Every lot is tried & tested in a relevant biological assay.
- Zafaralla, G.C. et al. (1988) Biochemistry 27, 7102.
- Alomone Labs α-Conotoxin SI inhibits muscle nicotinic ACh receptors expressed in Xenopus oocytes.A. Representative time course of α-Conotoxin SI (#STC-825) inhibition of α1/β1/γ/δ nAChR currents, elicited every 50 sec by transient application of 20 µM acetylcholine, while membrane potential was held at -80 mV, and reversibly inhibited by 0.2 µM and 1 µM α-Conotoxin SI (top horizontal bars). B. Superimposed traces of α1/β1/γ/δ nAChR currents upon application of control, 0.2 µM and 1 µM α-Conotoxin SI (taken from the recording in A).
α-Conotoxin SI is a 13-amino acid residue peptide toxin originally isolated from Conus striatus venom. The toxin’s structure is stabilized by six hydrogen bonds and disulfides between cysteine residues 2 and 7 and 3 and 131. It is a potent and selective antagonist of α1/β1/δ/γ nicotinic acetylcholine receptors (nAChRs).
Nicotinic acetylcholine receptors are ionotropic multi-subunit, neurotransmitter-gated receptors of the cholinergic system. They are responsible for mediating the effects of the neurotransmitter acetylcholine (ACh). nAChRs are assembled from one or more α subunits (α1-α10) alone or together with one or more β subunits (β1–β4)2.
α-Conotoxin SI (#STC-825) is a highly pure, synthetic, and biologically active peptide toxin.
- α-Conotoxin EI (#STC-900)
- α-Conotoxin GI (#STC-500)
- α-Conotoxin MI (#STC-370)
- αA-Conotoxin OIVA (#STC-520)
- αA-Conotoxin PIVA (#STC-600)
- αC-Conotoxin PrXA (#STC-620)
- Anti-Nicotinic Acetylcholine Receptor β1 (CHRNB1) (extracellular) Antibody (#ANC-011)
- Anti-Nicotinic Acetylcholine Receptor α1 (CHRNA1) (extracellular) Antibody (#ANC-001)
- Muscle-Type nAChR Basic Research Pack (#ESB-900)
- Muscle-Type nAChR Premium Research Pack (#ESP-900)
- Muscle-Type nAChR Deluxe Research Pack (#ESD-900)
- Muscle Specific nAChR Antagonist Explorer Kit (#EK-207)