Human CDON / CDO Protein (His Tag)

CDO,CDON1,HPE11,ORCAM

100ug (NPP3734) Please inquiry

Catalog Number	P11965-H08H
Organism Species	Human
Host	Human Cells
Synonyms	CDO,CDON1,HPE11,ORCAM
Molecular Weight	The recombinant human CDON consists of 949 amino acids and has a calculated molecular mass of 103 kDa. It migrates as an approximately 125 kDa band in SDS-PAGE under reducing conditions.
predicted N	Asp 26
SDS-PAGE
Purity	> 65 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human CDON (AAI14436.1) extracellular domain (Met 1-Asp 963) was expressed, with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area	Immunology \|Signal Transduction \|Signaling Pathway \|Representative pathway \|Hedgehog Signaling Pathway
Formulation	Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	Cell adhesion molecule-related, down-regulated by oncogenes (CDON), also known as CDO, is an Ig superfamily member, is a component of a cell surface receptor that positively regulates skeletal myogenesis. Brother of CDO (BOC) is a cell surface receptor that derives its name from the structurally related protein, CDON. They are components of a cell surface receptor that positively regulates myogenesis in vitro. Expression of Cdo and Boc in myoblast cell lines is downregulated by the ras oncogene, and forced re-expression of either Cdo or Boc can override ras-induced inhibition of myogenic differentiation. CDO and BOC play a role in the inverse relationship between differentiation and transformation of cells in the skeletal muscle lineage. CDON binds to Bnip-2 and JLP, scaffold proteins for Cdc42 and p38alpha/beta MAPK, respectively. The Bnip-2/Cdc42 and JLP/p38alpha/beta complexes associate in a CDON-dependent manner, resulting in Bnip-2/Cdc42-dependent p38alpha/beta activation and stimulation of cell differentiation. It is proposed that CDO mediates, at least in part, the effects of cell-cell interactions between muscle precursors that are critical in myogenesis.
Reference	Kang JS, et al. (1998) CDO, a robo-related cell surface protein that mediates myogenic differentiation. J Cell Biol. 143(2): 403-13. Wegorzewska M, et al. (2003) Overexpression of the immunoglobulin superfamily members CDO and BOC enhances differentiation of the human rhabdomyosarcoma cell line RD. Mol Carcinog. 37(1): 1-4. Cole F, et al. (2003) Microform holoprosencephaly in mice that lack the Ig superfamily member Cdon. Curr Biol. 13(5): 411-5. Jehee FS, et al. (2006) Mutational screening of FGFR1, CER1, and CDON in a large cohort of trigonocephalic patients. Cleft Palate Craniofac J. 43(2): 148-51. Kavran JM, et al. (2010) All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner. J Biol Chem. 285(32): 24584-90. Lu M, et al. (2010) N-cadherin ligation, but not Sonic hedgehog binding, initiates Cdo-dependent p38alpha/beta MAPK signaling in skeletal myoblasts. Proc Natl Acad Sci U S A. 107(9): 4212-7.