Recombinant Cyriopagopus schmidti Tau-theraphotoxin-Hs1a CSB-EP316743DRU
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Double-knot toxin (DkTx) (Tau-TRTX-Hs1a)
Species: (Organism)
Cyriopagopus schmidti (Chinese bird spider) (Haplopelma schmidti)
Gene Names:
N/A
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPVTTNCAKEGEVCGWGSKCCHGLDCPLAFIPYCEKYRGRND
Expression Region:
1-79aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
13.1 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:
Others
Function:
Involvement in disease:
Relevance:
Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents. It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein-protein interface and inserting hydrophobic residues into the bilayer. It also partitions naturally into membranes, with the two lobes exhibiting opposing energetics for membrane partitioning and channel activation. In addition, the toxin disrupts a cluster of hydrophobic residues behind the selectivity filter that are critical for channel activation.
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:
Reference:
"TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action." Gao Y., Cao E., Julius D., Cheng Y. Nature 534:347-351(2016)
