PKA 2 beta (PRKAR2B) Antibody (N-term) Blocking peptide
€363.00
In stock
SKU
AC-BP7052a
Background:
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol.
Other Names:
cAMP-dependent protein kinase type II-beta regulatory subunit, PRKAR2B
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP7052a was selected from the N-term region of human PRKAR2B . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: PRKAR2B
Gene ID: 5577
Primary Accession: P31323
Other Accession: KAP3_HUMAN
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol.
Other Names:
cAMP-dependent protein kinase type II-beta regulatory subunit, PRKAR2B
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP7052a was selected from the N-term region of human PRKAR2B . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: PRKAR2B
Gene ID: 5577
Primary Accession: P31323
Other Accession: KAP3_HUMAN
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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