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SRP5120

Sigma-Aldrich

PRKAR1B, His tagged human

recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

PRKAR1

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

~52 kDa

NCBI accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PRKAR1B(5575)

General description

PRKAR1B is the type I-beta regulatory subunit of cyclic AMP-dependent protein kinase A (PKA) which is an essential enzyme in the cAMP signaling pathway. PKA holoenzyme is composed of 2 regulatory and 2 catalytic subunits and dissociates from the regulatory subunits upon binding of cAMP. PKA controls many biochemical events in the cell including regulation of metabolism, ion transport, and gene transcription. PKA undergoes a dramatic conformational change upon complex formation with the catalytic subunit. PRKAR1B subunits can dimerize through an N-terminal motif and this dimerization is necessary for binding to PKA anchoring proteins (AKAPs) and targeting of PKA to its site of action.

Physical form

Supplied in 50mM sodium phosphate, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.

Preparation Note

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Storage Class

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Cathrine R Carlson et al.
Journal of molecular biology, 327(3), 609-618 (2003-03-14)
Protein kinase A (PKA) regulatory (R) subunits dimerize through an N-terminal motif. Such dimerization is necessary for binding to PKA anchoring proteins (AKAPs) and targeting of PKA to its site of action. In the present study, we used the yeast

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