Alternative Name(s):

NACHRA3

Species: (Organism)

Homo sapiens (Human)

Gene Names:

CHRNA3

Tag info:

C-terminal 10xHis-tagged

Target Protein AA Sequence:

SEAEHRLFERLFEDYNEIIRPVANVSDPVIIHFEVSMSQLVKVDEVNQIMETNLWLKQIWNDYKLKWNPSDYGGAEFMRVPAQKIWKPDIVLYNNAVGDFQVDDKTKALLKYTGEVTWIPPAIFKSSCKIDVTYFPFDYQNCTMKFGSWSYDKAKIDLVLIGSSMNLKDYWESGEWAIIKAPGYKHDIKYNCCEEIYPDITYSLYIRRL

Expression Region:

32-240aa

Subcellular Location:

Cell junction, synapse, postsynaptic cell membrane, Multi-pass membrane protein, Cell membrane, Multi-pass membrane protein

Tissue Specificity:

Protein Length:

Extracellular Domain

Pathway:

Mol. Weight:

26.0 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Neuroscience

Function:

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

Involvement in disease:

Relevance:

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-3/CHRNA3 sub-subfamily

Reference:

"Functional interaction between Lypd6 and nicotinic acetylcholine receptors." Arvaniti M., Jensen M.M., Soni N., Wang H., Klein A.B., Thiriet N., Pinborg L.H., Muldoon P.P., Wienecke J., Imad Damaj M., Kohlmeier K.A., Gondre-Lewis M.C., Mikkelsen J.D., Thomsen M.S. J. Neurochem. 138:806-820(2016)