Anti-RIC-3

Anti-RIC-3

RIC-3 Acetylcholine Receptor Chaperone, Resistant to Inhibitor of Cholinesterase 3, RIC3
Cat #: ANC-020
Sizes: 25 µl, 50 µl, 0.2 ml
Source: Rabbit
Type: Polyclonal
Applications: IH, WB
May also work in: IC, IFC, IP
Reactivity: H, M, R

Anti-RIC-3Application key:

CBE- Cell-based ELISA, FC- Flow cytometry, IC- Immunocytochemistry, IE- Indirect ELISA, IFC- Indirect flow cytometry, IH- Immunohistochemistry, IP- Immunoprecipitation, LCI- Live cell imaging, N- Neutralization, WB- Western blot

Species reactivity key:

H- Human, M- Mouse, R- Rat
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Anti-RIC-3 (#ANC-020) is a highly selective antibody directed against an epitope of the mouse protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize RIC-3 from human, mouse, and rat samples.

• Applications
• Specifications
• Scientific Background
• Related Products

Western blot

Western blot analysis of human SH-SY5Y neuroblastoma cell line lysate:
1. Anti-RIC-3 antibody (#ANC-020), (1:200).
2. Anti-RIC-3 antibody, preincubated with the control peptide antigen.

Western blot analysis of mouse heart membranes (lanes 1 and 4), rat heart lysate (lanes 2 and 5) and rat brain lysate (lanes 3 and 6):
1-3. Anti-RIC-3 antibody (#ANC-020), (1:200).
4-6. Anti-RIC-3 antibody, preincubated with the control peptide antigen.
Immunohistochemistry

Expression of RIC-3 in mouse olfactory bulb and fornix
Immunohistochemical staining of perfusion-fixed frozen mouse brain sections with Anti-RIC-3 antibody (#ANC-020), (1:400), followed by goat-anti-rabbit-AlexaFluor-488. A. RIC-3 staining in mouse olfactory bulb shows staining in the external plexiform layer (EPL) and in some glomeruli (G). Arrows point at glomeruli with RIC-3 positive core. B. RIC-3 staining in mouse fornix, is detected in neuronal profiles (vertical arrows) and neuronal processes (horizontal arrow). Cell nuclei are stained with DAPI (blue).
Immunogen
Peptide (C)EKLINRVGPNGESR, corresponding to amino acid residues 161-174 of mouse RIC-3 (Accession Q8BPM6). Intracellular, C-terminus.

HomologyRat, human – identical.
PurityAffinity purified on immobilized antigen.
FormulationLyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN₃.
Standard quality control of each lotWestern blot analysis.
Peptide confirmationConfirmed by amino acid analysis and mass spectrometry.
Storage before reconstitutionThe antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C.
Reconstitution25 µl, 50 µl or 0.2 ml double distilled water (DDW), depending on the sample size.
Antibody concentration after reconstitution0.8 mg/ml.
Storage after reconstitutionThe reconstituted solution can be stored at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing. Centrifuge all antibody preparations before use (10000 x g 5 min).
Control antigen storage before reconstitutionLyophilized powder can be stored intact at room temperature for 2 weeks. For longer periods, it should be stored at -20°C.
Control antigen reconstitution100 µl double distilled water (DDW).
Control antigen storage after reconstitution-20ºC.
Preadsorption Control1 µg peptide per 1 µg antibody.
Scientific background

RIC-3, resistance to inhibitors of cholinesterase 3, is a conserved endoplasmic reticulum-resident protein that is known to be a chaperone for the nicotinic acetylcholine receptors (nAChR) and for the serotonin channels (5-HT3 receptors)¹.

RIC-3 affects the maturation of multiple nAChRs which has been shown to facilitate nAChR assembly and trafficking^3,4.

Multiple transcripts of RIC-3 displaying differential expression are detected in humans. The full-length transcript includes two transmembrane domains followed by a coiled-coil domain, a nonconserved N-terminus and C-terminus domain, which includes a second coiled-coil domain. The short isoform lacks the coiled-coil domains and is very conserved in mammals^1,2,4.

References

1. Ben-David, Y. and Treinin, M. (2017) Oncotarget 8, 5662.
2. Ben-David, Y. et al. (2016) Mol. Brain 9, 47.
3. Safdie, G. et al. (2016) Mol. Biol. Cell 27, 2994.
4. Mulcahy, M.J. et al. (2015) PLoS One 10, e0134409.