Cell Signaling Technology

Product Pathways - Cell Cycle / Checkpoint

CIP2A (D1M3H) Rabbit mAb #14805

No. Size Price
14805S 100 µl ( 10 western blots ) ¥3,100.00 现货查询 购买询价
14805 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human, Endogenous 90 Rabbit IgG
IP 1:100

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,

Specificity / Sensitivity

CIP2A (D1M3H) Rabbit mAb recognizes endogenous levels of total CIP2A protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val342 of human CIP2A protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using CIP2A (D1M3H) Rabbit mAb.

Background

Protein phosphatase 2A (PP2A) is a trimeric protein phosphatase and tumor suppressor that regulates the phosphorylation status of a wide variety of phosphoproteins. PP2A targets include many that play a role in the maintenance and progression of cancer (1). The cancerous inhibitor of protein phosphatase 2A (CIP2A) is a single pass membrane protein that binds the PP2A catalytic subunit to inhibit PP2A phosphatase activity (2). CIP2A is normally expressed at low levels in normal cells and tissues, but is elevated in human malignancies where it is thought to be oncogenic. Research studies demonstrate aberrant CIP2A expression in multiple tumor types, including those derived from the head and neck, liver, colon, lung, osteosarcoma, pancreatic, breast, and myeloid cancers (reviewed in 3). This evidence suggests that CIP2A interacts with many proteins that may play a role in cancer maintenance and progression (3). Additional studies indicate that CIP2A inhibits PP2A-mediated dephosphorylation of the proto-oncogene Myc at Ser64, which stabilizes and prevents proteolytic degradation of the Myc transcription factor (4).

  1. Westermarck, J. and Hahn, W.C. (2008) Trends Mol Med 14, 152-60.
  2. Junttila, M.R. et al. (2007) Cell 130, 51-62.
  3. De, P. et al. (2014) Oncotarget 5, 4581-602.
  4. Junttila, M.R. and Westermarck, J. (2008) Cell Cycle 7, 592-6.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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