Anti-FMRP (Ser499) Antibody

Our Anti-FMRP (Ser499) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects chicken, human, mouse, and rat FMRP (Ser499) and is antigen affinity purified from pooled serum. It is great for use in WB, IHC.



SKU: p1125-499

Volume: 100 µL
1-2 business days
Price:
Sale price$445.00

Product Details

FMRP (Ser499)
Fragile X Mental Retardation Protein (FMRP) is an RNA-binding protein that plays an essential role in cognitive brain function. Mutations in the FMR1 gene, which codes for FMRP, can result in fragile X syndrome, autism, as well as other cognitive deficits (Brown et al.,1998, Goodlin-Jones et al., 2004). Phosphorylation of the highly conserved Ser-499 has been shown to trigger hierarchical phosphorylation of nearby serines and may play a role in suppressing target mRNA translation (Ceman et al., 2003, Narayanan et al. 2008).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
IHC, WB
Rabbit
FMR1
71 kDa
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser499 of rat FMRP, conjugated to keyhole limpet hemocyanin (KLH).
Chicken, Human, Mouse, Rat
Bovine, Canine, Non-Human Primate, Sheep, Xenopus, Zebrafish
AB_2492094
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho and non-phosphopeptide affinity columns.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
WB Brain: 1:1000
IHC: 1:250-1:1000
Unconjugated
Specific for endogenous levels of the ~71 kDa FMRP protein phosphorylated at Ser499. Immunolabeling is completely eliminated by treatment with λ-phosphatase.
Phosphorylated
Ser499
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Blue Ice
FMR 1 antibody, Fmr1 antibody, Fmr1 gene antibody, FMR1_HUMAN antibody, FMRP antibody, Fragile X mental retardation 1 antibody, Fragile X mental retardation 1 protein antibody, Fragile X mental retardation protein 1 antibody, Fragile X mental retardation protein antibody, fragile X mental retardation syndrome-related protein 1 antibody, fragile X mental retardation autosomal homolog 1 antibody, FRAXA antibody, fxr1 antibody, MGC87458 antibody, POF antibody, POF1 antibody, Protein FMR-1 antibody, Protein FMR1 antibody, wu:fb16f11 antibody, wu:fd18c10 antibody, zgc:66226 antibody
24948

Product Specific References for Applications and Species

Immunohistochemistry: Chicken
PMID Dilution Publication
26719241 1:1000 Guimarães-Souza, E.M., et al. 2016. Fragile X Mental Retardation Protein expression in the retina is regulated by light. Experimental Eye Research, 146, pp.72-82.
Immunohistochemistry: Human
PMID Dilution Publication
30630951 1:250-1:1000 Chen, Y., et al. 2019. Aggregation of the nucleic acid–binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation. Journal of Biological Chemistry, 294(10), pp.3696-3706.
Immunohistochemistry: Mouse
PMID Dilution Publication
357285961:200Monday, H.R., et al. 2022. Presynaptic FMRP and local protein synthesis support structural and functional plasticity of glutamatergic axon terminals. Neuron, .
26719241 1:1000 Guimarães-Souza, E.M., et al. 2016. Fragile X Mental Retardation Protein expression in the retina is regulated by light. Experimental Eye Research, 146, pp.72-82.
Western Blot: Chicken
PMID Dilution Publication
32449186 not listed Yu, X., et al. 2020. Dynamics of the Fragile X Mental Retardation Protein Correlates with Cellular and Synaptic Properties in Primary Auditory Neurons following Afferent Deprivation. Journal of Comparative Neurology.
26719241 1:2000 Guimarães-Souza, E.M., et al. 2016. Fragile X Mental Retardation Protein expression in the retina is regulated by light. Experimental Eye Research, 146, pp.72-82.
Western Blot: Human
PMID Dilution Publication
30630951 1:1000 Chen, Y., et al. 2019. Aggregation of the nucleic acid–binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation. Journal of Biological Chemistry, 294(10), pp.3696-3706.
Western Blot: Mouse
PMID Dilution Publication
37949069not listedZou, Z, et al. 2023. FMRP phosphorylation modulates neuronal translation through YTHDF1. Molecular cell, 4304-4317.
360678231:1000Ardourel, M., et al. 2022. FMRP-related Retinal Phenotypes: Evidence of Glutamate-Glutamine Metabolic Cycle Impairment. Experimental Eye Research, 109238.
35191199 not listed Yildirim, Z., et al. 2019. Intercepting IRE1 kinase-FMRP signaling prevents atherosclerosis progression. EMBO Molecular Medicine, p.e15344.
31112584 1:1000 DeMarco, B., et al. 2019. FMRP-G-quadruplex mRNA-miR-125a interactions: Implications for miR-125a mediated translation regulation of PSD-95 mRNA. PloS One, 14(5), p.e0217275.
27957526 1:1000 Bartley, C.M., et al. 2016. Mammalian FMRP S499 is phosphorylated by CK2 and promotes secondary phosphorylation of FMRP. eNeuro, 3(6).
26719241 1:2000 Guimarães-Souza, E.M., et al. 2016. Fragile X Mental Retardation Protein expression in the retina is regulated by light. Experimental Eye Research, 146, pp.72-82.
26580204 1:500 Reynolds, C.D., et al. 2015. FMRP S499 is phosphorylated independent of mTORC1-S6K1 activity. PLoS One, 9(5), p.e96956.
24806451 not listed Bartley, C.M., et al. 2014. FMRP S499 is phosphorylated independent of mTORC1-S6K1 activity. PLoS One, 9(5), p.e96956.
Western Blot: Rat
PMID Dilution Publication
374941911:500Winden, KD, et al. 2023. Increased Degradation of FMRP Contributes to Neuronal Hyperexcitability in Tuberous Sclerosis Complex. Cell reports, 112838.
23831253 not listed Bernard, P.B., et al. 2013. Phosphorylation of FMRP and alterations of FMRP complex underlie enhanced mLTD in adult rats triggered by early life seizures. Neurobiology of Disease, 59, pp.1-17.

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