|Application ||WB, E|
|Other Accession||P58466, NP_872580.1, NP_067021.1|
|Calculated MW||29203 Da|
|Antigen Region||1-30 aa|
|Other Names||Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1, Nuclear LIM interactor-interacting factor 3, NLI-IF, NLI-interacting factor 3, Small C-terminal domain phosphatase 1, SCP1, Small CTD phosphatase 1, CTDSP1, NIF3, NLIIF, SCP1|
|Target/Specificity||This CTDSP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human CTDSP1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CTDSP1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||NIF3, NLIIF, SCP1|
|Function||Preferentially catalyzes the dephosphorylation of 'Ser- 5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.|
|Cellular Location||Nucleus. Note=Colocalizes with RNA polymerase II|
|Tissue Location||Expression is restricted to non-neuronal tissues. Highest expression in skeletal muscle, spleen, lung and placenta.|
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Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Zhang, M., et al. Protein Sci. 19(5):974-986(2010)
Ji, H., et al. Plant J. 61(1):96-106(2010)
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
Sapkota, G., et al. J. Biol. Chem. 281(52):40412-40419(2006)
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