Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

hnRNP A2/B1 (2A2) Mouse mAb #9304

Applications Reactivity Sensitivity MW (kDa) Isotype
W F H Mk Endogenous 34 to 36 Mouse IgG1

Applications Key:  W=Western Blotting  F=Flow Cytometry
Reactivity Key:  H=Human  Mk=Monkey
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 A2/B1 (2A2) Mouse mAb detects endogenous levels of total hnRNP A2/B1 proteins. This antibody does not cross-react with other proteins.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a human hnRNP B1 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using hnRNP A2/B1 (2A2) Mouse mAb.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of MDA-MB-134 cells using hnRNP A2/B1 (2A2) Mouse mAb (blue) compared to a nonspecific negative control antibody (red).

Background

Heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism and transport of nuclear pre-mRNA transcripts (1). Alternative splicing produces transcripts that encode two homologous hnRNP proteins, hnRNPA2 and hnRNPB1, from a single gene sequence (2). Studies demonstrate hnRNP A2/B1 splicing repression across multiple targets (3,4) and that both proteins can bind and protect telomere repeat sequences from DNase digestion (5,6). Altered expression of hnRNP B1 is seen in several forms of cancer, including squamous cell carcinoma, adenocarcinoma, and various forms of lung cancer (7). Over expression of hnRNP B1 may be associated with inhibition of DNA-PK activity and impaired DNA repair during early stages of cancer development (8). Autoantigens to hnRNP A2/B1 (termed RA33) are associated with rheumatoid arthritis, systemic lupus erythromatosus and mixed connective tissue disease (9-11).

  1. Myer, V.E. and Steitz, J.A. (1995) RNA 1, 171-82.
  2. Kozu, T. et al. (1995) Genomics 25, 365-71.
  3. Clower, C.V. et al. (2010) Proc Natl Acad Sci U S A 107, 1894-9.
  4. Moran-Jones, K. et al. (2009) Cancer Res 69, 9219-27.
  5. Moran-Jones, K. et al. (2005) Nucleic Acids Res 33, 486-96.
  6. Kamma, H. et al. (2001) Biochem Biophys Res Commun 280, 625-30.
  7. Hamasaki, M. et al. (2001) Anticancer Res 21, 979-84.
  8. Iwanaga, K. et al. (2005) Biochem Biophys Res Commun 333, 888-95.
  9. Fritsch, R. et al. (2002) J Immunol 169, 1068-76.
  10. Fritsch-Stork, R. et al. (2006) Arthritis Res Ther 8, R118.
  11. Skriner, K. et al. (1997) J Clin Invest 100, 127-35.

Application References

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

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