Recombinant Human Heterogeneous Nuclear Ribonucleoprotein D0 (HNRNPD) Protein (GST)

Name: Recombinant Human Heterogeneous Nuclear Ribonucleoprotein D0 (HNRNPD) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-10300P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Heterogeneous Nuclear Ribonucleoprotein D0 (HNRNPD) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14103
Target Symbol	HNRNPD
Synonyms	ARE binding protein AUFI type A; AU-rich element RNA-binding protein 1; AUF; AUF1; AUF1A; Heterogeneous nuclear ribonucleoprotein D0; hnRNP D; hnRNP D0; Hnrnpd; hnRNPD0; HNRPD; HNRPD_HUMAN; P37
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	AVGGSAGEQEGAMVAATQGAAAAAGSGAGTGGGTASGGTEGGSAESEGAKIDASKNEEDEGHSNSSPRHSEAATAQREEWKMFIGGLSWDTTKKDLKDYFSKFGEVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVIDPKRAKAMKTKEPVKKIFVGGLSPDTPEEKIREYFGGFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKCEIKVAMSKEQYQQQQQWGSRGGFAGRARGRGGGPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSNQQSGYGKVSRRGGHQNSYKPY
Expression Range	18-355aa
Protein Length	Partial
Mol. Weight	63.9kDa
Research Area	Transcription
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	Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation.
Subcellular Location	Nucleus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally.
Database References	HGNC: 5036 OMIM: 601324 KEGG: hsa:3184 STRING: 9606.ENSP00000313199 UniGene: PMID: 28291226 Both hnRNP D and DL are able to control their own expression by alternative splicing of cassette exons in their 3'UTRs. Exon inclusion produces mRNAs degraded by nonsense-mediated decay. Moreover, hnRNP D and DL control the expression of one another by the same mechanism. PMID: 29263134 Lnc_ASNR interacted with the protein ARE/poly (U)-binding/degradation factor 1(AUF1), which is reported to promote rapid degradation of the Bcl-2 mRNA, an inhibitor of apoptosis. Lnc_ASNR binds to AUFI in nucleus, decreasing the cytoplasmic proportion of AUF1 which targets the B-cell lymphoma-2 (Bcl-2) mRNA. PMID: 27578251 in the present case, the identified mutations in HNRNPD and risk polymorphisms are plausible molecular players in the manifestation of CD. PMID: 28300425 AUF1 p45 triggers the RNA switch in the flaviviral genome that is crucial for viral replication. These findings represent an important example of how cellular (host) factors promote the propagation of RNA viruses PMID: 29263261 AUF1 might be a potential player in renal tubulointerstitial fibrosis through modulation of TGF-beta signal transduction via posttranscriptional regulation of Nedd4L. PMID: 28986222 Results indicate that the IL-6/STAT3/NF-kappaB positive feedback loop includes AUF1 and is responsible for the sustained active status of cancer-associated fibroblasts. PMID: 27248826 Depletion of AUF1 abolishes the global interaction of miRNAs and AGO2. AUF1 functions in promoting miRNA-mediated mRNA decay globally. PMID: 28334781 High AUF1 expression is associated with esophageal squamous cell carcinoma. PMID: 27826622 Arginine methylation improves the viral RNA chaperone activity of AUF1 p45. PMID: 27520967 These results suggest that the post-transcriptional regulation of ATX expression by HuR and AUF1 modulates cancer cell migration. PMID: 27784781 analysis of the effect of the N-terminal RNA recognition motif on AUF1 PMID: 27437398 We found a C-rich element (CRE) in mu-opioid receptor (MOR) 3'-untranslated region (UTR) to which poly (rC) binding protein 1 (PCBP1) binds, resulting in MOR mRNA stabilization. AUF1 phosphorylation also led to an increased interaction with PCBP1. PMID: 27836661 Findings indicate that hnRNP D and arginine methylation play important roles in the regulation of Flt-1 mRNA alternative polyadenylation. PMID: 26728997 Down-regulation of hnRNPD inhibits the proliferation of esophageal squamous cell carcinoma cells by promoting cell apoptosis. PMID: 26648300 in human ovarian, esophageal, and pancreatic cancer tissues, the expression of SOD1 was significantly correlated with that of AUF-1, further supporting the importance of AUF-1 in regulating SOD1 gene expression PMID: 25908445 hnRNPD has roles in cellular proliferation and survival, besides RNA splicing and stability in oral cancer PMID: 26318153 These data specify a post-transcriptional mechanism through which AUF1 and YB1 contribute to the normal development of erythropoietic cells, and to non-hematopoietic tissues in which AUF1- and YB1-based regulatory mRNPs assemble on heterologous mRNAs PMID: 25720531 preserves genomic integrity through its actions on target RNAs PMID: 25366541 Auf1 may play a role in the elimination of oxidized RNA, which is required for the maintenance of proper gene expression under conditions of oxidative stress PMID: 25486179 Taken together, these findings proved the inhibitory effect of TP-1 on the growth and metastasis of SMMC-7721 cells, and TP-1 might be offered for future application as a powerful chemopreventive agent against hepatocellular carcinoma (HCC) metastasis. PMID: 25787750 AUF1 interacts with the EV71 IRES to negatively regulate viral translation and replication. PMID: 25077793 a novel mechanism by which AUF1 binding and transfer of microRNA let-7 to AGO2 facilitates let-7-elicited gene silencing. PMID: 26253535 Functional analysis of selected regulated proteins revealed that knockdown of HNRPD, PHB2 and UB2V2 can increase HCMV replication, while knockdown of A4 and KSRP resulted in decreased HCMV replication. PMID: 25910425 AUF1 has been implicated in controlling a variety of physiological functions through its ability to regulate the expression of numerous mRNAs containing 3'-UTR AREs, thereby coordinating functionally related pathways. PMID: 24687816 MicroRNA-141 and microRNA-146b-5p have a role in inhibiting the prometastatic mesenchymal characteristics through the RNA-binding protein AUF1 targeting the transcription factor ZEB1 and the protein kinase AKT PMID: 25261470 IL-6 has a major role in activating breast stromal fibroblasts through STAT3-dependent AUF1 induction PMID: 25231991 AUF1 p45 promotes West Nile virus replication by an RNA chaperone activity that supports cyclization of the viral genome. PMID: 25078689 The prolyl isomerase pin1 regulates mRNA levels of genes with short half-lives by targeting specific RNA binding proteins, such as HuR and AUF1. PMID: 24416409 Our findings suggest that the AUF1 gene may play an important role in hepatocellular carcinoma progression PMID: 24213928 hnRNP D is critically involved in LDLR mRNA degradation in liver tissue in vivo. PMID: 24158514 analysis of how AUF1 target mRNAs and how AUF1 binding possibly regulates protein and/or microRNA binding events at adjacent sites PMID: 23940053 Results suggest that cleavage of AUF1 may be a strategy employed by coxsackievirus B3 (CVB3) to enhance the stability of its viral genome. PMID: 23572232 Hsp27 and F-box protein beta-TrCP promote degradation of mRNA decay factor AUF1. PMID: 23530064 ING4 may regulate c-MYC translation by its association with AUF1. PMID: 23603392 Here authors describe experiments suggesting that AUF1, a host RNA binding protein involved in mRNA decay, plays a role in the infectious cycle of picornaviruses such as poliovirus and human rhinovirus. PMID: 23131833 EBER1 may disturb the normal homeostasis between AUF1 and ARE-containing mRNAs or compete with other AUF1-interacting targets in cells latently infected by Epstein-Barr virus. PMID: 23012480 Findings point to a contribution of AUF1 to the deleterious effects of cytokines on beta cell functions and suggest a role for this RNA-binding protein in the early phases of type 1 diabetes. PMID: 22159912 The binding sites for HuR and AUF1 present in androgen receptor mRNA, defined by their exact target sequences, are the same sequence for both proteins. PMID: 22368252 AUF1 and HuR bind to VEGFA ARE RNA under both normoxic and hypoxic conditions, and a pVHL-RNP complex determines VEGFA mRNA decay. PMID: 22086907 the ability of AUF1 isoforms to regulate the mRNA binding and decay-promoting activities of TTP PMID: 22203679 Data suggest that AUF-1 and YB-1 are required for normal accumulation of beta-globin mRNA in erythroid cells; YB-1 and AUF-1 exhibit sequence-specific binding to 3-prime-untranslated region of beta-globin mRNA. PMID: 22134169 This review briefly describes the roles of mRNA decay in gene expression in general and ARE-mediated decay (AMD) in particular, with a focus on AUF1 and the different modes of regulation that govern AUF1 involvement in AMD. PMID: 21956942 Knockdown AUF1 mRNA expression by AUF1 siRNA in MKP-1 WT bone marrow macrophages significantly delayed degradation of IL-6, IL-10 and TNF- alpha mRNAs compared with controls PMID: 21733716 p16( INK4a) is also a modulator of transcription and apoptosis through controlling the expression of two major transcription regulators, AUF1 and E2F1 PMID: 21799732 These results suggest that the p38 MAP kinase (MAPK)-MK2-Hsp27 signaling axis may target AUF1 destruction by proteasomes, thereby promoting AU-rich element mRNA stabilization. PMID: 21245386 p40(AUF1) regulates a critical node within the NF-kappaB signaling pathway to permit IL10 induction for the anti-inflammatory arm of an innate immune response. PMID: 21135123 Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding affinity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands PMID: 20926381 Leukotriene B(4) BLT receptor signaling regulates the level and stability of cyclooxygenase-2 (COX-2) mRNA through restricted activation of Ras/Raf/ERK/p42 AUF1 pathway PMID: 20489206 the degradation of bcl-2 mRNA induced by AS1411 results from both interference with nucleolin protection of bcl-2 mRNA and recruitment of the exosome by AUF1. PMID: 20571027

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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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