hnRNP A2/B1 Antibody - #DF6296
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# DF6296, RRID:AB_2838262.
折りたたみ/展開
Heterogeneous nuclear ribonucleoprotein A2; Heterogeneous nuclear ribonucleoprotein A2/B1; Heterogeneous nuclear ribonucleoprotein B1; Heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 / hnRNP B1; hnRNP A2; hnRNP A2/B1; hnRNP B1; hnRNP-A2; hnRNP-B1; hnRNPA2; Hnrnpa2b1; hnRNPB1; HNRPA2; HNRPA2B1; HNRPB1; Nuclear ribonucleoprotein particle A2 protein; RNP A2; RNP B1; RNP-A2; RNP-B1; RNPA2; RNPB1; ROA2_HUMAN; SNRPB1;
免疫原
- P22626 ROA2_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY
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 - P22626 基板として
Site | PTM Type | Enzyme | Source |
---|---|---|---|
M1 | Acetylation | Uniprot | |
K3 | Acetylation | Uniprot | |
K3 | Ubiquitination | Uniprot | |
T4 | Phosphorylation | Uniprot | |
T7 | Phosphorylation | Uniprot | |
K13 | Ubiquitination | Uniprot | |
K22 | Acetylation | Uniprot | |
K22 | Ubiquitination | Uniprot | |
S29 | Phosphorylation | Uniprot | |
T32 | Phosphorylation | Uniprot | |
S36 | Phosphorylation | Uniprot | |
R38 | Methylation | Uniprot | |
Y40 | Phosphorylation | Uniprot | |
Y41 | Phosphorylation | Uniprot | |
K46 | Acetylation | Uniprot | |
K46 | Methylation | Uniprot | |
K46 | Sumoylation | Uniprot | |
K46 | Ubiquitination | Uniprot | |
T48 | Phosphorylation | Uniprot | |
S58 | Phosphorylation | Uniprot | |
K59 | Acetylation | Uniprot | |
K59 | Ubiquitination | Uniprot | |
S70 | Phosphorylation | Uniprot | |
S71 | Phosphorylation | Uniprot | |
S85 | Phosphorylation | Uniprot | |
K94 | Acetylation | Uniprot | |
K94 | Ubiquitination | Uniprot | |
S102 | Phosphorylation | Uniprot | |
K104 | Acetylation | Uniprot | |
K104 | Sumoylation | Uniprot | |
K104 | Ubiquitination | Uniprot | |
K112 | Acetylation | Uniprot | |
K112 | Ubiquitination | Uniprot | |
K113 | Ubiquitination | Uniprot | |
K120 | Acetylation | Uniprot | |
K120 | Sumoylation | Uniprot | |
K120 | Ubiquitination | Uniprot | |
R129 | Methylation | Uniprot | |
Y131 | Phosphorylation | Uniprot | |
Y135 | Phosphorylation | Uniprot | |
K137 | Ubiquitination | Uniprot | |
T140 | Phosphorylation | Uniprot | |
T145 | Phosphorylation | Uniprot | |
R147 | Methylation | Uniprot | |
S149 | Phosphorylation | Uniprot | |
K151 | Ubiquitination | Uniprot | |
R153 | Methylation | Uniprot | |
T159 | Phosphorylation | O14757 (CHEK1) | Uniprot |
K168 | Acetylation | Uniprot | |
K168 | Sumoylation | Uniprot | |
K168 | Ubiquitination | Uniprot | |
K173 | Acetylation | Uniprot | |
K173 | Sumoylation | Uniprot | |
K173 | Ubiquitination | Uniprot | |
Y174 | Phosphorylation | Uniprot | |
T176 | Phosphorylation | Uniprot | |
K186 | Sumoylation | Uniprot | |
S189 | Phosphorylation | Uniprot | |
S198 | Phosphorylation | Uniprot | |
R200 | Methylation | Uniprot | |
S201 | Phosphorylation | Uniprot | |
R203 | Methylation | Uniprot | |
S212 | Phosphorylation | Uniprot | |
R213 | Methylation | Uniprot | |
S225 | Phosphorylation | Uniprot | |
R228 | Methylation | Uniprot | |
S231 | Phosphorylation | Uniprot | |
S236 | Phosphorylation | Uniprot | |
R238 | Methylation | Uniprot | |
Y244 | Phosphorylation | Uniprot | |
Y247 | Phosphorylation | Uniprot | |
S259 | Phosphorylation | Uniprot | |
Y262 | Phosphorylation | Uniprot | |
R266 | Methylation | Uniprot | |
Y287 | Phosphorylation | Uniprot | |
Y290 | Phosphorylation | Uniprot | |
Y295 | Phosphorylation | Uniprot | |
S297 | Phosphorylation | Uniprot | |
Y300 | Phosphorylation | Uniprot | |
Y306 | Phosphorylation | Uniprot | |
S311 | Phosphorylation | Uniprot | |
Y313 | Phosphorylation | Uniprot | |
K317 | Sumoylation | Uniprot | |
S318 | Phosphorylation | Uniprot | |
S324 | Phosphorylation | Uniprot | |
R325 | Methylation | Uniprot | |
Y331 | Phosphorylation | Uniprot | |
Y336 | Phosphorylation | Uniprot | |
S341 | Phosphorylation | Uniprot | |
S344 | Phosphorylation | Uniprot | |
Y347 | Phosphorylation | Uniprot | |
R350 | Methylation | Uniprot | |
S351 | Phosphorylation | Uniprot | |
R352 | Methylation | Uniprot | |
Y353 | Phosphorylation | Uniprot |
研究背景
Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm. Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs. Plays also a role in the activation of the innate immune response. Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6. In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production.
(Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport.
Sumoylated in exosomes, promoting miRNAs-binding.
Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity). According to a report, methylation affects subcellular location and promotes nuclear localization. According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity).
Nucleus. Nucleus>Nucleoplasm. Cytoplasm. Cytoplasmic granule. Secreted>Extracellular exosome.
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661). Component of ribonucleosomes (PubMed:17289661). Not found in the nucleolus (PubMed:17289661). Found in exosomes following sumoylation (PubMed:24356509).
Nucleus. Cytoplasm.
Note: Predominantly nucleoplasmic, however is also found in the cytoplasm of cells in some tissues (PubMed:17289661).
Homodimer; dimerization is required for nucleocytoplasmic translocation. Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8. Interacts with TARDBP. Interacts with CKAP5. Interacts with TBK1. Interacts with STING1. Interacts with SRC.
The low complexity (LC) region is intrinsically disordered. When incubated at high concentration, it is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidence suggests that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels.
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