 326-346 (2007-10-25)
Protein complexes have largely been studied by immunoaffinity purification and (mass spectrometric) analysis. Although this approach has been widely and successfully used it is limited because it has difficulties reliably discriminating true from false protein complex components, identifying post-translational modifications
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