Key features and details
- PE Rabbit monoclonal [EP2102Y] to cAMP Protein Kinase Catalytic subunit
- Suitable for: Flow Cyt
- Reacts with: Human
- Conjugation: PE. Ex: 488nm, Em: 575nm
Product namePE Anti-cAMP Protein Kinase Catalytic subunit antibody [EP2102Y]
See all cAMP Protein Kinase Catalytic subunit primary antibodies
DescriptionPE Rabbit monoclonal [EP2102Y] to cAMP Protein Kinase Catalytic subunit
ConjugationPE. Ex: 488nm, Em: 575nm
Tested applicationsSuitable for: Flow Cytmore details
Species reactivityReacts with: Human
Synthetic peptide within Human cAMP Protein Kinase Catalytic subunit aa 300-400 (C terminal). The exact sequence is proprietary.
- Flow Cyt: MCF7 cells.
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at +4°C. Store In the Dark.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 1% BSA, PBS
Concentration information loading...
PurityProtein A purified
- Pathways and Processes
- Metabolic signaling pathways
- Lipid and lipoprotein metabolism
- Lipid metabolism
Our Abpromise guarantee covers the use of ab252099 in the following tested applications.
FunctionPhosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation.
Tissue specificityIsoform 1 is ubiquitous. Isoform 2 is sperm-specific and is enriched in pachytene spermatocytes but is not detected in round spermatids.
Sequence similaritiesBelongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.
Contains 1 AGC-kinase C-terminal domain.
Contains 1 protein kinase domain.
modificationsAsn-3 is partially deaminated to Asp giving rise to 2 major isoelectric variants, called CB and CA respectively.
Autophosphorylated. Phosphorylation is enhanced by vitamin K(2). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity.
Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficienncy.
Cellular localizationCytoplasm. Cell membrane. Nucleus. Mitochondrion. Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes and Cell projection, cilium, flagellum. Expressed in the midpiece region of the sperm flagellum.
- Information by UniProt
- cAMP dependent protein kinase alpha catalytic subunit antibody
- cAMP dependent protein kinase beta catalytic subunit antibody
- cAMP dependent protein kinase catalytic beta subunit isoform 4ab antibody
Overlay histogram showing MCF7 cells stained with ab252099 (red line). The cells were fixed with 80 % methanol (5 min) and then permeabilized with 0.1 % PBS-Triton X-100 for 15 min. The cells were incubated in 1x PBS containing 10 % normal goat serum to block non-specific protein-protein interaction followed by the antibody (ab252099) (1x 106 in 100µl at 0.5 µg/ml (1/1000)) for 30 min at 22°C.
Isotype control antibody (black line) was Rabbit IgG (monoclonal) Phycoerythrin (ab209478) used at the same concentration and conditions as the primary antibody. Unlabelled sample (blue line) was also used as a control.
Acquisition of >5,000 events were collected using a 50 mW Yellow/Green laser (561nm) and 586/15 bandpass filter.
This antibody gave a positive signal in MCF7 cells fixed with 4 % formaldehyde (10 min) / permeabilized with 0.1 % PBS-Triton X-100 for 15 min used under the same conditions.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab252099 has not yet been referenced specifically in any publications.