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P2363

Sigma-Aldrich

Protein Kinase G II from rat

>90% (SDS-PAGE), recombinant, expressed in baculovirus infected Sf9 cells, solution

Synonym(s):

Protein Kinase, 3′,5′-Cyclic GMP Dependent from rat

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About This Item

MDL number:
UNSPSC Code:
41106305
NACRES:
NA.32

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

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
Further defining the critical genes for the 4q21 microdeletion disorder
Hu X, et al.
American Journal of Medical Genetics. Part A, 120-125 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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