PRKAR1B Mouse Monoclonal Antibody (M05), clone 1F8
- Known as:
- PRKAR1B Mouse Monoclonal Antibody (M05), clonality 1F8
- Catalog number:
- CEL-005575-M05
- Product Quantity:
- 0.05mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- PRKAR1B Mouse Monoclonal Antibody (M05) clone 1F8
Related genes to: PRKAR1B Mouse Monoclonal Antibody (M05), clone 1F8
- Gene:
- GATAD1 NIH gene
- Name:
- GATA zinc finger domain containing 1
- Previous symbol:
- -
- Synonyms:
- ODAG, RG083M05.2, FLJ22489
- Chromosome:
- 7q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-03-31
- Date modifiied:
- 2019-04-23
- Gene:
- LRRC17 NIH gene
- Name:
- leucine rich repeat containing 17
- Previous symbol:
- -
- Synonyms:
- P37NB, H_RG318M05.3
- Chromosome:
- 7q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-08-07
- Date modifiied:
- 2014-11-18
- Gene:
- PRKAR1B NIH gene
- Name:
- protein kinase cAMP-dependent type I regulatory subunit beta
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 7p22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-17
- Date modifiied:
- 2016-01-27
- Gene:
- TJP1 NIH gene
- Name:
- tight junction protein 1
- Previous symbol:
- -
- Synonyms:
- ZO-1, MGC133289, DKFZp686M05161
- Chromosome:
- 15q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-04-26
- Date modifiied:
- 2016-10-05
Related products to: PRKAR1B Mouse Monoclonal Antibody (M05), clone 1F8
Related articles to: PRKAR1B Mouse Monoclonal Antibody (M05), clone 1F8
- Head and neck squamous cell carcinoma (HNSC) is one of the most prevalent malignancies worldwide. PRKAR1B, a regulatory component of protein kinase A (PKA), has been widely investigated for its potential involvement in tumorigenesis across different diseases. However, its specific role in HNSC remains elusive. In this study, significant differences in PRKAR1B expression were observed across various cancer types. PRKAR1B was highly expressed in HNSC and was strongly associated with poor prognosis in HNSC patients. Moreover, it was identified as an independent prognostic factor significantly associated with clinical parameters. Correlation analysis revealed that PRKAR1B expression was associated with genes such as C7orf50, EIF3B, TBRG4, DDX56, and BRAT1. Additionally, it was associated with TMB and was correlated with the infiltration of immune cells such as M1 macrophages, activated mast cells, and eosinophils. Notably, PRKAR1B was identified as a predictive marker for the efficacy of CTLA-4 inhibitors, with high PRKAR1B expression potentially conferring superior therapeutic responses. Drug sensitivity analysis further suggested that Lapatinib and Erlotinib may be beneficial in HNSC patients with high PRKAR1B expression. Meanwhile, experiments showed that PRKAR1B knockdown inhibited HNSC cell proliferation and migration. Lastly, PRKAR1B protein expression was upregulated in clinical HNSC samples. Overall, this study thoroughly examined PRKAR1B expression and its prognostic significance in HNSC, investigated related molecular pathways and immune cell interactions, and validated its role via experiments. - Source: PubMed
Publication date: 2026/02/20
Zhao PengLi KangXiu WuFengLiu ZhaokunHuang YanxiaoJiang YoufangZhang PengPeng Lixiang - Proteins can be denatured and precipitated under different denaturation conditions, and ligand bound proteins are more resistant to denaturing induced precipitation. Consequently, ligand target proteins can be identified by measuring solubility shifts. Nowadays, numerous methods have been developed to screen ligand target proteins based on different denaturation mechanisms. However, due to the different responses of proteins to different denaturation conditions, there is a significant complementary between these methods. Direct pooling of the denatured supernatants from different denaturation strategies can utilize this complementary, however, the pooling procedure inevitably averages the ligand-induced solubility shift across conditions, significantly compromising target identification sensitivity. - Source: PubMed
Publication date: 2025/09/29
Ma YanniZhang XiaoleiShi LongrunYan JiayangWang KeyunYe Mingliang - Marbach-Schaaf neurodevelopmental syndrome (MASNS) is an ultra-rare, monogenic disease caused by pathogenic variation in PRKAR1B, which codes for the R1β regulatory subunit of protein kinase A (PKA), a key effector of cAMP signaling within the nervous system. This work provides a comprehensive clinical description of 12 subjects with pathogenic PRKAR1B variants, including two individuals with a heterozygous deletion including PRKAR1B, supporting haploinsufficiency as a possible mechanism of disease. Phenotypic information was obtained by interview, using a systematic multi-dimensional questionnaire. Besides expanding the evidence for established MASNS phenotypes like developmental delay, ID, ASD, pain insensitivity, as well as mild dysmorphisms, we broaden the clinical spectrum through the description of new and underreported findings, in particular increased body weight. In addition, the presence of genomic deletions suggests dosage sensitivity of PRKAR1B, demonstrating that both sequence and copy number variants should be considered in diagnostic testing. This work gives valuable insight into the pathophysiology of MASNS and sets a framework upon which to design future mechanistic studies of PKA signaling in brain development. - Source: PubMed
Publication date: 2025/10/29
Burkart SebastianGuzeloglu TarikSoares Ana RValenzuela IreneTizzano Eduardo FGómez-Andres DavidPasquier LaurentLegendre MarineBerges CamilleThevenon JulienGauthier MarjolaineHeid CalebRanum EllyShen JosephFrees MichelleSchmidtke Michael WPilar CaroSchaaf Christian P - Many transcript isoforms generated by intronic polyadenylation (IPA) encode isoforms of canonical proteins. Microproteins are an emerging class of small proteins translated from small open reading frames (sORFs) in noncoding RNAs and mRNAs, but their production by IPA isoforms is unknown. - Source: PubMed
Publication date: 2025/10/23
Devaux AlexandreTanaka IrisFouilleul QuentinHeneman-Masurel AmélieCadix MandyMichallet SophieChakraborty AlinaLabbé Céline MFontrodona NicolasSahoo SubhadarsiniClaude Jean-BaptisteDeloger MarcGestraud PierreTessier LudovicMortada HusseinLameiras SoniaRaynal VirginieBaulande SylvainServant NicolasAuboeuf DidierEymin BéatriceVagner StéphanDutertre Martin - The RIβ subunit of cAMP-dependent protein kinase (PKA) is highly expressed in the brain, yet it remains the least studied of the PKA regulatory subunits (R). As pathologic variants of its gene are increasingly implicated in neurodevelopmental disorders, neurodegeneration, and cancer, gaining more information about the structure/function of RIβ, and how it differs from RIα, has become increasingly important. We previously reported the structure of the RIβC holoenzyme, which revealed a novel conformation where ATP binding was stabilized by a head-to-head anti-parallel packing of the C-tail wrapped around the N-lobe of the catalytic subunit (C). Although visible, the Dimerization/Docking Domain was poorly folded and reduced. Since RIβ is oxidized in brain tissues, we asked if oxidation or binding of an A Kinase Anchoring Protein (AKAP) would affect the holoenzyme structure. Oxidation or addition of an AKAP peptide to crystals led to the release of nucleotide. To capture this at higher resolution we crystallized RIβC in the presence of an AKAP peptide. This new structure represents an RIβ:C heterodimer. Density for the D/D domain was missing; ATP was absent, the kinase adopted an open conformation, and the C-terminus of the RIβ subunit was no longer resolved. Because the crosstalk between ATP and cAMP in the R:C complex appears to be mediated by the two N3A motifs (N3A and N3A) as well as by the linker, which in free RIβ is intrinsically disordered, we describe the conserved features of these two motifs as well as the linker and show how each contributes in a unique but coordinated way to allosteric activation of RIβ holoenzymes by cAMP. A key difference in our RIβ:C structure is the rotation of the side chain of W260 at the N-terminus of the αA Helix in N3A. W260, at the R:C interface in the holoenzyme, is also the capping residue for cAMP bound to CNB-A, so we may have actually captured the first step in cAMP activation. - Source: PubMed
Wu JianBruystens Jessica G HSahoo PuspashreeBubis JoséMaillard Rodrigo ATaylor Susan SIlouz Ronit