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Synaptic functional regulator FMR1 (Fragile X mental retardation protein 1 homolog) (FMRP) (Protein FMR-1)

 FMR1_PONAB              Reviewed;         594 AA.
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
23-MAY-2018, entry version 80.
RecName: Full=Synaptic functional regulator FMR1 {ECO:0000305};
AltName: Full=Fragile X mental retardation protein 1 homolog {ECO:0000250|UniProtKB:Q06787};
Short=FMRP {ECO:0000250|UniProtKB:Q06787};
Short=Protein FMR-1 {ECO:0000250|UniProtKB:Q06787};
Name=FMR1 {ECO:0000250|UniProtKB:Q06787};
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
TISSUE=Brain cortex;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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. Plays a
role in the alternative splicing of its own mRNA. Plays a role in
mRNA nuclear export. Together with export factor NXF2, is involved
in the regulation of the NXF1 mRNA stability in neurons.
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. 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. Plays a role as a repressor of mRNA
translation during the transport of dendritic mRNAs to postnyaptic
dendritic spines. Component of the CYFIP1-EIF4E-FMR1 complex which
blocks cap-dependent mRNA translation initiation. Represses mRNA
translation by stalling ribosomal translocation during elongation.
Reports are contradictory with regards to its ability to mediate
translation inhibition of MBP mRNA in oligodendrocytes. 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. Facilitates the assembly of
miRNAs on specific target mRNAs. Plays also a role as an activator
of mRNA translation of a subset of dendritic mRNAs at synapses. In
response to mGluR stimulation, FMR1-target mRNAs are rapidly
derepressed, allowing for local translation at synapses. Binds to
a large subset of dendritic mRNAs that encode a myriad of proteins
involved in pre- and postsynaptic functions. 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. Binds to
intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of
mRNA targets. Binds to G-quadruplex structures in the 3'-UTR of
its own mRNA. Binds also to RNA ligands harboring a kissing
complex (kc) structure; this binding may mediate the association
of FMR1 with polyribosomes. Binds mRNAs containing U-rich target
sequences. 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. 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. Associates with export factor NXF1 mRNA-containing
ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner.
Binds to a subset of miRNAs in the brain. May associate with
nascent transcripts in a nuclear protein NXF1-dependent manner. 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).
Moreover, plays a role in the modulation of the sodium-activated
potassium channel KCNT1 gating activity. 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. Modulates the
voltage-dependent calcium channel CACNA1B expression at the plasma
membrane by targeting the channels for proteosomal degradation.
Plays a role in regulation of MAP1B-dependent microtubule dynamics
during neuronal development. 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. 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.
{ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787,
-!- SUBUNIT: Homodimer. Forms heterodimer with FXR1;
heterodimerization occurs in a methylation-dependent manner. Forms
heterodimer with FXR2. Homooligomer. Component of the CYFIP1-
EIF4E-FMR1 complex at least composed of CYFIP, EIF4E and FMR1;
this mRNA cap binding complex formation increases in presence of
the brain cytoplasmic RNA BC1 and is dynamically regulated in an
activity-dependent manner to repress and then possibly release
dendritic mRNAs for translation in response to mGluR stimulation.
Associates with the SMN core complex that contains SMN,
and STRAP/UNRIP. Part of a ribonucleoprotein complex with
AGO2/EIF2C2 and miRNAs. Interacts with AGO2/EIF2C2. Interacts (via
C-terminus) with CACNA1B; this interaction induces a deacrease in
the number of presynaptic functional CACNA1B channels at the cell
surface. Interacts with CYFIP1; this interaction recruits CYFIP1
to capped mRNA. Interacts with CYFIP2. Interacts with EIF5; this
interaction occurs in a RNA-dependent manner. Interacts with
dynein. Interacts with FXR1 and FXR2. Interacts with methylated
histone H3. Interacts with IGF2BP1; this interaction allows to
recruit IGF2BP1 to mRNA in a FMR1-dependent manner. Interacts (via
N-terminus) with KCNMB4. Interacts with KCNT1 (via C-terminus);
this interaction alters gating properties of KCNT1. Interacts (via
phosphorylated form) with MCRS1 (via N-terminus). Interacts with
MOV10; this interaction is direct, occurs in an RNA-dependent
manner on polysomes and induces association of MOV10 with RNAs.
Interacts with MYO5A and PURA; these interactions occur in
association with polyribosome. Interacts with NCL. Interacts with
NUFIP1. Interacts (via N-terminus) with NUFIP2. Interacts with
NXF1; this interaction occurs in a mRNA-dependent and
polyribosome-independent manner in the nucleus. Interacts with
NXF2 (via N-terminus); this interaction is direct and occurs in a
NXF1 mRNA-containing mRNP complexes. Interacts with RANBP9 (via C-
terminus); this interaction is direct and inhibits binding of FMR1
to RNA homopolymer. Interacts with RPLP0. Interacts (via C-
terminus) with SMN (via C-terminus); this interaction is direct
and occurs in a RNA-independent manner. Interacts with TDRD3 (via
C-terminus); this interaction is direct. Interacts with YBX1; this
interaction occurs in association with polyribosome. Interacts
with nucleosome. Associates with polyribosome; this association
occurs in a mRNA-dependent manner. Associates with cytoplasmic
messenger ribonucleoprotein particles (mRNPs). Associates with
microtubules in a kinesin- and dynein-dependent manner. Interacts
with HABP4. {ECO:0000250|UniProtKB:P35922,
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06787}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome,
centromere {ECO:0000250|UniProtKB:P35922}. Chromosome
{ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Stress granule
{ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic
ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}.
Perikaryon {ECO:0000250|UniProtKB:Q06787}. Cell projection
{ECO:0000250|UniProtKB:Q06787}. Cell projection, axon
{ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine
{ECO:0000250|UniProtKB:P35922}. Cell junction, synapse,
synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection,
growth cone {ECO:0000250|UniProtKB:Q06787}. Cell projection,
filopodium tip {ECO:0000250|UniProtKB:P35922}. Cell junction,
synapse {ECO:0000250|UniProtKB:P35922}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell
junction, synapse, presynaptic cell membrane
{ECO:0000250|UniProtKB:P35922}. Cell membrane
{ECO:0000250|UniProtKB:P35922}. Note=Colocalizes with H2AFX/H2A.x
in pericentromeric heterochromatin in response to DNA damaging
agents. Localizes on meiotic pachytene-stage chromosomes. Forms
nuclear foci representing sites of ongoing DNA replication in
response to DNA damaging agents. Shuttles between nucleus and
cytoplasm in a XPO1/CRM1-dependent manner. Localizes to
cytoplasmic granules, also referred to as messenger
ribonucleoprotein particles or mRNPs, along dendrites and
dendritic spines. FMR1-containing cytoplasmic granules colocalize
to F-actin-rich structures, including filopodium, spines and
growth cone during the development of hippocampal neurons. FMR1-
containing cytoplasmic granules are transported out of the soma
along axon and dendrite to synaptic contacts in a microtubule- and
kinesin-dependent manner. Colocalizes with CACNA1B in the
cytoplasm and at the cell membrane of neurons. Colocalizes with
CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region.
Colocalizes with CYFIP1 and EIF4E in dendrites and probably at
synapses. Colocalizes with FXR1, kinesin, 60S acidic ribosomal
protein RPLP0 and SMN in cytoplasmic granules in the soma and
neurite cell processes. Colocalizes with FXR1 and FXR2 in discrete
granules, called fragile X granules (FXGs), along axon and
presynaptic compartments. Colocalizes with TDRD3 in cytoplasmic
stress granules (SGs) in response to various cellular stress.
{ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787,
-!- DOMAIN: The N-terminal 134 amino acids are necessary for
homodimerization and RNA-binding. The N-terminal 298 amino acids
are sufficient to interact with KCNMB4 and to regulate presynaptic
action potential (AP) duration in neurons. The two agenet-like
domains are necessary for binding to histone H3 in a methylation-
dependent manner. The KH domains are necessary for mediating miRNA
annealing to specific RNA targets. The KH 2 domain is necessary
for binding to kissing complex (kc) RNA ligands. The RGG box
domain is necessary for binding to mRNA targets that contain G-
quadruplex structures. The RGG-box domain is necessary for binding
to a triple stem-loop RNA structure, called Sod1 stem loop
interacting with FMRP (SoSLIP), in the superoxide dismutase SOD1
mRNA. The RGG box domain is necessary for binding to its own mRNA.
The RGG-box domain is necessary for binding to homopolymer
poly(G). {ECO:0000250|UniProtKB:Q06787}.
-!- PTM: Phosphorylated. Phosphorylated on several serine residues.
Phosphorylation at Ser-479 is required for phosphorylation of
other nearby serine residues. Phosphorylation has no effect on the
binding of individual mRNA species, but may affect the association
with polyribosome. Unphosphorylated FMR1 is associated with
actively translating polyribosome, whereas a fraction of
phosphorylated FMR1 is associated with apparently stalled
polyribosome. Dephosphorylation by an activated phosphatase may
release the FMR1-mediated translational repression and allow
synthesis of a locally required protein at snypases.
{ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787}.
-!- PTM: Monoubiquitinated. Polyubiquitinated. Ubiquitinated and
targeted for proteasomal degradation after activation of
metabotropic glutamate receptor (mGluR).
-!- PTM: Methylated; methylation is necessary for heterodimerization
with FXR1, association with polyribosomes, recruitment into stress
granules and translation of FMR1 target mRNAs. Methylated by
PRMT1, PRMT3 and PRMT4, in vitro. {ECO:0000250|UniProtKB:Q06787}.
-!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; CR859475; CAH91646.1; -; mRNA.
RefSeq; NP_001125966.1; NM_001132494.1.
UniGene; Pab.6654; -.
ProteinModelPortal; Q5R9B4; -.
SMR; Q5R9B4; -.
STRING; 9601.ENSPPYP00000023279; -.
PRIDE; Q5R9B4; -.
GeneID; 100172902; -.
KEGG; pon:100172902; -.
CTD; 2332; -.
eggNOG; ENOG410IF9J; Eukaryota.
HOGENOM; HOG000293377; -.
HOVERGEN; HBG005739; -.
InParanoid; Q5R9B4; -.
KO; K15516; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; ISS:UniProtKB.
GO; GO:0010369; C:chromocenter; ISS:UniProtKB.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:1902737; C:dendritic filopodium; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:1990812; C:growth cone filopodium; ISS:UniProtKB.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0098793; C:presynapse; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0033592; F:RNA strand annealing activity; ISS:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
GO; GO:1900453; P:negative regulation of long term synaptic depression; ISS:UniProtKB.
GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0033129; P:positive regulation of histone phosphorylation; ISS:UniProtKB.
GO; GO:1902416; P:positive regulation of mRNA binding; ISS:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
GO; GO:0098908; P:regulation of neuronal action potential; ISS:UniProtKB.
GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 1.
InterPro; IPR008395; Agenet-like_dom.
InterPro; IPR032196; FXMR_C2.
InterPro; IPR022034; FXMRP1_C_core.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF05641; Agenet; 1.
Pfam; PF16098; FXMR_C2; 1.
Pfam; PF12235; FXMRP1_C_core; 1.
Pfam; PF00013; KH_1; 2.
SMART; SM00322; KH; 2.
SUPFAM; SSF54791; SSF54791; 2.
PROSITE; PS50084; KH_TYPE_1; 2.
2: Evidence at transcript level;
Acetylation; Activator; Cell junction; Cell membrane; Cell projection;
Centromere; Chromosome; Complete proteome; Cytoplasm; DNA damage;
Membrane; Methylation; mRNA processing; mRNA splicing; mRNA transport;
Neurogenesis; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Synapse; Synaptosome;
Translation regulation; Transport; Ubl conjugation.
CHAIN 1 594 Synaptic functional regulator FMR1.
DOMAIN 4 50 Agenet-like 1. {ECO:0000255|PROSITE-
DOMAIN 63 115 Agenet-like 2. {ECO:0000255|PROSITE-
DOMAIN 218 279 KH 1. {ECO:0000255|PROSITE-
DOMAIN 281 348 KH 2. {ECO:0000255|PROSITE-
REGION 1 184 Required for nuclear localization.
REGION 172 211 Necessary for interaction with CYFIP1,
CYFIP2, FXR1 and FXR2.
REGION 376 470 Required for nuclear export.
REGION 398 594 Interaction with RANBP9.
REGION 513 527 RNA-binding RGG-box. {ECO:0000250}.
MOTIF 403 422 Nuclear export signal.
MOTIF 506 513 Nucleolar localization signal 1.
MOTIF 575 579 Nucleolar localization signal 2.
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 337 337 Phosphoserine.
MOD_RES 370 370 Phosphoserine.
MOD_RES 442 442 Phosphothreonine.
MOD_RES 450 450 Omega-N-methylarginine.
MOD_RES 479 479 Phosphoserine.
MOD_RES 523 523 Omega-N-methylarginine; alternate.
MOD_RES 523 523 Omega-N-methylated arginine; alternate.
MOD_RES 582 582 Phosphoserine.
SEQUENCE 594 AA; 67057 MW; C465B5790C6BEB0D CRC64;

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