|Other Names||Heterogeneous nuclear ribonucleoproteins C1/C2, hnRNP C1/C2, HNRNPC, HNRPC|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). 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). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6- methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671).|
|Cellular Location||Nucleus. Note=Component of ribonucleosomes.|
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This gene belongs to the subfamily of ubiquitouslyexpressed heterogeneous nuclear ribonucleoproteins (hnRNPs). ThehnRNPs are RNA binding proteins and they complex with heterogeneousnuclear RNA (hnRNA). These proteins are associated with pre-mRNAsin the nucleus and appear to influence pre-mRNA processing andother aspects of mRNA metabolism and transport. While all of thehnRNPs are present in the nucleus, some seem to shuttle between thenucleus and the cytoplasm. The hnRNP proteins have distinct nucleicacid binding properties. The protein encoded by this gene can actas a tetramer and is involved in the assembly of 40S hnRNPparticles. Multiple transcript variants encoding at least twodifferent isoforms have been described for this gene. [provided byRefSeq].
Konig, J., et al. Nat. Struct. Mol. Biol. 17(7):909-915(2010)Lee, E.K., et al. Nat. Struct. Mol. Biol. 17(6):732-739(2010)Brunner, J.E., et al. Virology 400(2):240-247(2010)Ertel, K.J., et al. J. Virol. 84(9):4229-4242(2010)Mosessian, S., et al. J. Biol. Chem. 284(44):30159-30166(2009)
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