Mouse Anti-GNAO1 Recombinant Antibody (CBLG1-1410) (V2LY-0226-LY151)

Name: Mouse Anti-GNAO1 Recombinant Antibody (CBLG1-1410)
SKU: V2LY-0226-LY151
Rating: 5 (1 reviews)

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Published Data

Mouse Anti-GNAO1 Recombinant Antibody (CBLG1-1410) (V2LY-0226-LY151) in IHC

IHC images of regenerative nerves from Gnao1-NKD mice and controls, MAG for regenerative myelin-associated protein (red), GFP for viral expression (green), scale bar = 500 μm. Zoomed in is the enlargement of the white box area, scale bar = 100 μm. ...View More

Xu, J., Peng, Q., Cai, J., Shangguan, J., Su, W., Chen, G., Sun, H., Zhu, C., & Gu, Y. (2024). The Schwann cell-specific G-protein Gαo (Gnao1) is a cell-intrinsic controller contributing to the regulation of myelination in peripheral nerve system. Acta neuropathologica communications, 12(1), 24. https://doi.org/10.1186/s40478-024-01720-3

Mouse Anti-GNAO1 Recombinant Antibody (CBLG1-1410) (V2LY-0226-LY151) in WB

The expression of MAG in the regenerated nerves of Gnao1-SKD mice and controls (Ctrl) was detected by WB. As shown are representative WB images (up) and the statistical histogram (bottom). T-test, n = 3, Ns, p > 0.05 vs control, no statistical difference. ...View More

Mouse Anti-GNAO1 Recombinant Antibody (CBLG1-1410) (V2LY-0226-LY151) in Immunoblot

Localization of Go in sucrose density gradient in developing and adult cerebella. A, immunoprecipitation of developing (postnatal day 7) and adult cerebellar membranes with anti-Go antibody. Immunoprecipitates were subjected to SDS-PAGE and immunoblotted using an anti-G antibody. Precipitates were obtained using anti-Go antibody (lanes 4 and 6) or control mouse IgG (lanes 3 and 5) from developing (lanes 3 and 4) and adult (lanes 5 and 6) cerebella. Lanes 1 and 2 show the lysate of the developing and adult cerebellar membranes, respectively. The top arrow with the solid line indicates the bands of G proteins, and the bottom arrow with the dotted line indicates the nonspecific binding protein to mouse IgG or protein G-Sepharose
during immunoprecipitation. B, the membrane fractions from a developing cerebellum (postnatal day 7) and an adult cerebellum were solubilized with Tx, subjected to sucrose gradient centrifugation, and fractionated from the top to the bottom (fractions 1-10). Go, G, Lyn, and transferrin receptor (TfR) in each fraction were detected by immunoblotting. Lanes 2-5 and 7-10 correspond to the DRM and non-DRM fractions, respectively. C, postnatal day 7 cerebellar membranes were treated with PTX or MCD as described under "Experimental Procedures," followed by solubilization and separation of the DRM and non-DRM fractions. Go in each fraction was detected by immunoblotting (IB). ...View More

Yuyama, K., Sekino-Suzuki, N., Sanai, Y., & Kasahara, K. (2007). Translocation of activated heterotrimeric G protein Galpha(o) to ganglioside-enriched detergent-resistant membrane rafts in developing cerebellum. The Journal of biological chemistry, 282(36), 26392-26400. https://doi.org/10.1074/jbc.M705046200

Mouse Anti-GNAO1 Recombinant Antibody (CBLG1-1410) (V2LY-0226-LY151) in IF

G-protein immunohistochemistry on sections of the olfactory mucosa of Chiloscyllium punctatum. The five antisera against G-protein α-subunits used labeled different olfactory receptor neurons (ORNs) (left column, red fluorescence) and Hoechst stained all nuclei (blue). (First row) antisera against Gαs/olf labeled mainly long ORNs, which soma sits in the lower layers of the neuroepithelium. These elongated cells have a rounded nucleus occupying most of the soma, a long and relatively narrow dendrite ending in an apical knob, which protrusions were not clearly associated with their soma. This marker also labeled other somas in the intermediate to low layers of the neuroepithelium (sometimes with associated cilia above the neuroepithelium surface but no dendrite clearly labeled), and randomly scattered cilia (sectioned or not). Sectioned labeled cilia showed in inset image. (Second row) antisera against Gαq/11/14 labeled mainly microvillous and crypt ORNs (inset image), and partial labeling of ORN dendrites in the upper neuroepithelium. (Third row) antisera against Gαi-1/2/3 labeled intermediate somas and possible associated cilia, some more faint apical cells, as well as progenitor cells in the basal layer (inset image). (Fourth row) antisera against Gαi-3 labeled somas in lower half of the neuroepithelium, possible associated cilia, and ORN axons in the lamina propria. (Fifth row) antisera against Gαo labeled the somas of different microvilli-bearing ORN populations, including the microvillous morphotype, the pear-shaped morphotype with a swelled dendrite, and the teardrop-shaped morphotype, as well as some short (perhaps sectioned) cilia close to the apical membrane, and scarce longer cilia (inset image). White arrowheads, labeled cilia. Scale bars = 10 μm. ...View More

Camilieri-Asch, V., Caddy, H. T., Hubbard, A., Rigby, P., Doyle, B., Shaw, J. A., Mehnert, A., Partridge, J. C., Yopak, K. E., & Collin, S. P. (2020). Multimodal Imaging and Analysis of the Neuroanatomical Organization of the Primary Olfactory Inputs in the Brownbanded Bamboo Shark, Chiloscyllium punctatum. Frontiers in neuroanatomy, 14, 560534. https://doi.org/10.3389/fnana.2020.560534

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBLG1-1410

Application

WB, IP, IF

Immunogen

Cattle GNAO1.

Host Species

Mouse

Specificity

Human, Mouse, Rat, Cattle

Antibody Isotype

IgG1, κ

Clonality

Monoclonal

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

PBS, gelatin

Preservative

Sodium azide

Concentration

0.2 mg/ml

Purity

> 95% Purity determined by SDS-PAGE.

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

guanine nucleotide binding protein, alpha O

Entrez Gene ID

2775

UniProt ID

P09471

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14.

Biological Process

Adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: GO_Central
Aging Source: Ensembl
Dopamine receptor signaling pathway Source: GO_Central
Forebrain development Source: Ensembl
Locomotory behavior Source: Ensembl
Muscle contraction Source: ProtInc
Negative regulation of calcium ion transport Source: Ensembl
Neuron projection development Source: Ensembl
Odontogenesis of dentin-containing tooth Source: Ensembl
Positive regulation of GTPase activity Source: Ensembl
Regulation of heart contraction Source: Ensembl
Response to cytokine Source: Ensembl
Response to drug Source: Ensembl
Response to hydrogen peroxide Source: Ensembl
Response to morphine Source: Ensembl

Cellular Location

Cell membrane; Membrane

Involvement in disease

Developmental and epileptic encephalopathy 17 (DEE17):
A severe neurologic disorder characterized by onset of intractable seizures in the first weeks or months of life and usually associated with EEG abnormalities. Affected infants have very poor psychomotor development and may have brain abnormalities, such as cerebral atrophy or thin corpus callosum. Some patients may show involuntary movements.
Neurodevelopmental disorder with involuntary movements (NEDIM):
A neurodevelopmental disorder manifesting with a wide range of clinical symptoms. Clinical features range from severe motor and cognitive impairment with marked choreoathetosis, self-injurious behavior and epileptic encephalopathy, to a milder phenotype featuring moderate developmental delay associated with complex stereotypies, mainly facial dyskinesia, and mild epilepsy. Hyperkinetic movements are often exacerbated by specific triggers, such as illness, emotion and high ambient temperature. Some patients have brain abnormalities, such as cerebral atrophy or thin corpus callosum.

PTM

Histaminylated at Gln-205 residues by TGM2.

Katanaev, V. L., Valnohova, J., Silachev, D. N., Larasati, Y. A., & Koval, A. (2023). Pediatric GNAO1 encephalopathies: from molecular etiology of the disease to drug discovery. Neural Regeneration Research, 18(10), 2188-2189.

Wirth, T., Garone, G., Kurian, M. A., Piton, A., Millan, F., Telegrafi, A., ... & Anheim, M. (2022). Highlighting the dystonic phenotype related to GNAO1. Movement Disorders, 37(7), 1547-1554.

Wang, D., Dao, M., Muntean, B. S., Giles, A. C., Martemyanov, K. A., & Grill, B. (2022). Genetic modeling of GNAO1 disorder delineates mechanisms of Gαo dysfunction. Human Molecular Genetics, 31(4), 510-522.

Di Rocco, M., Galosi, S., Lanza, E., Tosato, F., Caprini, D., Folli, V., ... & Martinelli, S. (2022). Caenorhabditis elegans provides an efficient drug screening platform for GNAO1-related disorders and highlights the potential role of caffeine in controlling dyskinesia. Human Molecular Genetics, 31(6), 929-941.

Axeen, E., Bell, E., Viehoever, A. R., Schreiber, J. M., Sidiropoulos, C., & Goodkin, H. P. (2021). Results of the first GNAO1-related neurodevelopmental disorders caregiver survey. Pediatric Neurology, 121, 28-32.

Kelly, M., Park, M., Mihalek, I., Rochtus, A., Gramm, M., Pérez‐Palma, E., ... & Murdock, D. R. (2019). Spectrum of neurodevelopmental disease associated with the GNAO1 guanosine triphosphate–binding region. Epilepsia, 60(3), 406-418.

Schirinzi, T., Garone, G., Travaglini, L., Vasco, G., Galosi, S., Rios, L., ... & Leuzzi, V. (2019). Phenomenology and clinical course of movement disorder in GNAO1 variants: results from an analytical review. Parkinsonism & Related Disorders, 61, 19-25.

Koy, A., Cirak, S., Gonzalez, V., Becker, K., Roujeau, T., Milesi, C., ... & Cif, L. (2018). Deep brain stimulation is effective in pediatric patients with GNAO1 associated severe hyperkinesia. Journal of the Neurological Sciences, 391, 31-39.

Feng, H., Khalil, S., Neubig, R. R., & Sidiropoulos, C. (2018). A mechanistic review on GNAO1-associated movement disorder. Neurobiology of disease, 116, 131-141.

Waak, M., Mohammad, S. S., Coman, D., Sinclair, K., Copeland, L., Silburn, P., ... & Malone, S. (2018). GNAO1-related movement disorder with life-threatening exacerbations: movement phenomenology and response to DBS. Journal of Neurology, Neurosurgery & Psychiatry, 89(2), 221-222.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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