Aviva Systems Biology Corp Fmr1 Antibody 50Ug50Ul

DMSO, Molecular Biology Grade

40470006-1 100 mL
EUR 88.18

Aviva Systems Biology Laboratories manufactures the aviva systems biology corp fmr1 antibody 50ug/50ul reagents distributed by Genprice. The Aviva Systems Biology Corp Fmr1 Antibody 50Ug/50Ul reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. To purchase these products, for the MSDS, Data Sheet, protocol, storage conditions/temperature or for the concentration, please contact Aviva Systems Biology. Other Aviva products are available in stock. Specificity: Aviva Category: Systems Group: Biology Corp

Agarose, Molecular Biology Grade

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Agarose, Molecular Biology Grade

500 g Ask for price

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BCIP (Molecular Biology Grade)

250 mg
EUR 75.6

BCIP (Molecular Biology Grade)

1 g
EUR 108

CHAPS (Molecular Biology Grade)

1 g
EUR 66

CHAPS (Molecular Biology Grade)

5 g
EUR 157.2

Biology Corp information

ARP40379_P050 - Fmr1 antibody - C-terminal region (ARP40379_P050)

ARP40379_P050 100ul
EUR 389

ARP40380_P050 - FMR1 Antibody - C-terminal region (ARP40380_P050)

ARP40380_P050 100ul
EUR 389

FMR1 ELISA Kit (Human) (OKAN06412)

OKAN06412 96 Wells
EUR 950.4
Description: Description of target: The protein encoded by this gene binds RNA and is associated with polysomes. The encoded protein may be involved in mRNA trafficking from the nucleus to the cytoplasm. A trinucleotide repeat (CGG) in the 5' UTR is normally found at 6-53 copies, but an expansion to 55-230 repeats is the cause of fragile X syndrome. Expansion of the trinucleotide repeat may also cause one form of premature ovarian failure (POF1). Multiple alternatively spliced transcript variants that encode different protein isoforms and which are located in different cellular locations have been described for this gene.;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.113 ng/mL

FMR1 ELISA Kit (Human) (OKCD01047)

OKCD01047 96 Wells
EUR 997.2
Description: Description of target: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (PubMed:16631377, PubMed:18653529, PubMed:19166269, PubMed:23235829, PubMed:25464849). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA nuclear export (By similarity). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (By similarity). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein (MBP) mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (By similarity). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (By similarity). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postnyaptic dendritic spines (PubMed:11532944, PubMed:11157796, PubMed:12594214, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (By similarity). Represses mRNA translation by stalling ribosomal translocation during elongation (By similarity). Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes (PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:14703574, PubMed:17057366, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (PubMed:17057366). Plays also a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:19097999, PubMed:19166269). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (By similarity). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:7692601, PubMed:11719189, PubMed:11157796, PubMed:12594214, PubMed:17417632, PubMed:23235829, PubMed:24448548). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (PubMed:23235829). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:11719189, PubMed:18579868, PubMed:25464849, PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (PubMed:7692601, PubMed:11532944, PubMed:12594214, PubMed:15282548, PubMed:18653529). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (PubMed:15805463). Binds mRNAs containing U-rich target sequences (PubMed:12927206). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (By similarity). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (By similarity). Binds to a subset of miRNAs in the brain (PubMed:14703574, PubMed:17057366). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (PubMed:18936162). In vitro, binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:7688265, PubMed:7781595, PubMed:12950170, PubMed:15381419, PubMed:8156595). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (PubMed:20512134). Negatively regulates the voltage-dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (By similarity). Modulates the voltage-dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation (By similarity). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (By similarity). Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large-conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (PubMed:25561520). Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AFX/H2A.x and BRCA1 phosphorylations (PubMed:24813610).By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toiUniProtKB:P35922 (FMR1_MOUSE)UniProtKB:Q80WE1 (FMR1_RAT)30 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.10"The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein."_x005F_x005F_x000D_Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G._x005F_x005F_x000D_Cell 74:291-298(1993) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, INVOLVEMENT IN FRAX.Ref.13"FMR1 protein: conserved RNP family domains and selective RNA binding."_x005F_x005F_x000D_Ashley C.T. Jr., Wilkinson K.D., Reines D., Warren S.T._x005F_x005F_x000D_Science 262:563-566(1993) [PubMed] [Europe PMC] [Abstract]Cited for: ASSOCIATION IN MRNP, RNA-BINDING.Ref.14"FXR1, an autosomal homolog of the fragile X mental retardation gene."_x005F_x005F_x000D_Siomi M.C., Siomi H., Sauer W.H., Srinivasan S., Nussbaum R.L., Dreyfuss G._x005F_x005F_x000D_EMBO J. 14:2401-2408(1995) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, SUBCELLULAR LOCATION.Ref.23"Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function."_x005F_x005F_x000D_Darnell J.C., Jensen K.B., Jin P., Brown V., Warren S.T., Darnell R.B._x005F_x005F_x000D_Cell 107:489-499(2001) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN.Ref.24"The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif."_x005F_x005F_x000D_Schaeffer C., Bardoni B., Mandel J.L., Ehresmann B., Ehresmann C., Moine H._x005F_x005F_x000D_EMBO J. 20:4803-4813(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN.Ref.25"Evidence that fragile X mental retardation protein is a negative regulator of translation."_x005F_x005F_x000D_Laggerbauer B., Ostareck D., Keidel E.M., Ostareck-Lederer A., Fischer U._x005F_x005F_x000D_Hum. Mol. Genet. 10:329-338(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FXR1 AND FXR2, SUBUNIT, RNA-BINDING, CHARACTERIZATION OF VARIANT FRAX ASN-304.Ref.28"The N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding."_x005F_x005F_x000D_Adinolfi S., Ramos A., Martin S.R., Dal Piaz F., Pucci P., Bardoni B., Mandel J.L., Pastore A._x005F_x005F_x000D_Biochemistry 42:10437-10444(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, RNA-BINDING, DOMAIN.Ref.31"The fragile X mental retardation protein FMRP binds elongation factor 1A mRNA and negatively regulates its translation in vivo."_x005F_x005F_x000D_Sung Y.J., Dolzhanskaya N., Nolin S.L., Brown T., Currie J.R., Denman R.B._x005F_x005F_x000D_J. Biol. Chem. 278:15669-15678(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, ASSOCIATION WITH POLYRIBOSOME.Ref.33"The fragile X mental retardation protein binds and regulates a novel class of mRNAs containing U rich target sequences."_x005F_x005F_x000D_Chen L., Yun S.W., Seto J., Liu W., Toth M._x005F_x005F_x000D_Neuroscience 120:1005-1017(2003) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING.Ref.34"Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs."_x005F_x005F_x000D_Rackham O., Brown C.M._x005F_x005F_x000D_EMBO J. 23:3346-3355(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IGF2BP1, RNA-BINDING.Ref.35"The C-terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."_x005F_x005F_x000D_Menon R.P., Gibson T.J., Pastore A._x005F_x005F_x000D_J. Mol. Biol. 343:43-53(2004) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, INTERACTION WITH RANBP9, SUBCELLULAR LOCATION, DOMAIN.Ref.36"Biochemical and genetic interaction between the fragile X mental retardation protein and the microRNA pathway."_x005F_x005F_x000D_Jin P., Zarnescu D.C., Ceman S., Nakamoto M., Mowrey J., Jongens T.A., Nelson D.L., Moses K., Warren S.T._x005F_x005F_x000D_Nat. Neurosci. 7:113-117(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ASSOCIATION WITH MICRORNA, INTERACTION WITH AGO2.Ref.37"Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes."_x005F_x005F_x000D_Darnell J.C., Fraser C.E., Mostovetsky O., Stefani G., Jones T.A., Eddy S.R., Darnell R.B._x005F_x005F_x000D_Genes Dev. 19:903-918(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304, RNA-BINDING, DOMAIN.Ref.40"Dicer-derived microRNAs are utilized by the fragile X mental retardation protein for assembly on target RNAs."_x005F_x005F_x000D_Plante I., Davidovic L., Ouellet D.L., Gobeil L.A., Tremblay S., Khandjian E.W., Provost P._x005F_x005F_x000D_J. Biomed. Biotechnol. 2006:64347-64347(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN.Ref.42"Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses."_x005F_x005F_x000D_Antar L.N., Li C., Zhang H., Carroll R.C., Bassell G.J._x005F_x005F_x000D_Mol. Cell. Neurosci. 32:37-48(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.43"A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability."_x005F_x005F_x000D_Zalfa F., Eleuteri B., Dickson K.S., Mercaldo V., De Rubeis S., di Penta A., Tabolacci E., Chiurazzi P., Neri G., Grant S.G., Bagni C._x005F_x005F_x000D_Nat. Neurosci. 10:578-587(2007) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING.Ref.47"The G-quartet containing FMRP binding site in FMR1 mRNA is a potent exonic splicing enhancer."_x005F_x005F_x000D_Didiot M.C., Tian Z., Schaeffer C., Subramanian M., Mandel J.L., Moine H._x005F_x005F_x000D_Nucleic Acids Res. 36:4902-4912(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING.Ref.48"Fragile X mental retardation protein interactions with the microtubule associated protein 1B RNA."_x005F_x005F_x000D_Menon L., Mader S.A., Mihailescu M.R._x005F_x005F_x000D_RNA 14:1644-1655(2008) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN.Ref.49"Translational regulation of the human achaete-scute homologue-1 by fragile X mental retardation protein."_x005F_x005F_x000D_Faehling M., Mrowka R., Steege A., Kirschner K.M., Benko E., Foerstera B., Persson P.B., Thiele B.J., Meier J.C., Scholz H._x005F_x005F_x000D_J. Biol. Chem. 284:4255-4266(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, ASSOCIATION WITH POLYRIBOSOME AND MRNP.Ref.50"Fragile X mental retardation protein FMRP binds mRNAs in the nucleus."_x005F_x005F_x000D_Kim M., Bellini M., Ceman S._x005F_x005F_x000D_Mol. Cell. Biol. 29:214-228(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NXF1, RNA-BINDING, SUBCELLULAR LOCATION.Ref.51"A novel function for fragile X mental retardation protein in translational activation."_x005F_x005F_x000D_Bechara E.G., Didiot M.C., Melko M., Davidovic L., Bensaid M., Martin P., Castets M., Pognonec P., Khandjian E.W., Moine H., Bardoni B._x005F_x005F_x000D_PLoS Biol. 7:E16-E16(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN.Ref.52"Fragile X mental retardation protein controls gating of the sodium-activated potassium channel Slack."_x005F_x005F_x000D_Brown M.R., Kronengold J., Gazula V.R., Chen Y., Strumbos J.G., Sigworth F.J., Navaratnam D., Kaczmarek L.K._x005F_x005F_x000D_Nat. Neurosci. 13:819-821(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KCNT1.Ref.55"FMRP targets distinct mRNA sequence elements to regulate protein expression."_x005F_x005F_x000D_Ascano M. Jr., Mukherjee N., Bandaru P., Miller J.B., Nusbaum J.D., Corcoran D.L., Langlois C., Munschauer M., Dewell S., Hafner M., Williams Z., Ohler U., Tuschl T._x005F_x005F_x000D_Nature 492:382-386(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, CHARACTERIZATION OF VARIANT FRAX ASN-304.Ref.57"FMRP and myelin protein expression in oligodendrocytes."_x005F_x005F_x000D_Giampetruzzi A., Carson J.H., Barbarese E._x005F_x005F_x000D_Mol. Cell. Neurosci. 56:333-341(2013) [PubMed] [Europe PMC] [Abstract]Cited for: LACK OF FUNCTION, TISSUE SPECIFICITY.Ref.59"A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response."_x005F_x005F_x000D_Alpatov R., Lesch B.J., Nakamoto-Kinoshita M., Blanco A., Chen S., Stuetzer A., Armache K.J., Simon M.D., Xu C., Ali M., Murn J., Prisic S., Kutateladze T.G., Vakoc C.R., Min J., Kingston R.E., Fischle W., Warren S.T., Page D.C., Shi Y._x005F_x005F_x000D_Cell 157:869-881(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH METHYLATED HISTONE H3, DOMAIN, CHARACTERIZATION OF VARIANT FRAX GLN-138, MUTAGENESIS OF THR-102 AND TYR-103.Ref.60"MOV10 and FMRP regulate AGO2 association with microRNA recognition elements."_x005F_x005F_x000D_Kenny P.J., Zhou H., Kim M., Skariah G., Khetani R.S., Drnevich J., Arcila M.L., Kosik K.S., Ceman S._x005F_x005F_x000D_Cell Rep. 9:1729-1741(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MOV10, RNA-BINDING.Ref.64"FMRP interacts with G-quadruplex structures in the 3'-UTR of its dendritic target Shank1 mRNA."_x005F_x005F_x000D_Zhang Y., Gaetano C.M., Williams K.R., Bassell G.J., Mihailescu M.R._x005F_x005F_x000D_RNA Biol. 11:1364-1374(2014) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN, MUTAGENESIS OF SER-500.Ref.69"Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome."_x005F_x005F_x000D_Siomi H., Choi M., Siomi M.C., Nussbaum R.L., Dreyfuss G._x005F_x005F_x000D_Cell 77:33-39(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304, RNA-BINDING.Ref.75"Fragile X syndrome due to a missense mutation."_x005F_x005F_x000D_Myrick L.K., Nakamoto-Kinoshita M., Lindor N.M., Kirmani S., Cheng X., Warren S.T._x005F_x005F_x000D_Eur. J. Hum. Genet. 22:1185-1189(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FRAX GLU-266, CHARACTERIZATION OF VARIANT FRAX GLU-266, RNA-BINGING, ASSOCIATION WITH POLYRIBOSOME.Ref.76"Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures."_x005F_x005F_x000D_Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J., Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T., Klyachko V.A._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FRAX GLN-138, CHARACTERIZATION OF VARIANT FRAX GLN-138, FUNCTION, INTERACTION WITH KCNMB4, DOMAIN. Isoform 10: binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304).1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.58"Nuclear Fragile X Mental Retardation Protein is localized to Cajal bodies."_x005F_x005F_x000D_Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W._x005F_x005F_x000D_PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FRAX ASN-304 (ISOFORM 10). Isoform 6: binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304).1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.58"Nuclear Fragile X Mental Retardation Protein is localized to Cajal bodies."_x005F_x005F_x000D_Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W._x005F_x005F_x000D_PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FRAX ASN-304 (ISOFORM 10). (Microbial infection) Acts as a positive regulator of influenza A virus (IAV) replication. Required for the assembly and nuclear export of the viral ribonucleoprotein (vRNP) components.1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.62"Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus."_x005F_x005F_x000D_Zhou Z., Cao M., Guo Y., Zhao L., Wang J., Jia X., Li J., Wang C., Gabriel G., Xue Q., Yi Y., Cui S., Jin Q., Wang J., Deng T._x005F_x005F_x000D_Nat. Commun. 5:3259-3259(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH INFLUENZA A NP (MICROBIAL INFECTION), CHARACTERIZATION OF VARIANT FRAX ASN-304 (MICROBIAL INFECTION), INDUCTION (MICROBIAL INFECTION). ;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.113 ng/mL

OCOA14324-20UG - FMR1 Protein Lysate

OCOA14324-20UG 20ug
EUR 269

OCOA21433-20UG - FMR1 Protein Lysate

OCOA21433-20UG 20ug
EUR 169

OPCD03276-10UG - FMR1 Recombinant Protein

OPCD03276-10UG 10ug
EUR 139

OPCD03276-200UG - FMR1 Recombinant Protein

OPCD03276-200UG 200ug
EUR 659

OKCD01047-96W - FMR1 ELISA Kit (Human)

OKCD01047-96W 96Wells
EUR 675

AAP40379-100UG - Fmr1 Peptide - C-terminal region

AAP40379-100UG 100ug
EUR 99

AAP40380-100UG - FMR1 Peptide - C-terminal region

AAP40380-100UG 100ug
EUR 99

OKCF00001-250ML - AvivaBlot™ Pico One ECL Reagent

OKCF00001-250ML 250mL
EUR 130

OKCF00002-250ML - AvivaBlot™ Femto ECL Reagent

OKCF00002-250ML 250mL
EUR 175

ComboMiniTM Horizontal Electrophoresis System (110V)

CBMN-7 each
EUR 500

ComboMiniTM Horizontal Electrophoresis System (220V)

CBMN-8 each
EUR 530

DTT (Molecular Biology Grade)

CE131 5 g
EUR 93.6

DTT (Molecular Biology Grade)

CE132 10 g
EUR 133.2