Log in

Q4lab

Home  |  Model Systems  |  Cells  |  Cell lines  |  C2C12
Home  |  Model Systems  |  Cells  |  Cell lines  |  C2C12

Model System - C2C12

from ATCC: The C2C12 cell line differentiates rapidly, forming contractile myotubes and producing characteristic muscle proteins.

C2C12
Category:  Cells  /  Cell lines
Last revision: Dec 16, 2014
Author(s): 
Contact
Name: Antonella Bongiovanni
Address: IBIM-CNR, Palermo via Ugo La Malfa, 153
Email: bongiovanni@ibim.cnr.it

 

Figure legend:

(Top) Assessment of myogenic differentiation of C2C12 cells. 
Myoblasts (D0) and myotubes after two (DII), three (DIII) and six days (DVI) of differentiation.

(Bottom) Western blots showing the expression of MyHC, myogenin, and MyoD in lysates of C2C12 cells after the indicated days of differentiation. Ponceau staining is shown as a control of the total protein loaded per lane.

Genotype: Organism: Mus musculus, mouse, wt
Origin: The C2C12 is a subclone (produced by H. Blau, et al) of the mouse myoblast cell line established by D. Yaffe and O. Saxel.

Description

C2C12 cell line is the cellular system to study Skeletal Muscle physiology and differentiation.


How to mantain and differentiate: The mouse myoblast cell line C2C12 were maintained in high glucose DMEM supplemented with 20% foetal calf serum (FCS), sodium pyruvate, L-glutamine, penicillin and streptomycin (proliferation medium) at 37°C in a humidified atmosphere with 5% CO2. Myotube differentiation was induced when the medium was supplemented with 2% horse serum in place of FCS (differentiation medium).

 

Quality validation: Yes

Validation info

The model system has been characterized by several techniques and has been published in peer-reviewed journals.

       

      Citations
      Romancino DP, Paterniti G, Campos Y, De Luca A, Di Felice V, d'Azzo A, Bongiovanni A. Identification and characterization of the nano-sized vesicles released by muscle cells. FEBS Lett. 2013;587:1379-84
      Bongiovanni A, Romancino DP, Campos Y, Paterniti G, Qiu X, Moshiach S, Di Felice V, Vergani N, Ustek D, d'Azzo A. Alix protein is substrate of ozz-e3 ligase and modulates actin remodeling in skeletal muscle. J Biol Chem. 2012;287:12159-71
      Campos Y, Qiu X, Zanoteli E, Moshiach S, Vergani N, Bongiovanni A, Harris AJ, d'Azzo A. Ozz-E3 ubiquitin ligase targets sarcomeric embryonic myosin heavy chain during muscle development. PLoS One. 2010;5:e9866
      d'Azzo A, Bongiovanni A, Nastasi T. E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation. Traffic. 2005;6:429-41.
      Nastasi T, Bongiovanni A, Campos Y, Mann L, Toy JN, Bostrom J, Rottier R, Hahn C, Conaway JW, Harris AJ, D'Azzo A. Ozz-E3, a muscle-specific ubiquitin ligase, regulates beta-catenin degradation during myogenesis. Dev Cell. 2004;6:269-82.

       

      Document Actions
      by Abstract