P9614
Lambda protein phosphatase
liquid, Bacteriophage Lambda, recombinant, expressed in E. coli
Sinonimo/i:
Lambda-PPase
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About This Item
Prodotti consigliati
Ricombinante
expressed in E. coli
Livello qualitativo
Forma fisica
liquid
PM
25 kDa
Concentrazione
≥400000 units/mL
Condizioni di spedizione
dry ice
Temperatura di conservazione
−70°C
Descrizione generale
Lambda protein phosphatase is a recombinant protein expressed in Escherichia coli. It requires Mn2+ or Ni2+ as activators.
Azioni biochim/fisiol
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.
Definizione di unità
One unit will hydrolyze 1 nanomole of p-nitrophenyl phosphate per min at pH 7.5 at 30 deg C.
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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I clienti hanno visto anche
Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.
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.
The Journal of Biological Chemistry, 285(53), 41993-42000 (2010)
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
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
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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