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  • mProX™ Human PRKACA Stable Cell Line

    [CAT#: S01YF-1023-PY58]
    Product Category:
    Membrane Protein Stable Cell Lines
    Subcategory:
    Kinase Cell Lines

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    Based on this stable cell line, we also provide cell-based in vitro assays to evaluate the effects of your compounds or antibodies.

    Sub Cat Product Name Target Protein Species Host Cell Type Assay Types Inquiry Datasheet
    S01YF-1222-KX437 Magic™ Human PKACα(PRKACA) in Vitro Assay Human Kinase Assay

    Product Information

    Target Family
    Kinases/Enzyme
    Target Protein Species
    Human
    Host Cell Type
    HEK293;CHO-K1
    Target Classification
    Kinase Cell Lines
    Target Research Area
    Cardiovascular Research
    Related Diseases
    Cardioacrofacial Dysplasia 1; Pigmented Nodular Adrenocortical Disease, Primary, 4
    Gene ID
    Human:5566
    UniProt ID
    Human:P17612

    Product Properties

    Biosafety Level
    Level 1
    Activity
    Yes
    Quantity
    10⁶ cells per vial
    Applications
    PRKACA is a gene that is involved in various biological processes and has implications in different diseases. In pancreatic and biliary neoplasms, PRKACA gene rearrangement and expression play a crucial role in the morpho-biology of oncocytic neoplasms. It is also associated with the development of subclonal oncocytic neoplasms and is strongly associated with oncocytic morphology. In small cell lung cancer, prolonged exposure to environmental concentrations of benzo[a]pyrene (BaP) promotes cancer stemness through the AhR/PKA/SOX2 pathway. Additionally, PRKACA is implicated in the regulation of the cytoskeleton and mitophagy in ischemic cardiomyopathy. Furthermore, PRKACA inhibitors have been discovered and synthesized, which selectively inhibit distinct classes of serine/threonine kinases. These findings provide insights into the role of PRKACA in different biological processes and diseases, and may have implications for potential therapeutic targets.

    Protocols

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    FAQ

    chat Casey Johnson (Verified Customer)

    Can the DNAJB1-PRKACA fusion protein be targeted in fibrolamellar hepatocellular carcinoma? Mar 05 2020

    chat Patrick Liam (Creative Biolabs Scientific Support)

    Yes, the DNAJB1-PRKACA fusion protein can be specifically targeted by peptide-based immunotherapy in fibrolamellar hepatocellular carcinoma. Mar 05 2020

    chat Taylor Williams (Verified Customer)

    Is PRKACA a viable therapeutic target for fibrolamellar carcinoma? Oct 24 2021

    chat Patrick Liam (Creative Biolabs Scientific Support)

    PRKACA is a viable therapeutic target for fibrolamellar carcinoma, as its inhibition results in cell death and tumor growth cessation. Oct 24 2021

    Published Data

    Fig.1 Knockdown of PRKACA in HEK293T-DP (DNAJB1-PRKACA fusion gene) cells.

    Following 48 and 72 hours of treatment, a substantial reduction in both PRKACA and DP protein levels was observed, effectively targeted by siRNA directed at PRKACA.

    Ref: Kim, Stephanie S., et al. "DNAJB1-PRKACA in HEK293T cells induces LINC00473 overexpression that depends on PKA signaling." Plos one 17.2 (2022): e0263829.

    Pubmed: 35167623

    DOI: 10.1371/journal.pone.0263829

    Research Highlights

    Cui, Can. et al. "Sesquiterpenoids from Alpinia oxyphylla with GLP-1 Stimulative Effects through Ca2+/CaMKII and PKA Pathways and Multiple-Enzyme Inhibition." Journal of agricultural and food chemistry, 2023.
    Researchers have identified six novel sesquiterpenoids (1-6) along with a pair of enantiomers (7a and 7b), as well as six previously known compounds (8-13) in Alpinia oxyphylla fruit extracts. The chemical structures of the new compounds were established through comprehensive spectroscopic analysis and ECD calculations. Significantly, the stereochemistry of 7a and 7b has been documented for the first time. These compounds demonstrated substantial GLP-1 stimulation in NCI-H716 cells, with stimulation ratios ranging from 90.4% to 668.9% at 50 μM. Further investigations revealed that compound 6 primarily enhanced GLP-1 secretion by regulating proglucagon transcription and processing, while compound 13 increased prkaca levels to exert its effects. Intriguingly, both compounds 6 and 13 were closely associated with Ca2+/CaMKII and PKA pathways in stimulating GLP-1 but had no relevance to TGR5 and GPR119 receptors. Additionally, most compounds exhibited inhibitory activity against α-glucosidase and PTP1B at concentrations of 100 and 200 μM, with no activity against GPa. Compounds 3, 9, 11, and 13 effectively suppressed α-glucosidase, displaying IC50 values comparable to acarbose (IC50 = 212.0 μM). This study underscores the rich diversity of sesquiterpenoids in A. oxyphylla with multifaceted biological activities.
    Cui, Can. et al. "Sesquiterpenoids from Alpinia oxyphylla with GLP-1 Stimulative Effects through Ca2+/CaMKII and PKA Pathways and Multiple-Enzyme Inhibition." Journal of agricultural and food chemistry, 2023.
    Pubmed: 37871265   DOI: 10.1021/acs.jafc.3c06093

    Liu, Muyin. et al. "Integrative proteomic analysis reveals the cytoskeleton regulation and mitophagy difference between ischemic cardiomyopathy and dilated cardiomyopathy." Molecular & cellular proteomics : MCP, 2023.
    Ischemic cardiomyopathy (ICM) and dilated cardiomyopathy (DCM) represent the primary causes of end-stage heart failure. However, there is a significant lack of comprehensive understanding regarding the global proteome and phosphoproteome dynamics in ICM and DCM, hindering a deep grasp of their fundamental biological characteristics and signaling mechanisms. Through extensive high-throughput quantification proteomics and phosphoproteomics analyses of clinical heart tissues afflicted with ICM or DCM, researchers gained comprehensive molecular insights into the pathogenesis of heart failure in both conditions. This investigation unveiled distinct protein and phosphorylation expression patterns between heart failure and normal heart tissues, emphasizing the unique features of ICM and DCM. Notably, the study highlighted the activation of the PRKACA-GSK3β signaling pathway in ICM, impacting microtubule network remodeling and actin filament regulation. Additionally, DCM exhibited pronounced mitochondrial energy supply impairment compared to ICM, leading to ROCK1-vimentin signaling pathway activation and enhanced mitophagy. This research not only elucidates key distinctions between ICM and DCM but also sheds light on the differing underlying mechanisms, offering valuable insights for potential therapeutic targets in the treatment of various heart failure types.
    Liu, Muyin. et al. "Integrative proteomic analysis reveals the cytoskeleton regulation and mitophagy difference between ischemic cardiomyopathy and dilated cardiomyopathy." Molecular & cellular proteomics : MCP, 2023.
    Pubmed: 37852321   DOI: 10.1016/j.mcpro.2023.100667

    Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR CLINICAL PROCEDURES" For licensing inquiries, please contact
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