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Rabbit Anti-Myc tag Polyclonal Antibody, Unconjugated

RRID:AB_307014

Antibody ID

AB_307014

Target Antigen

Myc tag

Proper Citation

(Abcam Cat# ab9106, RRID:AB_307014)

Clonality

polyclonal antibody

Comments

validation status unknown, seller recommendations provided in 2012: Electron Microscopy; ELISA; Immunofluorescence; Immunohistochemistry; Immunoprecipitation; Other; Western Blot; EM, Immunocytochemistry/Immunofluorescence, Immunohistochemistry-Fr, Immunohistochemistry-P, Immunoprecipitation, Western Blot

Host Organism

rabbit

Vendor

Abcam

Cat Num

ab9106

Publications that use this research resource

Amyloid-like aggregation of provasopressin in diabetes insipidus and secretory granule sorting.

  • Beuret N
  • BMC Biol.
  • 2017 Jan 26

Literature context:


Abstract:

BACKGROUND: Aggregation of peptide hormone precursors in the trans-Golgi network is an essential process in the biogenesis of secretory granules in endocrine cells. It has recently been proposed that this aggregation corresponds to the formation of functional amyloids. Our previous finding that dominant mutations in provasopressin, which cause cell degeneration and diabetes insipidus, prevent native folding and produce fibrillar aggregates in the endoplasmic reticulum (ER) might thus reflect mislocalized amyloid formation by sequences that evolved to mediate granule sorting. RESULTS: Here we identified two sequences responsible for fibrillar aggregation of mutant precursors in the ER: the N-terminal vasopressin nonapeptide and the C-terminal glycopeptide. To test their role in granule sorting, the glycopeptide was deleted and/or vasopressin mutated to inactivate ER aggregation while still permitting precursor folding and ER exit. These mutations strongly reduced sorting into granules and regulated secretion in endocrine AtT20 cells. CONCLUSION: The same sequences - vasopressin and the glycopeptide - mediate physiological aggregation of the wild-type hormone precursor into secretory granules and the pathological fibrillar aggregation of disease mutants in the ER. These findings support the amyloid hypothesis for secretory granule biogenesis.

Registered report: Kinase-dead BRAF and oncogenic RAS cooperate to drive tumor progression through CRAF.

  • Bhargava A
  • Elife
  • 2016 Feb 17

Literature context:


Abstract:

The Reproducibility Project: Cancer Biology seeks to address growing concerns about reproducibility in scientific research by conducting replications of selected experiments from a number of high-profile papers in the field of cancer biology. The papers, which were published between 2010 and 2012, were selected on the basis of citations and Altmetric scores (Errington et al., 2014). This Registered Report describes the proposed replication plan of key experiments from "Kinase-dead BRAF and oncogenic RAS cooperate to drive tumor progression through CRAF" by Heidorn and colleagues, published in Cell in 2010 (Heidorn et al., 2010). The experiments to be replicated are those reported in Figures 1A, 1B, 3A, 3B, and 4D. Heidorn and colleagues report that paradoxical activation of the RAF-RAS-MEK-ERK pathway by BRAF inhibitors when applied to BRAF(WT) cells is a result of BRAF/CRAF heterodimer formation upon inactivation of BRAF kinase activity, and occurs only in the context of active RAS. The Reproducibility Project: Cancer Biology is a collaboration between the Center for Open Science and Science Exchange, and the results of the replications will be published by eLife.

Funding information:
  • NIMH NIH HHS - F31 MH101956(United States)