CBL兔单克隆抗体[YE323](ab32027)可与人样本反应并经WB, IP, ICC, Flow Cyt实验严格验证，被5篇文献引用。所有产品均提供质保服务，中国75%以上现货。

Complete information for CBL gene (Protein Coding), Cbl Proto-Oncogene, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

CBL R343* results in a premature truncation of the Cbl protein at amino acid 343 of 906 (UniProt.org). R343* has not been characterized however, due to the effects of other truncation mutations downstream of R343 (PMID: 23744067, PMID: 10617633), R343* is predicted to lead to a loss of Cbl protein function ...

PŘEHLEDOVÝ ČLÁNEK Lynchův syndrom v rukách patologa Ondřej Daum 1, Zdeněk Beneš 2, Ladislav Hadravský 1, Jan Stehlík 3, Kateřina Černá 3, Martin Dušek 1,3, Bohuslava Kokošková 1, Michal Michal 1,3 1 Šiklův

Türkiye Klinikleri Psikiyatri - Özel Konular Arşivi Kişilerarası İlişkiler Psikoterapisi, Nazan Aydın, Oğuz Omay, Editör, dijital akademi türkiye klinikleri, Ankara, ss.25-31, 2019 ...

T cell (TC) activation requires the coordinated signaling of the T cell receptor (TCR) and coreceptor molecules, allowing TCs to respond to lower degrees of TCR occupancy. Coreceptor molecules set the threshold for TC activation by controlling different regulatory signaling loops. The Cbl family members prevent undesired activation of T cells by regulating TCR signals. In this report, we show that TC prestimulation by the CD43 coreceptor molecule before TCR engagement inhibits TCR-dependent c-Cbl tyrosine phosphorylation, c-Cbl interaction with the adapter molecule Crk-L and promotes Cbl-b degradation in a PKCθ-dependent manner. Consequently, the prolonged tyrosine phosphorylation and delayed degradation of ZAP-70 and of the ζ chain lead to enhanced mitogen-activated protein kinase activation and robust TC response. These data indicates that CD43-mediated signals lower the threshold for TC activation by restricting the c-Cbl and Cbl-b inhibitory effects on TCR signaling. In addition to the strength

TY - JOUR. T1 - The protooncogene product, PEBP2β/CBFβ, is mainly located in the cytoplasm and has an affinity with cytoskeletal structures. AU - Tanaka, Yuta. AU - Watanabe, Toshio. AU - Chiba, Natsuko. AU - Niki, Masaru. AU - Kuroiwa, Yasuyuki. AU - Nishihira, Tetsuro. AU - Satomi, Susumu. AU - Ito, Yoshiaki. AU - Satake, Masanobu. N1 - Funding Information: We thank Ms I Imamura for secretarial assistance. This investigation was supported in part by research grants from the Ministry of Education, Science and Culture of Japan, Proposal-Based Advanced Industrial Technology R&D Program, Takeda Science Foundation, The Ryoichi Naito Foundation for Medical Research, The Mochida Memorial Foundation for Medical and Pharmaceutical Research, Uehara Memorial Foundation and The Naito Foundation.. PY - 1997. Y1 - 1997. N2 - The Pebpb2/Cbfb gene encodes the non-DNA binding β subunit of the heterodimeric transcription factor, PEBP2/CBF, and has been implicated in a subtype of human acute myeloid leukemia, ...

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Polyclonal antibody for C CBL/CBL detection. Host: Rabbit.Size: 100μg/vial. Tested applications: WB. Reactive species: Human. C CBL/CBL information: Molecular Weight: 99633 MW; Subcellular Localization: Cytoplasm. Cell membrane. Colocalizes with FGFR2 in

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We used the L858R and L861Q EGFR mutants in this report. L858R is one of the two most common EGFR mutations detected in NSCLC ( 12). L861Q was identified by a mutagenesis screen in mice; this mutant EGFR exhibits increased tyrosine kinase activity and steady-state lower protein levels compared with WT receptor ( 33). The location of both L861Q and L858R is juxtaposed with each other in the activation loop, which provides the platform for kinase substrate(s) and modulates the catalytic activity of kinase by promoting a conformational change ( 34). Furthermore, oncogenic mutations in other RTKs involve an amino acid residue to the L861 of EGFR ( 35, 36). We observed ligand-independent phosphorylation of mutant EGFRs ( Fig. 1), suggesting that the mutants turn on survival signal transduction pathways, such as AKT in a ligand-independent manner. However, the oncogenic signals generated by the EGFR mutants were not sufficient for sustained growth of 32D cells in the absence of serum with or without ...

CBL - CBL Mutant (G397V), Myc-DDK-tagged ORF clone of Homo sapiens Cas-Br-M (murine) ecotropic retroviral transforming sequence (CBL) as transfection-ready DNA available for purchase from OriGene - Your Gene Company.

CBL G413R lies within the RING-type zinc finger domain of the Cbl protein (UniProt.org). C413R is predicted to disrupt Cbl stability by computational modeling (PMID: 26676746), but has not been biochemically characterized and therefore, its effect on Cbl protein function is unknown (PubMed, Jul 2020 ...

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Funding period: 2014. Project summary In acute myeloid leukaemia (AML), mutations to the FLT3 gene are strongly associated with a poor prognosis. While drugs that target this gene mutation are being trialled, over time AML cells appear to acquire gene mutations that allow them to resist the drugs.. Dr Carolyn Grove from the University of Western Australia is assessing another potential treatment that could increase the effectiveness of anti-FLT3 drugs. From preliminary research, Dr Grove has evidence that enhancing the activity of the c-Cbl gene product could provide a new treatment approach for patients with AML.. c-CBL codes for the cell signalling protein CBL and mutations to this gene are also implicated in AML development.. Were using laboratory models to test the possibility of treating acute myeloid leukaemia with drugs that activate the protein produced by the c-Cbl gene, said Dr Grove.. The results could lead to a new therapeutic approach for treating myeloid leukaemias as well as ...

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Aim: Development of monoclonal and polyclonal antibodies against recombinant GST-fused proteins including correspondingly N- and C-terminal parts of Ruk/CIN85

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CBLs determine the cellular localization of their interacting protein kinases (DAngelo et al., 2006; Xu et al., 2006; Cheong et al., 2007). The resulting CBL/CIPK complexes exert important functions at the plasma membrane by regulating the activity of ion channels and H+-ATPases (Xu et al., 2006; Fuglsang et al., 2007). The aims of this study were to investigate the potential dual lipid modification of CBL proteins by myristoylation and acylation and to unravel the influence of these lipid modifications on the functional regulation of processes decoding calcium signals. Our studies identify myristoylation and S-acylation by palmitic and stearic acids as essential modifications for calcium sensor function and report novel steps in the plasma membrane transport of acylated CBL proteins and in the membrane targeting of CBL/CIPK complexes. Importantly, our observation that the lipid modification status of the CBL protein determines the targeting of preassembled CBL/CIPK complexes provides a novel ...

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