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HNRNPA2B1 Antibody (aa127-137)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | P22626 |
| Reactivity | Human, Mouse, Rat, Rabbit, Monkey, Pig, Chicken, Horse, Bovine |
| Host | Goat |
| Clonality | Polyclonal |
| Calculated MW | 37kDa |
| Dilution | ELISA (1:64000), IHC-P (5 µg/ml), WB (1-3 µg/ml) |
| Gene ID | 3181 |
|---|---|
| Other Names | Heterogeneous nuclear ribonucleoproteins A2/B1, hnRNP A2/B1, HNRNPA2B1, HNRPA2B1 |
| Target/Specificity | Human HNRNPA2B1. This antibody is expected to recognize both reported isoforms (NP_002128.1; NP_112533.1). |
| Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
| Precautions | HNRNPA2B1 Antibody (aa127-137) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | HNRNPA2B1 |
|---|---|
| Synonyms | HNRPA2B1 |
| Function | 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 (PubMed:19099192). 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 (PubMed:10567417). 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 (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). |
| Cellular Location | 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). |
Citations (0)
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Application Protocols
Provided below are standard protocols that you may find useful for product applications.
Background
Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus.
References
Burd C.G.,et al.Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989).
Biamonti G.,et al.Nucleic Acids Res. 22:1996-2002(1994).
Kozu T.,et al.Genomics 25:365-371(1995).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Bienvenut W.V.,et al.Submitted (JUN-2009) to UniProtKB.
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