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P2645

Sigma-Aldrich

Protein Kinase A Catalytic Subunit from bovine heart

≥9 units/μg protein (cyclic-AMP is not required for this activity), lyophilized (white powder to sticky mass to hard pellet)

Sinonimo/i:

PKA

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About This Item

Classificazione EC (Enzyme Commission):
Numero MDL:
Codice UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.32
Prezzi e disponibilità al momento non sono disponibili

Stato

lyophilized (white powder to sticky mass to hard pellet)

Livello qualitativo

Attività specifica

≥9 units/μg protein (cyclic-AMP is not required for this activity)

PM

40,862 Da

Temperatura di conservazione

−20°C

Descrizione generale

Protein Kinase A enzyme is composed of two subunits- catalytic and regulatory. The catalytic subunit exists as a monomer in the presence of cAMP and has a molecular weight of 40,862 Da.[1][2]

Applicazioni

Protein Kinase A (PKA) Catalytic Subunit from bovine heart has been used-
  • to study PKA-mediated inhibition of IRK1 (inwardly rectifying K+) channels[3]
  • in in Vitro PKA pPhosphorylation assay[4]
  • in Vitro affinity binding assays[5]
  • to study effects of PKA on inspiratory drive currents in functionally active motorneurons[6]

Azioni biochim/fisiol

Protein Kinase A (PKA) controls the transduction of Hedgehog signaling and participates in proliferation and fate specification.[7] It phosphorylates several neurotransmitter receptors, transcription factors and constituents of various intracellular signaling pathways.[8]
Protein Kinase A catalyzes the transfer of terminal phosphate from ATP to threonine or serine residues present on various proteins. This protein is inactive in the absence of cAMP, where the catalytic and regulatory subunits are bound together. The regulatory subunit, in the presence of cAMP, binds to cAMP and releases the catalytic subunit.[9]

Confezionamento

Package size based on phosphorylating units

Definizione di unità

Phosphorylating Activity: One unit will transfer 1.0 picomole phosphate from ATP to hydrolyzed and partially dephosphorylated casein per minute at pH 6.5 at 30°C, determined by measuring the production of ADP.

Stato fisico

Lyophilized powder with sucrose and phosphate buffer salts as stabilizer.

Nota sulla preparazione

Prepared from protein kinase A (P 5511)

Esclusione di responsabilità

Please note that the pack size has been changed to align with the unit definition, while the number of phosphorylating units remain the same as before.

Inibitore

N° Catalogo
Descrizione
Determinazione del prezzo

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


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Petr G Vikhorev et al.
Cardiovascular research (2020-11-03)
Dilated cardiomyopathy (DCM) is associated with mutations in many genes encoding sarcomere proteins. Truncating mutations in the titin gene TTN are the most frequent. Proteomic and functional characterisations are required to elucidate the origin of the disease and the pathogenic
Protein kinase A activity and Hedgehog signaling pathway
Vitamins & Hormones, 88, 273-291 (2012)
J A Byun et al.
Science advances, 6(25), eabb1250-eabb1250 (2020-07-01)
The functional response of a signaling system to an allosteric stimulus often depends on subcellular conditions, a phenomenon known as pluripotent allostery. For example, a single allosteric modulator, Rp-cAMPS, of the prototypical protein kinase A (PKA) switches from antagonist to
Regions of the Escherichia coli primary sigma factor sigma70 that are involved in interaction with RNA polymerase core enzyme.
Nagai, et al.
Genes Cells, 2, 725-734 (2019)
E Wischmeyer et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(12), 5819-5823 (1996-06-11)
Strongly rectifying IRK-type inwardly rectifying K+ channels are involved in the control of neuronal excitability in the mammalian brain. Whole-cell patch-clamp experiments show that cloned rat IRK1 (Kir 2.1) channels, when heterologously expressed in mammalian COS-7 cells, are inhibited following

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