Product Pathways - Protein Translation
CLK3 Antibody #3256
|3256S||100 µl (10 western blots)||---||In Stock||---|
|3256||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||59, 17||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry)
Specificity / Sensitivity
CLK3 Antibody detects endogenous levels of full-length and truncated forms of CLK3 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding His51 of CLK3. Antibodies were purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from Jurkat, HT29 and PC12 cell lines using CLK3 Antibody.
The cdc2-like kinase (CLK) family contains at least four highly conserved isoforms: CLK1, CLK2, CLK3 and CLK4 (1,2). CLKs are dual specificity kinases that autophosphorylate on serine, threonine and tyrosine residues and phosphorylate exogenous substrates on serine and threonine residues (2). CLK family members exist as both a full-length catalytically active form and an alternatively-spliced, inactive truncated form (1). A family of highly phosphorylated proteins, called serine and arginine rich (SR) proteins, are phosphorylated by CLKs (3-5). SR proteins are splicing factors that regulate the assembly of the spliceosome, a macromolecular complex where RNA splicing occurs in the nucleus. They are also involved in the selection of splice sites. Thus, CLKs may play important roles in regulating RNA splicing.
CLK3 is abundantly expressed in the testis and, similar to other family members, has been implicated in regulating RNA splicing (6-8).
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- Nayler, O. et al. (1997) Biochem. J. 326, 693-700.
- Colwill, K. et al. (1996) EMBO J. 15, 265-275.
- Prasad, J. and Manley, J.L. (2003) Mol. Cell Biol. 23, 4139-4149.
- Muraki, M. et al. (2004) J. Biol. Chem. 279, 24246-24254.
- Menegay, H. et al. (1999) Exp. Cell Res. 253, 463-473.
- Becker, W. et al. (1996) Biochim. Biophys. Acta 1312, 63-67.
- Duncan, P.I. et al. (1998) Exp. Cell Res. 241, 300-308.
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