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Magic™ Membrane Protein Human CHRNB3 (Cholinergic receptor nicotinic beta 3 subunit) Full Length (CAT#: MPC0471K) Made to Order

This product is a 52.7 kDa Human CHRNB3 membrane protein expressed in HEK293. The protein is for research use only and is not approved for use in humans or in clinical diagnosis.

Product Specifications

  • Host Species
  • Human
  • Target Protein
  • CHRNB3
  • Protein Length
  • Full length
  • Protein Class
  • Transporter; Ion channel
  • Molecular Weight
  • 52.7 kDa
  • TMD
  • 4
  • Sequence
  • MLPDFMLVLIVLGIPSSATTGFNSIAENEDALLRHLFQGYQKWVRPVLHS
    NDTIKVYFGLKISQLVDVDEKNQLMTTNVWLKQEWTDHKLRWNPDDYGGI
    HSIKVPSESLWLPDIVLFENADGRFEGSLMTKVIVKSNGTVVWTPPASYK
    SSCTMDVTFFPFDRQNCSMKFGSWTYDGTMVDLILINENVDRKDFFDNGE
    WEILNAKGMKGNRRDGVYSYPFITYSFVLRRLPLFYTLFLIIPCLGLSFL
    TVLVFYLPSDEGEKLSLSTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYL
    LFIMIFVTLSIIVTVFVINVHHRSSSTYHPMAPWVKRLFLQKLPKLLCMK
    DHVDRYSSPEKEESQPVVKGKVLEKKKQKQLSDGEKVLVAFLEKAADSIR
    YISRHVKKEHFISQVVQDWKFVAQVLDRIFLWLFLIVSVTGSVLIFTPAL
    KMWLHSYH

Product Description

  • Expression Systems
  • HEK293
  • Tag
  • Flag-StrepII or based on specific requirements
  • Protein Format
  • Detergent or based on specific requirements

Target

  • Target Protein
  • CHRNB3
  • Full Name
  • Cholinergic receptor nicotinic beta 3 subunit
  • Introduction
  • 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.
  • Alternative Names
  • neuronal acetylcholine receptor subunit beta-3; acetylcholine receptor, neuronal nicotinic, beta-3 subunit; acetylcholine receptor, nicotinic, beta 3 (neuronal); cholinergic receptor, nicotinic beta 3; cholinergic receptor, nicotinic, beta 3 (neuronal); cholinergic receptor, nicotinic, beta polypeptide 3; CHRNB3; Cholinergic receptor nicotinic beta 3 subunit

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