PRKAR2B antibody (pSer114) (Alexa Fluor 488)

Catalog No. ABIN1177142

There are 2+ publications for this product available. The Mouse Monoclonal anti-PRKAR2B antibody is suitable to detect PRKAR2B in samples from Human, Mouse and Rat. It has been validated for ICS.

Quick Overview for PRKAR2B antibody (pSer114) (Alexa Fluor 488) (ABIN1177142)

Target: PRKAR2B (Protein Kinase, CAMP-Dependent, Regulatory, Type II, beta (PRKAR2B))

Reactivity: Human, Mouse, Rat

Host: Mouse

Clonality: Monoclonal

Conjugate: This PRKAR2B antibody is conjugated to Alexa Fluor 488

Application: Intracellular Staining (ICS)

Clone: 47-PKA

Product Details anti-PRKAR2B Antibody (Alexa Fluor 488)

Binding Specificity: pSer114

Brand: BD Phosflow™

Purification: The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

Immunogen: Phosphorylated Human PKA[RIIbeta] peptide Peptide

Isotype: IgG1 kappa

Application Details

Application Notes: Either BD Cytofix™ fixation buffer or BD™ Phosflow Fix Buffer I may be used for cell fixation. Any of the three BD™ Phosflow permeabilization buffers may be used.

Sample Volume: 20 μL

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Aqueous buffered solution containing BSA and ≤0.09 % sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: 4 °C

Storage Comment: The antibody was conjugated to Alexa Fluor® 647 under optimum conditions, and unreacted Alexa Fluor® 647 was removed. Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze.

References for anti-PRKAR2B antibody (Alexa Fluor 488) (ABIN1177142)

Elliott, Shanks, Khan, Brooks, Burkett, Nelson, Kyttaris, Juang, Tsokos, Kammer: "Down-regulation of IL-2 production in T lymphocytes by phosphorylated protein kinase A-RIIbeta." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 172, Issue 12, pp. 7804-12, (2004) (PubMed).

Budillon, Cereseto, Kondrashin, Nesterova, Merlo, Clair, Cho-Chung: "Point mutation of the autophosphorylation site or in the nuclear location signal causes protein kinase A RII beta regulatory subunit to lose its ability to revert transformed fibroblasts." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, Issue 23, pp. 10634-8, (1995) (PubMed).

Target Details for PRKAR2B

Target: PRKAR2B (Protein Kinase, CAMP-Dependent, Regulatory, Type II, beta (PRKAR2B))

Alternative Name: PKA RIIb

Background: CAMP-dependent Protein Kinase (PKA) is composed of two distinct subunits: catalytic (C) and regulatory (R). Four regulatory subunits have been identified: RIalpha, RIbeta, RIIalpha, and RIIbeta. These subunits define type I and II PKAs. Following binding of cAMP, the regulatory subunits dissociate from the catalytic subunits, rendering the enzyme active. Type I and type II holoenzymes have three potential C subunits (Calpha, Cbeta, or Cgamma). Most cells, including T lymphocytes, express both type I and type II PKAs. RIIa expression is associated with cellular transformation, while RIIbeta expression correlates with mitotic arrest and cellular differentiation. Type II PKA can be distinguished by autophosphorylation of the R subunits, while type I PKA binds Mg/ATP with high affinity. The cAMP-dependent autophosphorylation of the human RIIbeta subunits occurs at serine 114 (S114). In addition to their enzyme regulatory activity, the RIIalpha and RIIbeta subunits determine the subcellular location of the holoenzymes via their interactions with specific intracellular anchoring proteins. The 47/PKA monoclonal antibody recognizes the phosphorylated S114 in the RIIbeta subunit of PKA. The orthologous phosphorylation site in mouse and rat PKA[RIIbeta] is S112.
Synonyms: KAP3, PKAR2B, PRKAR2B

Pathways: Hedgehog Signaling, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Myometrial Relaxation and Contraction, M Phase, G-protein mediated Events, Interaction of EGFR with phospholipase C-gamma, SARS-CoV-2 Protein Interactome, The Global Phosphorylation Landscape of SARS-CoV-2 Infection