Cholinergic Receptor, Nicotinic, beta Polypeptide 1 (Muscle) (CHRNB1) (Extracellular) antibody

Antigen: Cholinergic Receptor, Nicotinic, beta Polypeptide 1 (Muscle) (CHRNB1)

Binding Site: Extracellular

Clonality: Monoclonal

Host: Rabbit

Reactivity: Human, Rat (Rattus)

Application: Western Blotting (WB), Immunocytochemistry (ICC), Flow Cytometry (FACS)

Certificates: ISO 9001:2008

Catalog no.: ABIN649249

Additional Information

Alternative name: ACHR-beta

Gene ID: 1140

UniProt: P11230

Description: Other names: CHRNB1, ACHRB, CHRNB, Acetylcholine receptor subunit beta

Characteristics: Rabbit Monoclonal Antibody

Specificity: A synthetic peptide corresponding to residues in the extracellular region of human Acetylcholine receptor subunit beta was used as an immunogen.

Molecular Weight: 56 kDA

Comments:

Background: The nicotinic acetylcholine receptor controls electrical signaling between nerve and muscle cells by opening and closing a gated, membrane-spanning pore. The gate is a constricting hydrophobic girdle at the middle of the lipid bi-layer, formed by weak interactions between neighboring inner helices. When acetylcholine enters the ligand-binding domain, it triggers rotations of the protein chains on opposite sides of the entrance to the pore (1). The widespread distribution of the beta subunit suggests it may serve as a common subunit in different AChR combinations in various brain regions. Regulation of the expression of beta subunit appears to be relatively unrestrained, with an apparent excess of protein synthesized in the cytoplasm relative to that which ultimately arrives at functional targets in the plasma membrane (2).

Application Details

Application Notes: The suggested dilution is: WB: ~~ 1:5000 FC: ~~ 1:30 ICC: ~~ 1:100

Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Storage: ACHR-beta Antibody (extracellular) can be stored at -20°C for up to 12 months from time of receipt.

Research Area: Phospho-specific antibodies, Cell Signaling, Protein Modifications, Cell Structure, Neurology

Restrictions: For Research Use only

Publications

Product: Miyazawa, Fujiyoshi, Unwin: "Structure and gating mechanism of the acetylcholine receptor pore." in: Nature, Vol. 423, Issue 6943, pp. 949-55, 2003 (PubMed).