Purification notesab61796 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
FunctionBinds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs that affects mRNA splicing, processing and stability. M6A alters the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch' to facilitate binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621).
Sequence similaritiesBelongs to the RRM HNRPC family. RALY subfamily. Contains 1 RRM (RNA recognition motif) domain.
Post-translational modificationsPhosphorylated on Ser-260 and Ser-299 in resting cells. Phosphorylated on Ser-253 and on 1 serine residue in the poly-Ser stretch at position 238 in response to hydrogen peroxide. Sumoylated. Sumoylation reduces affinity for mRNA.
Cellular localizationNucleus. Component of ribonucleosomes.
ab61796 at 1/50 - 1/100 dilution staining hnRNP C1 + C2 in human brain Left apical lobe by Immunohistochemistry, Paraffin-embedded tissue, in the absence or presence of the immunising peptide.
References for Anti-hnRNP C1 + C2 (phospho S260) antibody (ab61796)
This product has been referenced in:
Chen S et al. Reduced expression of lamin A/C results in modified cell signaling and metabolism coupled with changes in expression of structural proteins. J Proteome Res8:5196-211 (2009).
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