hnRNP C1/C2 Antibody - #DF3075
製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
引用形式: Affinity Biosciences Cat# DF3075, RRID:AB_2835458.
折りたたみ／展開
C1; C2; Heterogeneous nuclear ribonucleoprotein C (C1/C2); Heterogeneous nuclear ribonucleoprotein C; Heterogeneous nuclear ribonucleoproteins C1/C2; HNRNP; hnRNP C1 / hnRNP C2; hnRNP C1/C2; Hnrnpc; HNRPC; HNRPC_HUMAN; MGC104306; MGC105117; MGC117353; MGC131677; Nuclear ribonucleoprotein particle C1 protein; Nuclear ribonucleoprotein particle C2 protein; SNRPC;
免疫原
- P07910 HNRPC_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLSSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSKSGKLKGDDLQAIKKELTQIKQKVDSLLENLEKIEKEQSKQAVEMKNDKSEEEQSSSSVKKDETNVKMESEGGADDSAEEGDLLDDDDNEDRGDDQLELIKDDEKEAEEGEDDRDSANGEDDS
種類予測
Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - P07910 基板として
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| A2 | Acetylation | Uniprot | |
| S3 | Phosphorylation | Uniprot | |
| K8 | Acetylation | Uniprot | |
| K8 | Sumoylation | Uniprot | |
| K8 | Ubiquitination | Uniprot | |
| T9 | Phosphorylation | Uniprot | |
| K29 | Ubiquitination | Uniprot | |
| K30 | Ubiquitination | Uniprot | |
| S31 | Phosphorylation | Uniprot | |
| S38 | Phosphorylation | Uniprot | |
| K39 | Acetylation | Uniprot | |
| K39 | Methylation | Uniprot | |
| K39 | Ubiquitination | Uniprot | |
| K42 | Sumoylation | Uniprot | |
| K42 | Ubiquitination | Uniprot | |
| S47 | Phosphorylation | Uniprot | |
| K50 | Acetylation | Uniprot | |
| K50 | Sumoylation | Uniprot | |
| K50 | Ubiquitination | Uniprot | |
| Y57 | Phosphorylation | Uniprot | |
| R61 | Methylation | Uniprot | |
| K89 | Sumoylation | Uniprot | |
| K89 | Ubiquitination | Uniprot | |
| K98 | Methylation | Uniprot | |
| S100 | Phosphorylation | Uniprot | |
| Y105 | Phosphorylation | Uniprot | |
| S107 | Phosphorylation | Uniprot | |
| T109 | Phosphorylation | Uniprot | |
| S113 | Phosphorylation | Uniprot | |
| S115 | Phosphorylation | Uniprot | |
| S119 | Phosphorylation | Uniprot | |
| S120 | Phosphorylation | Uniprot | |
| S121 | Phosphorylation | Uniprot | |
| Y126 | Phosphorylation | Uniprot | |
| Y132 | Phosphorylation | Uniprot | |
| Y133 | Phosphorylation | Uniprot | |
| R135 | Methylation | Uniprot | |
| Y137 | Phosphorylation | Uniprot | |
| S138 | Phosphorylation | Uniprot | |
| Y139 | Phosphorylation | Uniprot | |
| R142 | Methylation | Uniprot | |
| R151 | Methylation | Uniprot | |
| S156 | Phosphorylation | Uniprot | |
| K157 | Acetylation | Uniprot | |
| R160 | Methylation | Uniprot | |
| S162 | Phosphorylation | Uniprot | |
| T165 | Phosphorylation | Uniprot | |
| S166 | Phosphorylation | Uniprot | |
| K170 | Acetylation | Uniprot | |
| K170 | Ubiquitination | Uniprot | |
| S171 | Phosphorylation | Uniprot | |
| S175 | Phosphorylation | Uniprot | |
| K176 | Sumoylation | Uniprot | |
| K176 | Ubiquitination | Uniprot | |
| K187 | Acetylation | Uniprot | |
| K187 | Ubiquitination | Uniprot | |
| K189 | Methylation | Uniprot | |
| K189 | Ubiquitination | Uniprot | |
| K197 | Ubiquitination | Uniprot | |
| K198 | Ubiquitination | Uniprot | |
| K204 | Ubiquitination | Uniprot | |
| K206 | Ubiquitination | Uniprot | |
| S209 | Phosphorylation | Uniprot | |
| K216 | Acetylation | Uniprot | |
| K216 | Ubiquitination | Uniprot | |
| K219 | Ubiquitination | Uniprot | |
| K223 | Sumoylation | Uniprot | |
| K223 | Ubiquitination | Uniprot | |
| K229 | Sumoylation | Uniprot | |
| K229 | Ubiquitination | Uniprot | |
| K232 | Acetylation | Uniprot | |
| K232 | Sumoylation | Uniprot | |
| K232 | Ubiquitination | Uniprot | |
| S233 | Phosphorylation | Uniprot | |
| S238 | Phosphorylation | Uniprot | |
| S239 | Phosphorylation | Uniprot | |
| S240 | Phosphorylation | Uniprot | |
| S241 | Phosphorylation | Uniprot | |
| K243 | Sumoylation | Uniprot | |
| K243 | Ubiquitination | Uniprot | |
| K244 | Ubiquitination | Uniprot | |
| T247 | Phosphorylation | Uniprot | |
| K250 | Sumoylation | Uniprot | |
| K250 | Ubiquitination | Uniprot | |
| S253 | Phosphorylation | P48729 (CSNK1A1) | Uniprot |
| S260 | Phosphorylation | P68400 (CSNK2A1) , P48729 (CSNK1A1) | Uniprot |
| K284 | Ubiquitination | Uniprot | |
| S299 | Phosphorylation | P48729 (CSNK1A1) | Uniprot |
| S306 | Phosphorylation | Uniprot |
研究背景
Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. 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. 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. 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.
Phosphorylated 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.
Nucleus.
Note: Component of ribonucleosomes.
Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a 19S complex that interacts with HNRNPA2B1 tetramers. Component of the 40S hnRNP particle. Identified in the spliceosome C complex. Interacts with IGF2BP1. Interacts with DHX9; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments.
Belongs to the RRM HNRPC family. RALY subfamily.
研究領域
· Genetic Information Processing > Transcription > Spliceosome.
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