Protein Kinase A regulatory subunit I alpha Antibody (N-term) Blocking peptide
€363.00
In stock
SKU
AC-BP8095a
Background:
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK 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 of AMPK have been identified in humans. PKR1 is one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Functional null mutations in the gene cause Carney complex (CNC), an autosomal dominant multiple neoplasia syndrome. The gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2.
Other Names:
cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed, PRKAR1A, PKR1, PRKAR1, TSE1
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP8095a was selected from the N-term region of human PKR1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: PRKAR1A
Gene ID: 5573
Primary Accession: P10644
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 (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK 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 of AMPK have been identified in humans. PKR1 is one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Functional null mutations in the gene cause Carney complex (CNC), an autosomal dominant multiple neoplasia syndrome. The gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2.
Other Names:
cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed, PRKAR1A, PKR1, PRKAR1, TSE1
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP8095a was selected from the N-term region of human PKR1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: PRKAR1A
Gene ID: 5573
Primary Accession: P10644
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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