P2363
Protein Kinase G II from rat
>90% (SDS-PAGE), recombinant, expressed in baculovirus infected Sf9 cells, solution
Sinónimos:
Protein Kinase, 3′,5′-Cyclic GMP Dependent from rat
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About This Item
Productos recomendados
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
assay
>90% (SDS-PAGE)
form
solution
specific activity
~0.7 U/mg
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
rat ... Prkg2(25523)
General description
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.
Biochem/physiol Actions
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.
Unit Definition
One unit will phosphorylate one μmole of VASPtide (RRKVSKQE) per minute at pH 7.4
Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_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
Transcriptional profiling of PRKG2-null growth plate identifies putative down-stream targets of PRKG2
Koltes JE, et al.
BMC Research Notes, 177 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
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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