APPLICATION
Application Note
*Optimal dilutions/concentrations should be determined by the researcher.
Application |
Recommended Dilution |
1-3μg/ml |
Not tested in other applications.
Calculated MW
Positive Control
The peptide used to generate this antibody is available for purchase (GTX88687-PEP).
Predict Reactivity
Mouse, Rat(>80% identity)
PROPERTIES
Form
Liquid
Buffer
TBS, 0.5% BSA
Preservative
0.02% Sodium azide
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
0.50 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Human
Immunogen
Peptide with sequence C-SRHVKKEHFISQ, from the internal region of the protein sequence according to NP_000740.1.
Purification
Purified by ammonium sulphate precipitation followed by antigen affinity chromatography
Conjugation
Unconjugated
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
TARGET
Synonyms
cholinergic receptor nicotinic beta 3 subunit
Cellular Localization
Cell membrane; Multi-pass membrane protein
Background
The nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The nAChRs are (hetero)pentamers composed of homologous subunits. The subunits that make up the muscle and neuronal forms of nAChRs are encoded by separate genes and have different primary structure. There are several subtypes of neuronal nAChRs that vary based on which homologous subunits are arranged around the central channel. They are classified as alpha-subunits if, like muscle alpha-1 (MIM 100690), they have a pair of adjacent cysteines as part of the presumed acetylcholine binding site. Subunits lacking these cysteine residues are classified as beta-subunits (Groot Kormelink and Luyten, 1997 [PubMed 9009220]). Elliott et al. (1996) [PubMed 8906617] stated that the proposed structure for each subunit is a conserved N-terminal extracellular domain followed by 3 conserved transmembrane domains, a variable cytoplasmic loop, a fourth conserved transmembrane domain, and a short C-terminal extracellular region.[supplied by OMIM, Apr 2010]
Database
Research Area
DATA IMAGES
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GTX88687 WB Image
WB analysis of human cerebellum lysate using GTX88687 AChR beta 3 antibody, Internal. Dilution : 1μg/ml Loading : 35μg protein in RIPA buffer
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REFERENCE
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REVIEW
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