Product Pathways - Ca / cAMP / Lipid Signaling
Choline Kinase α (D5X9W) Rabbit mAb #13422
|13422S||100 µl (10 western blots)||---||In Stock||---|
|13422||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Monkey||Endogenous||50||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
Choline Kinase α (D5X9W) Rabbit mAb recognizes endogenous levels of total choline kinase α protein. Based on the antigen sequence, this antibody is not expected to recognize choline kinase β.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro85 of human choline kinase α protein.
Western blot analysis of extracts from SK-BR-3, MDA-MB-231 and MCF7 cells using Choline Kinase α (D5X9W) Rabbit mAb.
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing full-length human choline kinase α (hChoKα; +) protein, using Choline Kinase α (D5X9W) Rabbit mAb.
Immunoprecipitation of choline kinase from HCT 116 cell extracts using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or Choline Kinase α (D5X9W) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot was performed using Choline Kinase α (D5X9W) Rabbit mAb. A light chain specific secondary antibody was used.
Choline kinase (ChoK) catalyzes the phosphorylation of choline, a key step in the biosynthesis of the membrane phospholipid phosphatidylcholine. At least three ChoK isoforms exist in mammalian cells, α-1, α-2, and β. The two α isoforms are transcribed from the same CHKA gene as splice variants, while the β isoform resides on a separate CHKB gene (reviewed in 1).
Research studies indicate that ChoKα levels affect signaling through MAPK and Akt pathways (2,3). Investigators have shown that ChoKα plays a role in proliferation and carcinogenesis and is highly expressed/activated in human cancers (4-7). Additional research studies suggest ChoKα may be a potential target for cancer therapy (8).
- Janardhan, S. et al. (2006) Curr Med Chem 13, 1169-86.
- Yalcin, A. et al. (2010) Oncogene 29, 139-49.
- Chua, B.T. et al. (2009) Mol Cancer 8, 131.
- Ramírez de Molina, A. et al. (2002) Oncogene 21, 4317-22.
- Ramírez de Molina, A. et al. (2007) Lancet Oncol 8, 889-97.
- Hernando, E. et al. (2009) Oncogene 28, 2425-35.
- Miyake, T. and Parsons, S.J. (2012) Oncogene 31, 1431-41.
- Bañez-Coronel, M. et al. (2008) Curr Cancer Drug Targets 8, 709-19.
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