Cell Signaling Technology

Product Pathways - Translational Control

hnRNP K (A222) Antibody #4699

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M R Endogenous 58-62 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

hnRNP K (A222) Antibody detects endogenous levels of total hnRNP K protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala222 of human hnRNP K protein. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa and Hep G2 cells using hnRNP K (A222) Antibody.

Background

Heterogeneous nuclear ribonucleoprotein K (hnRNP K) belongs to a family of RNA binding multiprotein complexes (hnRNP proteins) that facilitate pre-mRNA processing and transport of mRNA from the nucleus to cytoplasm (1-3). hnRNP K contains three unique structural motifs termed KH domains that bind poly(C) DNA and RNA sequences (4,5). Intricate architecture enables hnRNP K to facilitate mRNA biosynthesis (6), transcriptional regulation (7), and signal transduction. Research studies have shown that cytoplasmic hnRNP K expression is increased in oral squamous cell carcinoma and pancreatic cancer, and may be a potential prognostic factor (8,9). hnRNP K coordinates with p53 to regulate its target gene transcription in response to DNA damage. Proteasome degradation of hnRNP K is mediated by E3 ligase MDM2 (10). The interaction between hnRNP K and c-Src leads to hnRNP K phosphorylation, which allows for hnRNP K activation of silenced mRNA translation (11).

  1. Dreyfuss, G. et al. (1993) Annu Rev Biochem 62, 289-321.
  2. Siomi, H. et al. (1994) Cell 77, 33-9.
  3. Miau, L.H. et al. (1998) J Biol Chem 273, 10784-91.
  4. Tomonaga, T. and Levens, D. (1995) J Biol Chem 270, 4875-81.
  5. Choi, H.S. et al. (2009) Biochem Biophys Res Commun 380, 431-6.
  6. Bustelo, X.R. et al. (1995) Mol Cell Biol 15, 1324-32.
  7. Michelotti, E.F. et al. (1996) Mol Cell Biol 16, 2350-60.
  8. Zhou, R. et al. (2010) Int J Cancer 126, 395-404.
  9. Matta, A. et al. (2009) Int J Cancer 125, 1398-406.
  10. Moumen, A. et al. (2005) Cell 123, 1065-78.
  11. Ostareck-Lederer, A. et al. (2002) Mol Cell Biol 22, 4535-43.

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

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