Saltar al contenido
Merck

P2014

Sigma-Aldrich

Phosphorylase Kinase from rabbit muscle

lyophilized powder, ≥60 units/mg protein

Sinónimos:

ATP:phosphorylase-b phosphotransferase, Dephosphophosphorylase kinase

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

Número de CAS:
Comisión internacional de enzimas:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

Formulario

lyophilized powder

actividad específica

≥60 units/mg protein

composición

Protein, 20-40% biuret

actividad extraña

ATPase ≤0.5%
phosphorylase a ≤1%
phosphorylase b ≤5%

temp. de almacenamiento

−20°C

Descripción general

Phosphorylase kinase contains four subunits each containing an α, β, γ, and sigma component. The sigma component binds 4 calcium molecules and is termed calmodulin while the γ unit acts as the catalytic subunit.

Aplicación

Phosphorylase kinase from rabbit muscle has been used in a study to assess features of glycogen phosphorylase. It has also been used in a study to investigate the activation of different forms of muscle phosphorylase kinase by actin.

Definición de unidad

One unit will form 1.0 μmolar unit of phosphorylase a from phosphorylase b per min at pH 7.7 at 30°C in the presence of ATP.

Forma física

Lyophilized powder containing (NH4)2SO4, sucrose, β-glycerophosphate and dithioerythritol

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


Elija entre una de las versiones más recientes:

Certificados de análisis (COA)

Lot/Batch Number

¿No ve la versión correcta?

Si necesita una versión concreta, puede buscar un certificado específico por el número de lote.

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

G Kamp
Biological chemistry Hoppe-Seyler, 367(2), 109-117 (1986-02-01)
The activities of glycogen phosphorylases a and b from the body wall musculature of the marine worm Arenicola marina (Annelida, Polychaeta) were determined after various periods of anoxia. Already under normoxic conditions one third of the total activity was produced
M Amin-ul Mannan et al.
Journal of molecular biology, 425(12), 2083-2099 (2013-04-02)
The endoplasmic reticulum transmembrane receptor Ire1 senses over-accumulation of unfolded proteins in the endoplasmic reticulum and initiates the unfolded protein response (UPR). The cytoplasmic portion of Ire1 has a protein kinase domain (KD) and a kinase extension nuclease (KEN) domain
Kathryn A Skelding et al.
Advances in experimental medicine and biology, 740, 703-730 (2012-03-29)
Calcium/calmodulin-stimulated protein kinases can be classified as one of two types - restricted or multifunctional. This family of kinases contains several structural similarities: all possess a calmodulin binding motif and an autoinhibitory region. In addition, all of the calcium/calmodulin-stimulated protein
Thomas P Howard et al.
Plant signaling & behavior, 6(12), 2026-2030 (2011-11-25)
The chloroplast protein CP12 forms a multi-enzyme complex with the Calvin-Benson cycle enzymes phosphoribulokinase (PRK) and NADP-glyceraldehyde-3-phosphate dehydrogenase (GAPDH). PRK and GAPDH are inactivated when present in this complex, a process shown in vitro to be dependent upon oxidized CP12.
S Camus et al.
Oncogene, 31(39), 4333-4342 (2011-12-20)
Angiogenesis is essential for development and tumor progression. With the aim of identifying new compound inhibitors of the angiogenesis process, we used an established enhanced green fluorescent protein-transgenic zebrafish line to develop an automated assay that enables high-throughput screening of

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico