Recombinant Human Heterogeneous Nuclear Ribonucleoproteins A2/B1 (HNRNPA2B1) Protein (His&Myc)

Name: Recombinant Human Heterogeneous Nuclear Ribonucleoproteins A2/B1 (HNRNPA2B1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00892P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Heterogeneous Nuclear Ribonucleoproteins A2/B1 (HNRNPA2B1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P22626
Target Symbol	HNRNPA2B1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY
Expression Range	1-353aa
Protein Length	Full Length
Mol. Weight	44.9 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. 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. 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.
Subcellular Location	Nucleus. Nucleus, nucleoplasm. Cytoplasm. Cytoplasmic granule. Secreted, extracellular exosome.; [Isoform A2]: Nucleus. Cytoplasm.
Database References	HGNC: 5033 OMIM: 600124 KEGG: hsa:3181 STRING: 9606.ENSP00000346694 UniGene: PMID: 29328485 m6A switches may account for the previously seen enhanced hnRNP A2/B1 binding adjacent to m6A; instead of direct binding to m6A, m6A may promote accessibility of hnRNP A2/B1 to certain binding sites, thereby explaining how m6A can facilitate the ability of hnRNP A2/B1 to enhance nuclear events such as pri-miRNA processing PMID: 29379020 revealed a novel heterozygous missense mutation of hnRNPA2B1 gene (c.929C>T, p. P310L) in the two patients which was then verified in all affected individuals PMID: 28389692 Cilostazol pretreatment can reduce the excessive expression of inflammatory cytokines and chemokines and hnRNP A2/B1 by the Behcet's disease-related stimulants. PMID: 28850024 UCP2 stimulates hnRNPA2/B1, GLUT1 and PKM2 expression and sensitizes pancreatic cancer cells to glycolysis inhibition. PMID: 27989750 Data suggest that galectin-3 and heterogeneous ribonucleoprotein particle component hnRNPA2B1 interact as members of the early splicing machinery. PMID: 27435226 effect of mutations on the aggregation propensity of hnRNPA2 PMID: 28542905 ALS-associated hnRNPA2B1 D290V mutant patient fibroblasts and motor neurons differentiated from iPSCs (iPSC-MNs) demonstrate abnormal splicing changes, likely due to increased nuclear-insoluble hnRNPA2B1. Mutant iPSC-MNs display decreased survival in long-term culture and exhibit hnRNPA2B1 localization to cytoplasmic granules as well as exacerbated changes in gene expression and splicing upon cellular stress. PMID: 27773581 Motor-neuron disease (MND)-linked RNA-binding proteins (RBPs), TDP-43, FUS, and hnRNPA2B1, bind to and induce structural alteration of UGGAAexp. These RBPs suppress UGGAAexp-mediated toxicity in Drosophila by functioning as RNA chaperones for proper UGGAAexp folding and regulation of pentapeptide repeat translation. PMID: 28343865 To examine the relationship between amino acid sequence and aggregation propensity, a diverse set of point mutations in the hnRNPA2B1 prion-like domain. PMID: 28137911 We concluded that hnRNPA2B1 promotes the tumorigenic potential of breast cancer cells, MCF-7 and MDA-MB-231, through the extracellular-signal-regulated kinase 1/2 or signal transducer and activator of transcription 3 pathway, which may serve as a target for future therapies. PMID: 28351333 results demonstrate that hnRNPA2/B1 promotes tumor cell growth by activating COX-2 signaling in NSCLC cells and imply that the hnRNPA2/B1/COX-2 pathway may be a potential therapeutic target for human lung cancers. PMID: 26774881 Detection of hnRNP A2/B1 expression may be useful as a biomarker for prediction of glioma progression. PMID: 25586062 The results indicate both genetic and physical interactions between disease-linked RNA-binding proteinss and DNAJB6/mrj, suggesting etiologic overlap between the pathogenesis of adult-onset inherited myopathies initiated by mutations in hnRNPA2B1 and DNAJB6. PMID: 26744327 hnRNPA2B1, hnRNPD, hnRNPL , and YBX1 might play important roles in gastric cancer tumorigenesis. PMID: 26805816 A unique role of the embryonic miR-369-HNRNPA2B1 axis in controlling metabolic enzyme function. PMID: 26176628 Study finds that the RNA-binding protein HNRNPA2B1 binds m(6)A-bearing RNAs in vivo and in vitro and its biochemical footprint matches the m(6)A consensus motif. HNRNPA2B1 directly binds a set of nuclear transcripts and elicits similar alternative splicing effects as the m(6)A writer METTL3. PMID: 26321680 Nuclear TDP-43 becomes neurotoxic by escaping from the inhibitory regulation by hnRNP-U or hnRNP-A2. PMID: 25378556 Tissue analysis and knockdown of hnRNPA2B1 using siRNA subsequently demonstrated both the overexpression and potential role for this molecule in lung tumorigenesis. PMID: 25483567 Cytoplasmic hnRNPA2 may affect the cancer cell phenotype through 3'-UTR mRNA-mediated regulation of beta-catenin expression and other cancer-relevant genes. PMID: 24823909 TDP-43 suppresses CGG-mediated toxicity through interactions with hnRNP A2/B1 and suggest a convergence of pathogenic cascades between repeat expansion disorders and RNA-binding proteins implicated in neurodegenerative disease. PMID: 24920338 data suggest that a prominent down-regulation of hnRNP-A2/B1 during hypoxia is associated with the post-transcriptional suppression of hASH1 synthesis. PMID: 25124043 In KRAS-dependent pancreatic ductal adenocarcinoma cell lines, HNRNPA2B1 interacts with and regulates the activity of KRAS G12V and G12D. PMID: 24998203 P55-70 of hnRNP B1 is a potential biomarker for autoimmune hepatitis in immunological tests. PMID: 24376828 Rsults demonstrate that hnRNP A2/B1 expression plays roles in the nuclear retention of the HIV-1 genomic RNA in the absence of Rev and in the release of the genomic RNA from translationally inactive, cytoplasmic RNP complexes. PMID: 24157614 hnRNPA2B1 is a key player in miRNA sorting into exosomes PMID: 24356509 Results demonstrate that by regulating DNA-Protein Kinase activity, hnRNP B1 can affect p53-mediated cell cycle progression and apoptosis, resulting in greater cell survival and subsequent proliferation in human adenocarcinoma of the lungs. PMID: 24675500 Arginine methylation of hnRNP A2 does not directly govern its subcellular localization. PMID: 24098712 hnRNP A2/B1 plays an inhibitory role in the replication of influenza A virus through suppressing NS1 RNA/protein levels and NS1 mRNA nucleocytoplasmic translocation. PMID: 24418537 Data indicate that apigenin binds to the C-terminal glycine-rich domain of hnRNPA2, preventing hnRNPA2 from forming homodimers, and therefore, it perturbs the alternative splicing of several hnRNPA2 targets. PMID: 23697369 our data suggest a novel type of gene regulation: a coordinated transcription or silencing of gene clusters delimited by DSB hot spots as well as PARP1 and HNRNPa2B1 binding sites. PMID: 23593027 Heterogeneous nuclear ribonucleoprotein A2/B1, an human telomerase reverse transcriptase - associated protein, is a potential prognostic biomarker for hepatocellular carcinoma patients PMID: 22372738 The positive expression rate of hnRNPA2/B1 in small cell lung cancer was significantly higher than that in the control specimens. PMID: 22325225 hnRNP A2/B1 protein is a regulator of HPV-16 late gene expression PMID: 22484615 Patient serum IgA was reactve against human recombinant hnRNP-A2/B1 in Behcet (83.3%), systemic lupus erythematosus (13.3%), rheumatoid arthritis (26.7%), Takayasu's arteritis (30%), and no IgA nephropathy patients, vs healthy controls (20%). PMID: 22205302 High HNRPA2B1 expression is associated with pancreatic cancer progression. PMID: 21642356 In addition to the core protein, hnRNP A2 also associated with Japanese encephalitis virus nonstructural protein 5 and with the 5'-untranslated region of the negative-sense Japanese encephalitis virus RNA. PMID: 21865391 The expression and distribution of hnRNP A2/B1 can affect the differentiation of SK-N-SH cells, as well as its co-localization with related oncogenes and tumor suppressor genes PMID: 21321999 hnRNP-A2/B1 affected tumor cell differentiation through interaction with oncogenes and tumor-suppressor genes, and it was overexpressed in human gastric cancer. PMID: 21175803 hnRNP A2/B1 and osteopontin expression was variable in CCRCCs and had no association with VHL genetic status. PMID: 20978319 Increased expression and cytoplasmic localization of hnRNP A2/B1 is associated with the development of hepatocellular carcinoma. PMID: 20604928 A conserved nonsense-mediated mRNA decay event within HNRNPA2B1 that appears to mediate autoregulation of HNRNPA2B1 expression levels, was identified upon UPF1 knockdown . PMID: 20946641 These data suggest involvement of hnRNP-A2 specific cellular autoimmune responses in rheumatoid arthritis pathogenesis PMID: 20232340 This protein has been found differentially expressed in thalami from patients with schizophrenia. PMID: 20471030 Neither grade nor stage of non-small cell lung carcinomas was correlated with hnRNP B1 immunreactivity PMID: 19609729 melanoma antigen expressed in G361, a representative melanoma cell line/ reacted with autoantibodies in patient sera PMID: 20181627 Increased protein levels of heterogeneous nuclear ribonucleoprotein A2/B1 in fetal Down syndrome brains. PMID: 11771750 Increased expression of heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP) in pancreatic tissue from smokers and pancreatic tumor cells. PMID: 12065097 Synovial overexpression of HNRNPA2 in rheumatoid arthritis (RA) patients in conjunction with the presence of autoreactive Th1-like cells indicates potential involvement of HNRNPA2 in the pathogenesis of RA. PMID: 12097415 These data suggest that the RBDII domain of hnRNP A2 targets hnRNP A2 to the periphery of the cell in a microtubule-dependent manner. PMID: 12243756

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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