Alternative Name(s):

CHRNA1Acetylcholine receptor subunit alpha

Species: (Organism)

Torpedo californica (Pacific electric ray)

Gene Names:

CHRNA1

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

SEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLISVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRI

Expression Region:

25-234aa

Subcellular Location:

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

Tissue Specificity:

Protein Length:

Partial

Pathway:

Mol. Weight:

28.8 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-1/CHRNA1 sub-subfamily

Reference:

"Proteolytic fragments of the nicotinic acetylcholine receptor identified by mass spectrometry: implications for receptor topography." Moore C.R., Yates J.R. III, Griffin P.R., Shabanowitz J., Martino P.A., Hunt D.F., Cafiso D.S. Biochemistry 28:9184-9191(1989)