P2645
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)
Synonyme(s) :
PKA
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About This Item
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.32
Produits recommandés
Forme
lyophilized (white powder to sticky mass to hard pellet)
Niveau de qualité
Activité spécifique
≥9 units/μg protein (cyclic-AMP is not required for this activity)
Poids mol.
40,862 Da
Température de stockage
−20°C
Description générale
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.
Application
Protein Kinase A (PKA) Catalytic Subunit from bovine heart has been used-
- to study PKA-mediated inhibition of IRK1 (inwardly rectifying K+) channels
- in in Vitro PKA pPhosphorylation assay
- in Vitro affinity binding assays
- to study effects of PKA on inspiratory drive currents in functionally active motorneurons
Actions biochimiques/physiologiques
Protein Kinase A (PKA) controls the transduction of Hedgehog signaling and participates in proliferation and fate specification. It phosphorylates several neurotransmitter receptors, transcription factors and constituents of various intracellular signaling pathways.
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.
Conditionnement
Package size based on phosphorylating units
Définition de l'unité
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.
Forme physique
Lyophilized powder with sucrose and phosphate buffer salts as stabilizer.
Notes préparatoires
Prepared from protein kinase A (P 5511)
Clause de non-responsabilité
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.
Inhibiteur
Réf. du produit
Description
Tarif
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
Cyclic nucleotides in the nervous system
Basic Neurochemistry, 423-441 (2012)
F T Hartl et al.
The Journal of biological chemistry, 258(6), 3950-3955 (1983-03-25)
The physical and chemical properties of purified catalytic and regulatory subunits of type II cAMP-dependent protein kinase from bovine brain, skeletal muscle, and cardiac muscle were compared. The catalytic subunits from all three sources were identical with respect to molecular
Ken Tougane et al.
Plant physiology, 152(3), 1529-1543 (2010-01-26)
Abscisic acid (ABA) is postulated to be a ubiquitous hormone that plays a central role in seed development and responses to environmental stresses of vascular plants. However, in liverworts (Marchantiophyta), which represent the oldest extant lineage of land plants, the
Christopher M Bocchiaro et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 23(4), 1099-1103 (2003-02-25)
Plasticity underlying adaptive, long-term changes in breathing behavior is hypothesized to be attributable to the modulation of respiratory motoneurons by intracellular second-messenger cascades. In quiescent preparations, protein kinases, including cAMP-dependent protein kinase A (PKA), potentiate glutamatergic inputs. However, the dynamic
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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