"Stromatoxin-1" Related Products

Synthetic Stromatoxin-1

Cat.No.: TOXPP-551S
Product Overview: This product is a blocker of Kv2 channels with the formula of C156H237N49O48S7.
Description: Stromatoxin-1 (ScTx-1) has been isolated from the venom of the African tarentula Stromatopelma calceata.Stromatoxin-1is a 34 amino-acid long peptide that belongs to the structural family of inhibitor cystine knot peptides reticulated by three disulfide bridges. It has an amidated C-terminus and bears strong homology with hanatoxin 1 (83%). Stromatoxin-1 inhibits with high affinities Kv2.1 and Kv2.2, that encode delayed K+channels (respectively, with IC50 of 12 and 21 nM). The block is voltage-dependent and slowly reversible. Stromatoxin-1is also a very sensitive inhibitor of Kv4.2, that encodes a transient K+current (IC50 of 1.2 nM). Here also, the block is voltage-dependent indicating that ScTx-1 acts as a gating modifier rather than a pore blocker. Reversibility is faster on Kv4.2 channels. In contrast, Stromatoxin-1has no effect on Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6 or Kv3.4 channels. The toxin has also no effect on voltage-dependent Na+and Ca2+ channels of cerebellar granule cells. Stromatoxin-1 was found to increase the spontaneous phasic contraction amplitude, muscle force and tone in isolated rat urinary bladder smooth muscle. It also enhances myogenic constriction in pressurized arterial segments.
Source: Synthetic
Species: Synthetic
Form: White lyophilized solid
Molecular Mass: 3791,3 Da
Protein length: 34
AA Sequence: AA sequence: Asp-Cys2-Thr-Arg-Met-Phe-Gly-Ala-Cys9-Arg-Arg-Asp-Ser-Asp-Cys15-Cys16-Pro-His-Leu-Gly-Cys21-Lys-Pro-Thr-Ser-Lys-Tyr-Cys28-Ala-Trp-Asp-Gly-Thr-Ile-NH2
Disulfide Bonds: Cys2-Cys16; Cys9-Cys21; Cys15-Cys28
Purity: > 98%
Reconstitution: Water or saline buffer

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Optional requirements on this protein    +Expand
C-fusion    N-fusion   Non-tagged
His    GST   Fc   Others
<1.0 eu/μg    <0.1 eu/μg   <0.01 eu/μg   Not required
Monomer Isolation    Dimer Isolation    Not required
>80% by SDS-PAGE    >90% by SDS-PAGE   >95% by SDS-PAGE   Others

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