P2363
Protein Kinase G II from rat
>90% (SDS-PAGE), recombinant, expressed in baculovirus infected Sf9 cells, solution
Synonyme(s) :
Protein Kinase, 3′,5′-Cyclic GMP Dependent from rat
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About This Item
Produits recommandés
Produit recombinant
expressed in baculovirus infected Sf9 cells
Niveau de qualité
Essai
>90% (SDS-PAGE)
Forme
solution
Activité spécifique
~0.7 U/mg
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Informations sur le gène
rat ... Prkg2(25523)
Description générale
Protein kinase, cGMP-dependent, type II (PRKG2), also known as type II cGMP-dependent protein kinase (cGK), is encoded by the gene mapped to human chromosome 4q13.1–q21.1.
Actions biochimiques/physiologiques
Protein kinase, cGMP-dependent, type II (PRKG2) is implicated in the regulation of intestinal fluid balance in man. The encoded protein plays an essential role in proliferative to hypertrophic transition of growth plate chondrocytes during endochondral ossification. Loss of PRKG2 function is associated with the development of renal cysts, intellectual disability and speech defect. In rodent and bovine models, deletion of the gene leads to dwarfism.
Définition de l'unité
One unit will phosphorylate one μmole of VASPtide (RRKVSKQE) per minute at pH 7.4
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Further defining the critical genes for the 4q21 microdeletion disorder
Hu X, et al.
American Journal of Medical Genetics. Part A, 120-125 null
Functional Analysis of Phenotypic Behaviors of a 5-Year-Old Male with Novel 4q21 Microdeletion
Fee A, et al.
ournal of Pediatric Neuropsychology,, 36-41 null
Transcriptional profiling of PRKG2-null growth plate identifies putative down-stream targets of PRKG2
Koltes JE, et al.
BMC Research Notes, 177 null
Characterization of the Gene Encoding the Human Type II cGMP-Dependent Protein Kinase (PRKG2)
Witczak O, et al.
Biochemical and Biophysical Research Communications, 113-119 null
D Pöhler et al.
FEBS letters, 374(3), 419-425 (1995-11-06)
Detailed studies of differences in distinct cGMP kinase isoforms are highly dependent on expression of large amounts of these enzyme isoforms that are not easily purified by conventional methods. Here cGMP-dependent protein kinases, the type I beta soluble form from
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