Abcam, ab5816, Anti-PKA beta (catalytic subunit) (phospho S338) antibody

Size: 50µL
Rabbit Polyclonal PKA beta (catalytic subunit) phospho S338 antibody. Suitable for WB and reacts with Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human cAMP-dependent protein kinase catalytic subunit beta phospho S338.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse,
Applications:WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human cAMP-dependent protein kinase catalytic subunit beta phospho S338. The exact immunogen used to generate this antibody is proprietary information.P22694,
Specificity:Peptide competition data indicate that this antibody cross-reacts with the PKA nu subunit (64% homologous) and partially with the alpha subunit (82% homologous).

Product details:
c-AMP-dependent Protein Kinase (PKA) is a serine/threonine kinase that regulates a number of cellular processes including proliferation, ion transport and gene transcription. PKA is composed of conserved catalytic subunits and regulatory subunits that dissociate upon activation by cAMP. The catalytic subunit of PKA contains the activation loop and mediates DNA binding and substrate recognition. The catalytic subunit is assembled and expressed as an active form and is phosphorylated on threonine 197 by PDK 1 in the activation loop and serine 338 in the carboxyl terminus. Phosphorylation of serine 338 plays a key role in stabilizing PKA and activating its substrates, and hence mediating its biological functions.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Purification notes-The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated PKA. The final product is generated by affinity chromatography using a PKA-derived peptide that is phosphorylated at serine 338., Storage buffer-pH: 7.3Preservative: 0.05% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), 0.1% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The PKA beta (catalytic subunit) also known as PRKACB or Protein Kinase A catalytic subunit beta plays a pivotal role in cellular signaling mechanisms. Mechanically it catalyzes the transfer of a phosphate group from ATP to a serine or threonine residue in target proteins impacting various cellular processes. This catalytic subunit has a molecular weight of approximately 40 kDa. It expresses widely in many tissues including the brain heart and skeletal muscle where it contributes to regulating metabolic and transcriptional activities.
Biological function summary
The PKA beta catalytic subunit functions in a larger context as part of the Protein Kinase A (PKA) complex which is a central player in the cyclic AMP (cAMP) signaling pathway. This complex acts as an effector of cAMP translating extracellular signals into intracellular actions by phosphorylating a wide range of target proteins. As a part of this complex it modulates activities related to glucose metabolism cell proliferation and gene expression reflecting its involvement in many cellular processes.
Pathways
PKA beta is integrally involved in the cAMP signaling and insulin signaling pathways. In the cAMP pathway it activates by binding to cAMP leading to dissociation from regulatory subunits and subsequent activation of substrate proteins. In the insulin signaling pathway it interacts with proteins like PI3K and Akt playing an important role in regulating glucose homeostasis and lipid metabolism. These pathways illustrate the PKA beta's importance in maintaining cellular and systemic metabolic balance.
The dysfunction of PKA beta is associated with conditions such as cardiac hypertrophy and certain types of cancer. Elevations or disruptions in PKA beta activity can lead to alterations in cell growth and metabolic regulation. PKA beta's relationship with proteins like CREB and Bcl-2 through these disorders has been observed where aberrant phosphorylation mediated by PKA can drive pathological cell survival proliferation and growth linking malfunction directly to disease progression.