Overview of Signal Transduction

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Signal transduction research focuses on the molecular and biochemical pathways and mechanisms by which a cell responds to its environment. Surface receptor-ligand interactions cause biochemical changes inside the cell leading to a pre-determined response. Aggregation of receptors on the cell surface activates receptor-associated kinases and phosphatases and brings signaling molecules into proximity. The juxtaposition of signaling molecules causes the formation of second messengers such as cyclic AMP, cyclic GMP, inositol trisphosphate (IP3), and diacylglycerol (DAG), leading to activation of calcium-dependent pathways and protein kinase C. The ensuing cascade of molecular events lead to gene expression, cell division, activation of cell-specific functions, or cell death, Signal transduction depends heavily on protein-protein interactions and post-translational modifications such as phosphorylation, glycosylation and myristoylation.

Bethyl’s signal transduction portfolio contains more than 7,800 antibodies. These antibodies have been manufactured on-site by Bethyl scientists. Our rigorous validation process ensures that the antibody will work in the applications outlined on the datasheet. These applications include: Western blot, immunohistochemistry, immunoprecipitation, immunocytochemistry, flow cytometry, proximity ligation assay, and ChIP. A Bethyl antibody is first validated for specificity in immunoprecipitation and/or western blot and if it passes our team will validate the antibody for additional applications. Our products are backed with a 100% guarantee to work in your assay, when used in under the same conditions outlined on the product datasheet, which provides confident, reliable results.

Bethyl sells a wide variety of antibodies for signal transduction research. Recent publications using our antibodies for studying signal transduction include:

  • The identification of a novel mechanism for Pol II mediated transcriptional elongation through well-characterized signaling pathways associated with DNA damage1
  • Linking two known tumor suppressors through their respective signaling pathways that terminate with the induction of senescence2
  • Unwinding the tumor-causing potential of EGFR by better understanding its signaling mechanisms and the pathways by which it’s broken down3
  • How family of proteins targets a phosphorylation site after mitosis is triggered and leads to the initiation of translation4
  • How a transcriptional regulator known to impact cell proliferation is also responsible for the cellular response to DNA damage signals5

 

Localization of human RelA binding sites in immunoprecipitates from ependymona tumor by ChIP-Seq

Localization of human RelA binding sites in immunoprecipitates from ependymona tumor by ChIP-Seq. Antibody: Rabbit anti-RelA (A301-824A).

Detection of human CD247/CD3Z by WB of immunoprecipitates from HeLa lysate.

Detection of human CD247/CD3Z by WB of immunoprecipitates from HeLa lysate.  Antibodies: Rabbit anti- anti-CD247/CD3Z recombinant monoclonal [BL-336-1B2] (A700-017) and rabbit anti-CD247/CD3Z  (A305-170A & A305-212A). Secondary: ReliaBLOT® reagents (WB120).

Analysis of human p53 (A300-247A) Jurkat cells by flow cytometry using rabbit anti-p53 (A300-247A) and control rabbit IgG

Analysis of human p53 (A300-247A) (red) Jurkat cells by flow cytometry using rabbit anti-p53 (A300-247A) (red) and control rabbit IgG (black). Secondary: FITC-conjugated goat anti-rabbit IgG (A120-114F).

 

Below is the entire list of targets involved in signal transduction. Can’t find what you are looking for? Bethyl offers a custom antibody service.

 

References

1. Bunch H, Lawney BP, Lin YF, Asaithamby A, Murshid A, Wang YE, Chen BP, Calderwood SK. 2015. Transcriptional elongation requires DNA break-induced signalling. Nat Commun. 2015 Dec 16;6:10191. [Bethyl antibodies used: TRIM28 Antibody (A300-274A), Phospho TRIM28 Antibody (A300-767A). Please note that these antibodies have not been validated by Bethyl for use in ChIP and as such Bethyl cannot guarantee results as published in this paper.]

2. Ivanschitz L, Takahashi Y, Jollivet F, Ayrault O, Le Bras M, de Thé H. 2015. PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence. Proc Natl Acad Sci USA. Nov 17;112(46):14278-14283. [Bethyl antibody used: HdmX/MDM4 Antibody (A300-287A)]

3. Zhou L, Yang H. 2011. The von Hippel-Lindau tumor suppressor protein promotes c-Cbl-independent poly-ubiquitylation and degradation of the activated EGFR. PLoS One. Nov 2;6(9):e23936. [Bethyl antibodies used: EGFR Antibody (A300-387A & A300-388A)] 

4. Hutchinson JA, Shanware NP, Chang H, Tibbetts RS. 2011. Regulation of ribosomal protein S6 phosphorylation by casein kinase 1 and protein phosphatase 1. J Biol Chem. Mar 11;286(10):8688-8696. [Bethyl antibody used: CKI-delta Antibody (A302-136A)]

5. Eletr ZM, Yin L, Wilkinson KD. 2013. BAP1 is phosphorylated at serine 592 in S-phase following DNA damage. FEBS Lett. Dec 11;587(24):3906-3911. [Bethyl antibodies used: MEK1 Antibody (A302-140A), BAP1 Antibody (A302-243A), HCF-1 Antibody (A301-399A)]