Cell Signaling Technology

Product Pathways - Phosphatases

Phospho-CTDSPL2 (Ser104) Antibody #5294

Applications Reactivity Sensitivity MW (kDa) Source
W IP H Mk Endogenous 61 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
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

Phospho-CTDSPL2 (Ser104) Antibody detects endogenous levels of CTDSPL2 only when phosphorylated at Ser104.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser104 of human CTDSPL2 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from NCI-H1703 cells, untreated or EGF-treated, and HeLa cells, untreated or λ-phosphatase-treated, using Phospho-CTDSPL2 (Ser104) Antibody (upper) and a total CTDSPL2 antibody (lower).

Background

CTD small phosphatase-like protein 2 (CTDSPL2, HSPC129) is a putative RNA-polymerase II carboxy-terminal domain (CTD) phosphatase (1) that belongs to a small subfamily of CTD phosphatases (2). The CTD of RNA polymerase II contains multiple Y-S-P-T-S-P-S repeats that are phosphorylated during the transcription cycle (3,4). In general, CTD phosphatases regulate the reversible CTD phosphorylation state of RNA-polymerase II at several stages of RNA synthesis and during post-transcriptional modification (4-6). CTDSPL2 has several structural and functional similarities to other CTD phosphatases, including FCP1, SCP1, DULLARD, and UBLCP1 (1,2).

Phosphorylation of CTDSPL2 at Ser104 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery (7). The site was independently found in select carcinoma cell lines and in tumors (8).

  1. Qian, H. et al. (2007) Mol Cell Biochem 303, 183-8.
  2. Kim, Y. et al. (2007) Proc Natl Acad Sci USA 104, 6596-601.
  3. Corden, J.L. et al. (1985) Proc Natl Acad Sci USA 82, 7934-8.
  4. Ahn, S.H. et al. (2004) Mol Cell 13, 67-76.
  5. Dahmus, M.E. (1996) J Biol Chem 271, 19009-12.
  6. Goodrich, J.A. and Tjian, R. (1994) Cell 77, 145-56.
  7. Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
  8. Dephoure, N. et al. (2008) Proc Natl Acad Sci USA 105, 10762-7.

Application References

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