Recombinant Human Heterogeneous Nuclear Ribonucleoprotein A1 (HNRNPA1) Protein (His)

Name: Recombinant Human Heterogeneous Nuclear Ribonucleoprotein A1 (HNRNPA1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03134P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HNRNPA1.

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Product Overview

Description	Recombinant Human Heterogeneous Nuclear Ribonucleoprotein A1 (HNRNPA1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P09651
Target Symbol	HNRNPA1
Synonyms	HNRNPA 1; Helix destabilizing protein; Helix-destabilizing protein; Heterogeneous nuclear ribonucleoprotein A1; Heterogeneous nuclear ribonucleoprotein A1B protein; Heterogeneous nuclear ribonucleoprotein B2 protein; Heterogeneous nuclear ribonucleoprotein core protein A1; hnRNP A1; hnRNP core protein A1; HNRNPA1; HNRPA1; MGC102835; Nuclear ribonucleoprotein particle A1 protein; ROA1_HUMAN; Single strand DNA binding protein UP1; Single strand RNA binding protein; Single-strand RNA-binding protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQ
Expression Range	2-354aa
Protein Length	Partial
Mol. Weight	40.9kDa
Research Area	Immunology
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	Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May bind to specific miRNA hairpins. Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1.; (Microbial infection) May play a role in HCV RNA replication.; (Microbial infection) Cleavage by Enterovirus 71 protease 3C results in increased translation of apoptosis protease activating factor APAF1, leading to apoptosis.
Subcellular Location	Nucleus. Cytoplasm.; Cytoplasm.
Database References	HGNC: 5031 OMIM: 164017 KEGG: hsa:3178 STRING: 9606.ENSP00000341826 UniGene: PMID: 29396485 By using an integrative structural biology approach, we show that hnRNP A1 forms a 1:1 complex with pri-mir-18a where both RNA recognition motifs (RRMs) bind to cognate RNA sequence motifs in the terminal loop of pri-mir-18a. PMID: 29946118 Data suggest that one way heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) regulates exon definition is to modulate the interaction of U2 small nuclear RNA auxiliary factor 2 (U2AF2) with decoy or bona fide 3' splice site (3'ss). PMID: 29650551 Our results indicate that hnRNP A1 promotes cell survival and cell cycle progression following UVB radiation PMID: 29229447 These findings indicated that hnRNPA1 is highly expressed in gastric cancer (GC)and promoted invasion by inducing Epithelialtomesenchymal transition (EMT) in GC cells. Thus, hnRNPA1 may be a potential therapeutic target for GC. PMID: 29484423 A significant overlap between hnRNPA1 and DDX5 splicing targets and they share many closely linked binding sites. PMID: 30042133 Results suggest that telomeric repeat-containing RNA (TERRA) regulates binding of heterogeneous nuclear ribonucleoprotein A1 to the telomere in a region surrounding the telomere, leading to a deeper understanding of the mechanism of TERRA function. PMID: 27958374 mutation in HNRNPA1 located in the nuclear localization signal domain of hnRNPA1, enhances the recruitment of mutant hnRNPA1 into stress granules, indicating that an altered nuclear localization signal activity plays an essential role in amyotrophic lateral sclerosis pathogenesis. PMID: 29033165 Rules of RNA specificity of hnRNP A1 revealed by global and quantitative analysis of its affinity distribution have been described. PMID: 28193894 study showed that UVB induces alternative splicing of hdm2 by increasing the expression and the binding of hnRNP A1 to hdm2 full-length mRNA PMID: 26757361 The authors show by NMR spectroscopy that both RNA recognition motifs of hnRNP A1 can bind simultaneously to a single bipartite motif of the human intronic splicing silencer ISS-N1, which controls survival of motor neuron exon 7 splicing. PMID: 28650318 current knowledge of the involvement of hnRNPA1 in cancer, including its roles in regulating cell proliferation, invasiveness, metabolism, adaptation to stress and immortalization. PMID: 28791797 Case Report: inflammatory myofibroblastic tumor (IMT) of the urinary bladder with a novel HNRNPA1-ALK fusion. PMID: 28504207 EGF signaling upregulates an E3 ubiquitin (Ub) ligase adaptor, SPRY domain-containing SOCS box protein 1 (SPSB1), which recruits Elongin B/C-Cullin complexes to conjugate lysine 29-linked poly Ubiquitin chains onto hnRNP A1. PMID: 28084329 hnRNP A1 directly binds to the 5' untranslated region of the RON mRNA and activates its translation through G-quadruplex RNA secondary structures PMID: 26930004 We demonstrate that the wild-type sequence harbors an hnRNP A1 and hnRNP A2/B1-binding exonic splicing silencer (ESS) overlapping the 5'splice site (5'ss) that prevents pseudoexon inclusion.we demonstrate that splice switching oligonucleotide (SSO) mediated blocking of the pseudoexon 3'ss and 5'ss effectively restores normal GLA splicing PMID: 27595546 The hnRNP A1 binding map can be used to identify potential targets for splice-switching oligonucleotides-based therapy. PMID: 27380775 Biophysical titrations reveal that the 5'-AUAGC-3' bulge undergoes a conformational change to assemble a functional hnRNP A1-human enterovirus 71 RNA complex. PMID: 28625847 PRMT5 regulates internal ribosome entry site-dependent translation via methylation of hnRNP A1. PMID: 28115626 KRAS-E2F1-ILK-hnRNPA1 regulatory loop enables pancreatic cancer cells to promote oncogenic KRAS signaling and to interact with the tumor microenvironment to promote aggressive phenotypes. PMID: 26616862 findings suggest that a new player, i.e., O-GlcNAcylation, regulates hnRNP A1 translocation and interaction with Trn1, possibly affecting its function PMID: 27913144 The results of this study suggest that hnRNPA1 is the causative gene in the family with flail arm ALS. This further expanded the disease phenotype of hnRNPA1 mutations. PMID: 27694260 Introduction of point mutations into the hnRNP A1-binding site or knockdown of hnRNP A1 expression promoted human papillomavirus 18 233;416 splicing and reduced E6 expression. PMID: 27489271 Studies provides evidence that hnRNP A1 is a new autoantigen of Behcet's Disease and associated with deep vein thrombosis. PMID: 27211563 these data suggest that the level of hnRNPA1 is strictly controlled to be within a certain range by the mRNA autoregulation in the physiological condition so that the cytotoxicity-causative alteration of hnRNPA1 expression does not take place. PMID: 28000042 The CCAT1/miR-490/hnRNPA1 axis promotes gastric cancer migration, and it may have a possible diagnostic and therapeutic potential in gastric cancer. PMID: 26825578 Data show that heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) unfolds the HRAS protein i-motif. PMID: 26674223 We demonstrate that an hnRNPA1 and CBX5 bi-directional core promoter fragment does not comprise intrinsic capacity for specific CBX5 down-regulation in metastatic cells PMID: 26791953 The sST2-5'UTR contains an IRES element, which is activated by a MEK/ERK-dependent increase in cytoplasmic localization of hnRNP A1 in response to FGF2, enhancing the translation of sST2. PMID: 27168114 hnRNP A1 is implicated in the free fatty acid-induced expression of SREBP-1a and of its target genes as well as in the lipid accumulation in hepatocytes. PMID: 26869449 analysis of HIV-1 intron splicing silencer and its interactions with the UP1 domain of hnRNPA1 PMID: 26607354 Our results indicate that the knockdown of hnRNP A1 has a specific function on the splicing of CD44 in breast cancer cells. PMID: 26151392 HNRNPA1 might play an important role in lung adenocarcinoma cells. PMID: 26581508 MiR-26a and mir-584 inhibit the binding of hnRNP A1-CDK6 mRNA and induce colorectal cancer cell apoptosis. PMID: 26494299 NF-kappaB2/p52:c-Myc:hnRNPA1 Pathway Regulates Expression of Androgen Receptor Splice Variants and Enzalutamide Sensitivity in Prostate Cancer PMID: 26056150 lowering the levels of hnRNP A1/A2 elicits defective transcription elongation on a fraction of P-TEFb-dependent genes, hence favoring the transcription of P-TEFb-independent genes PMID: 26011126 In neuroblastoma cells, hnRNP A1 directly interacts with Drp1 mRNA at its 3'UTR region, and enhances translation potential without affecting mRNA stability. PMID: 26518267 The disordered regions of key RNP granule components and the full-length granule protein hnRNPA1 can phase separate in vitro, producing dynamic liquid droplets. PMID: 26412307 ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1 PMID: 25616961 The marked loss of hnRNPA1 in motor neurons with concomitant cytoplasmic aggregation of TDP-43 may represent a severe disturbance of mRNA processing, suggesting a key role in progressive neuronal death in amyotrophic lateral sclerosis . PMID: 25338872 These findings suggested that hnRNP A1 plays key roles in the regulation of cell cycle progression and pathogenesis of Oral squamous cell carcinoma . PMID: 25752295 Its mutation is proved to be a rare cause of amyotrophic lateral sclerosis, frontotemporal dementia, and inclusion body myopathy. in the nertherlands. PMID: 24612671 miR-18a induces the apoptosis of colon cancer cells by directly binding to oncogenic hnRNP A1. PMID: 24166503 Its mutation is rare in patients with frontotemporal lobar degeneration. PMID: 24119545 Data reveal three distinct enthalpic contributions from the interactions of hnRNP Al (UP1) with the Na+ form of G-quadruplex DNA. PMID: 24831962 findings show HNRNPA1 modulates expression of an alternatively spliced transcript of HMGCR by regulating splicing and altering RNA stability, resulting in reduced HMGCR enzyme activity and increased LDL-Cholesterol uptake; results suggest HNRNPA1 plays a role in the variation of cardiovascular disease risk and statin response PMID: 24001602 HNRNPA1 is a novel transcriptional regulator of IL-6 expression, acting via the 5'-flanking sequence of the gene. PMID: 23985572 The results describe a UP1 binding mechanism that is likely different from current models used to explain the alternative splicing properties of hnRNP A1. PMID: 24628426 This functional hnRNP A1 deletion mutant is similar to a predicted hnRNP A1 isoform, which had not been previously experimentally characterized. PMID: 24530421 The results of this study suggested that mutations in hnRNPA1, A2/B1, and A3 genes are a rare finding in amyotrophic lateral sclerosis. PMID: 23827524

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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