STAT3α/β (N-Term) Rabbit Monoclonal Antibody (Clone RM465)

STAT3 is a ubiquitously expressed transcription factor and member of the STAT protein family that has roles in a variety of cellular functions including proliferation, apoptosis, and differentiation, as well as innate and adaptive immunity and stem cell pluripotency.^1,2,3 It contains N-terminal, coiled-coil, DNA binding, and linker domains that mediate nuclear translocation and export, as well as Src homology 2 (SH2) and C-terminal transactivation domains that are subject to phosphorylation.^4,5 Alternative splicing of STAT3 pre-mRNA leads to the formation of the full-length isoform STAT3α, as well as STAT3β, a truncated isoform that lacks a portion of the transactivation domain and is considered a dominant-negative regulator of STAT3 transcriptional activation.⁶ STAT3 signaling is inhibited by the negative regulator suppressor of cytokine signaling 3 (SOCS-3) and prevents excessive STAT3 activation.² Phosphorylation of STAT3 at tyrosine 705 (Tyr⁷⁰⁵) is mediated by JAKs in response to stimulation with cytokines or growth factors and induces STAT3 dimerization and nuclear translocation, leading to STAT3-dependent gene transcription.^2,1 Cayman's STAT3α/β Rabbit Monoclonal Antibody (Clone RM465) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Forbes, L.R., Milner, J., and Haddad, E. Signal transducer and activator of transcription 3: A year in review. Curr. Opin. Hematol. 23(1), 23-27 (2016).

2. Lau, Y.-T.K., Ramaiyer, M., Johnson, D.E., et al. Targeting STAT3 in cancer with nucleotide therapeutics. Cancers 11(11), 1681 (2019).

3. Raz, R., Lee, C.-K., Cannizzaro, L.A., et al. Essential role of STAT3 for embryonic stem cell pluripotency. Proc. Natl. Acad. Sci. USA 96(6), 2846-2851 (1999).

4. Dumoutier, L., de Meester, C., Tavernier, J., et al. New activation modus of STAT3: A tyrosine-less region of the interleukin-22 receptor recruits STAT3 by interacting with its coiled-coil domain. The Journal of Biological Chemisty 284(39), 26377-26384 (2009).

5. Sgrignani, J., Garofalo, M., Matkovic, M., et al. Structural biology of STAT3 and its implications for anticancer therapies development. Int. J. Mol. Sci. 19(6), 1591 (2018).

6. Maritano, D., Sugrue, M.L., Tininini, S., et al. The STAT3 isoforms α and β have unique and specific functions. Nat. Immunol. 5(4), 401-409 (2004).