目录号 | 产品详情 | 靶点 | |
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T1349 | Others DNA/RNA Synthesis | ||
5-Fluorouridine 是一种 5-fluorouracil 的代谢物,具有抗癌作用。它对 L1210 细胞的生长具有细胞毒性作用,其作用的 IC50值为 2 nM。它能抑制人结肠癌细胞 rRNA 的合成。 | |||
T13499 | Endogenous Metabolite | ||
3-Methyluridine 是一种修饰的细胞 RNA 的核苷(RNA nucleoside)。它通常以 RNA 修饰的形式出现,能够在古菌的 23S rRNA、真细菌的 16S 和 23S rRNA 以及真核核糖体 18S、25S 和 28SRNA 的中检测到。 | |||
T36971 | Nucleoside Antimetabolite/Analog | ||
5-Ethynyluridine 可用于标记新合成的 RNA。这种方法称为使用点击化学 (RICK) 捕获新转录的 RNA 相互作用组,系统地捕获与多种 RNA 结合的蛋白质,包括新生 RNA 和传统上被忽视的非多腺苷酸化 RNA。 | |||
T13969 | Others DNA/RNA Synthesis | ||
Xanthopterin hydrate 是东方大黄蜂翅膀中黄色颗粒的主要成分,是一种非共轭的蝶啶天然产物,在 386/456 nm 处产生特征性的激发光。 它可抑制 RNA 合成,引起大鼠肾脏生长和肥大。 | |||
T8354 | Nucleoside Antimetabolite/Analog Influenza Virus DNA/RNA Synthesis | ||
Triazavirin 是一种核酸的核苷类似物和抗病毒剂,通过抑制病毒 RNA 和 DNA 的合成以及基因组片段的复制而起作用。在流感传播阶段,它可作为保护剂。 | |||
T14522 | DNA/RNA Synthesis | ||
Beaucage reagent 可用于DNA 切割。 | |||
T1767 | DNA/RNA Synthesis | ||
BMH-21 是一种小分子 DNA 嵌入剂,可结合核糖体 DNA 并抑制 RNA 聚合酶 I (Pol I) 转录,具有抗癌活性。 | |||
T13166 | Others DNA/RNA Synthesis | ||
TK216 是一种口服有效的 E26 转录因子抑制剂,具有抗癌活性。它直接结合 EWS-FLI1 并抑制 EWS-FLI1 蛋白质相互作用,也可阻止 EWS-FLI1 与 RNA 解旋酶 A 的结合。 | |||
T40179 | DNA/RNA Synthesis | ||
Sodium Camptothecin 是一种植物生物碱,具有抗肿瘤活性。它是可逆 RNA 合成抑制剂,可以抑制腺病毒的复制。它能抑制 DNA 合成,并引起细胞内预形成的病毒 DNA 断裂。 | |||
T15611 | DNA/RNA Synthesis | ||
JH-RE-06是一种REV1-REV7互作抑制剂,IC50为0.78 μM,Kd 为0.42 μM。它靶向与 POLζ 的 REV7 亚基相互作用的 REV1,可改善化疗效果。它通过阻止诱变 POLζ 的募集来破坏诱变性跨损伤合成。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-06071 | SARS-CoV-2 RNA-dependent RNA polymerase/RDRP Protein (His) | SARS-CoV-2 | Baculovirus-Insect Cells | ||
SARS-CoV-2 RNA-dependent RNA polymerase/RDRP Protein (His) is expressed in Baculovirus-Insect Cells with His tag. The predicted molecular weight is 108.3 kDa. Accession number: YP_009725307.1
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TMPY-03983 | CIRBP Protein, Human, Recombinant (His) | Human | E. coli | ||
CIRBP, also known as cold-inducible RNA-binding protein, plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP responds to a wide array of cellular stresses, including short wavelength ultraviolet light (UVC), at the transcriptional and post-translational level. It acts as a translational activator.CIRBP can bind the 3 translated region of specific transcripts to stabilize them and facilitate their transport to ribosomes for translation. CIRBP affects NF-κB signaling as opposed to IL1B mRNA stability directly.
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TMPH-01110 | CIRBP Protein, Human, Recombinant (GST) | Human | E. coli | ||
CIRBP Protein, Human, Recombinant (GST) is expressed in E. coli.
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TMPH-02587 | CIRBP Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN.
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TMPH-01900 | DDX5 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.
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TMPH-03193 | Alba Protein, Pyrococcus furiosus, Recombinant (His & SUMO) | Pyrococcus furiosus | E. coli | ||
Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
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TMPH-01249 | ADAR Protein, Human, Recombinant (GST) | Human | E. coli | ||
Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication.
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TMPH-01248 | ADAR Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication.
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TMPH-02133 | DDX39B Protein, Human, Recombinant (GST) | Human | E. coli | ||
Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability.; Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly with [PubMed:23299939] reporting a stimulatory effect.; (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production.
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TMPH-00974 | DHX9 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
DHX9 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.
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TMPY-03344 | LSM3 Protein, Human, Recombinant (His) | Human | E. coli | ||
LSM3 (LSM3 Homolog, U6 Small Nuclear RNA And MRNA Degradation Associated) is a Protein Coding gene. LSM3 is a member of the snRNP Sm proteins family. It plays role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as a component of the pre-catalytic spliceosome (spliceosome B complex). Sm-like proteins can be detected in a variety of organisms. They all have the Sm sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. Diseases associated with LSM3 include Spondylolysis.
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TMPH-00980 | DHX33 Protein, Human, Recombinant (His) | Human | E. coli | ||
DHX33 Protein, Human, Recombinant (His) is expressed in E. coli.
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TMPH-01902 | DDX60 Protein, Human, Recombinant (His) | Human | E. coli | ||
DDX60 Protein, Human, Recombinant (His) is expressed in E. coli.
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TMPH-00533 | T7 RNA polymerase Protein, Enterobacteria phage T7, Recombinant (His & Myc) | Escherichia phage T7 | E. coli | ||
Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Plays also a role in viral DNA packaging, probably by pausing the transcription at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process.
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TMPH-00979 | DDX3Y Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
DDX3Y Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus.
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TMPH-00976 | DDX19A Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
DDX19A Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.
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TMPH-02884 | CTDP1 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.
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TMPH-00973 | DHX36 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
DHX36 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.
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TMPH-01556 | EIF2AK2 Protein, Human, Recombinant (His) | Human | Yeast | ||
IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection. Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin.
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TMPH-01899 | ALKBH5 Protein, Human, Recombinant (His) | Human | E. coli | ||
Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro). Requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing and export. Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells.
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TMPH-00975 | DDX1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
DDX1 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.
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TMPH-01310 | EIF3G Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit can bind 18S rRNA.; (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2.
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TMPH-00977 | DDX3X Protein, Human, Recombinant (B2M & His) | Human | E. coli | ||
DDX3X Protein, Human, Recombinant (B2M & His) is expressed in E. coli.
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TMPH-00978 | DDX3X Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
DDX3X Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus.
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TMPH-01901 | DDX53 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
DDX53 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.
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TMPH-01036 | Caprin-1/CAPRIN1 Protein, Human, Recombinant (His) | Human | Baculovirus | ||
May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types. Binds directly and selectively to MYC and CCND2 RNAs. In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs.
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TMPY-05773 | Human coronavirus (HCoV-HKU1) Nucleocapsid Protein (His) | HCoV-HKU1 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
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TMPY-03423 | MERS-CoV Nucleocapsid Protein (His) | MERS-CoV | Baculovirus-Insect Cells | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
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TMPY-01186 | Argonaute-2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Argonaute 2 (AGO2), also known as Eukaryotic translation initiation factor 2C2 (EIF2C2), belongs to the Argonaute family, AGO subfamily, which is a component of the RNA-induced silencing complex (RISC) and mediates small interfering RNA (siRNA)-directed mRNA cleavage and microRNA translational suppression. AGO2 protein is the catalytic engine of mammalian RNAi. It contains a PIWI domain that is structurally related to RNases H and possibly shares with them a two-metal-ion catalysis mechanism. Human AGO2 was unable to cleave preformed RNA duplexes and exhibited weaker binding affinity for RNA duplexes compared with the single strand RNA. The enzyme exhibited greater RNase H activity in the presence of Mn2+ compared with Mg2+. Human AGO2 exhibited weaker binding affinities and reduced cleavage activities for antisense RNAs with either a 5'-terminal hydroxyl or abasic nucleotide. In mouse hematopoiesis, AGO2 controls early development of lymphoid and erythroid cells. AGO2 is a highly specialized member of the Argonaute family with an essential nonredundant Slicer-independent function within the mammalian miRNA pathway. AGO2 regulates dFMR1 expression, and the relationship between dFMR1 and AGO2 was defined by their physical interaction and co-regulation of downstream targets. AGO2 and dFMR1 are also connected through a regulatory relationship. AGO2 is a regulator of dFMR1 expression and have clarified an important developmental role for AGO2 in the nervous system and germ line that requires dFMR1 function. In addition, AGO2 is regulated at both the transcriptional and posttranslational level, and also implicate AGO2 and enhanced micro-RNA activity in the tumorigenic progression of breast cancer cell lines.
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TMPY-05766 | Human coronavirus (HCoV-NL63) Nucleocapsid Protein (His) | HCoV-NL63 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
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TMPY-05775 | Human coronavirus (HCoV-229E) Nucleocapsid Protein (His) | HCoV-229E | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
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TMPY-05774 | Human coronavirus (HCoV-OC43) Nucleocapsid Protein (His) | HCoV-OC43 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
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TMPY-02130 | Argonaute-2 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Argonaute 2 (AGO2), also known as Eukaryotic translation initiation factor 2C2 (EIF2C2), belongs to the Argonaute family, AGO subfamily, which is a component of the RNA-induced silencing complex (RISC) and mediates small interfering RNA (siRNA)-directed mRNA cleavage and microRNA translational suppression. AGO2 protein is the catalytic engine of mammalian RNAi. It contains a PIWI domain that is structurally related to RNases H and possibly shares with them a two-metal-ion catalysis mechanism. Human AGO2 was unable to cleave preformed RNA duplexes and exhibited weaker binding affinity for RNA duplexes compared with the single strand RNA. The enzyme exhibited greater RNase H activity in the presence of Mn2+ compared with Mg2+. Human AGO2 exhibited weaker binding affinities and reduced cleavage activities for antisense RNAs with either a 5'-terminal hydroxyl or abasic nucleotide. In mouse hematopoiesis, AGO2 controls early development of lymphoid and erythroid cells. AGO2 is a highly specialized member of the Argonaute family with an essential nonredundant Slicer-independent function within the mammalian miRNA pathway. AGO2 regulates dFMR1 expression, and the relationship between dFMR1 and AGO2 was defined by their physical interaction and co-regulation of downstream targets. AGO2 and dFMR1 are also connected through a regulatory relationship. AGO2 is a regulator of dFMR1 expression and have clarified an important developmental role for AGO2 in the nervous system and germ line that requires dFMR1 function. In addition, AGO2 is regulated at both the transcriptional and posttranslational level, and also implicate AGO2 and enhanced micro-RNA activity in the tumorigenic progression of breast cancer cell lines.
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TMPY-06059 | Influenza A H1N1 (A/Guangdong-Maonan/SWL1536/2019) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-04688 | Influenza B (B/Florida/4/2006) Nucleoprotein/NP Protein (His) | Influenza B | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-00560 | Influenza A H3N2 (A/Aichi/2/1968) Nucleoprotein/NP Protein (His) | H3N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06062 | Influenza B (B/Phuket/3073/2013) Nucleoprotein/NP Protein (His) | Influenza B | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-04274 | Influenza A H1N1 (A/Brevig Mission/1/1918) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06060 | Influenza A H1N1 (A/Hawaii/70/2019) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-01382 | Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Nucleoprotein/NP Protein (I116M, His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPK-00265 | SARS-COV-2 Nucleocapsid Protein (His & Avi), Biotinylated | SARS-CoV-2 | E. coli | ||
Nucleocapsid protein (N) is the major viral structural component; its main function is to protect and encapsidate the viral RNA forming viral RNP complex. It is encoded by the S segment vRNA and is abundantly expressed in the cytoplasm of infected cells.
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TMPY-02876 | Influenza A H1N1 (A/California/07/2009) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-03955 | Influenza A H7N9 (A/Shanghai/2/2013) Nucleoprotein/NP Protein (His) | H7N9 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06057 | Influenza A H3N2 (A/Hong Kong/45/2019) Nucleoprotein/NP Protein (His) | H3N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06058 | Influenza A H3N2 (A/Hong Kong/2671/2019) Nucleoprotein/NP Protein (His) | H3N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06061 | Influenza B (B/Washington/02/2019) Nucleoprotein/NP Protein (His) | Influenza B | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-02617 | Influenza A H2N2 (A/Ann Arbor/6/1960) Nucleoprotein/NP Protein (His) | H2N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-04870 | Zika virus (ZIKV) (strain Zika SPH2015) ZIKV-NS1 protein (His) | ZIKV | HEK293 | ||
Zika virus NS1 antigen is one of seven non-structural proteins. NS1 is involved in RNA replication. The possible effects of NS1 on hosts include: localizes to host cell surface and secreted extracellularly, modulates signalling of the innate immune system, has possible damages to platelets and endothelial cells through anti-NS1 antibodies.
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TMPY-02286 | Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Matrix protein 1/M1 Protein (His) | H1N1 | E. coli | ||
The Influenza virus matrix protein 1 (M1) is a matrix protein of the influenza virus. M1 protein has been shown to play a crucial role in virus replication, assembly, and budding. It forms a coat inside the viral envelope. This is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. M1 consists of two domains connected by a linker sequence. The N-terminal domain has a multi-helical structure. The C-terminal domain also contains an alpha-helical structure. The M1 protein is the most abundant structural protein in influenza A virus particles. M1 protein of the influenza A virus plays multiple roles in virion assembly and infection. M1 protein was a candidate antigen for a broad-spectrum influenza virus vaccine and the adjuvant chitosan significantly improved the efficacy of the M1 vaccine.
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TMPY-05822 | Hepatitis B Virus (HBV)(ayw/France/Tiollais/1979) Capsid protein (His) | HBV-D | E. coli | ||
Hepatitis B virus (HBV) capsid assembly is a critical step in the propagation of the virus and is mediated by the core protein. The first cytoplasmic step in the formation of an infectious HBV virion is the formation of a capsid containing pregenomic RNA (pgRNA) and the viral polymerase (Pol). HBV capsid assembly is an attractive target for new antiviral therapies.
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