MilliporeSigma™ Calbiochem™ APETx2, Anthopleura elegantissima, Recombinant, E. coli

Originally isolated from sea anemone Anthopleura elegantissima , the 42 amino-acid toxin APETx2 is shown to block acidification-induced activation of homotrimeric acid-sensing ion channel composed of rat or human ASIC3, but not rat ASIC1a, ASIC1b, or ASIC2a, in a reversible man

Supplier:  MilliporeSigma™ 5.00527.0001

Catalog No. 50-052-70001

Description

Originally isolated from sea anemone Anthopleura elegantissima , the 42 amino-acid toxin APETx2 is shown to block acidification-induced activation of homotrimeric acid-sensing ion channel composed of rat or human ASIC3, but not rat ASIC1a, ASIC1b, or ASIC2a, in a reversible manner. APETx2 is also shown to inhibit the Na⁺-dependent, alkalization-induced nonconventional channel activity seen in human, but not rat, ASIC3. APETx2 in vivo efficacy is demonstrated in various rat pain induction models (100μL 2.2μM APETx2 via i.m. injection). Reported to display much reduced potency against Kv3.4 and little or no effect toward hERG, Kv2.2, Kv3.1, Kv4.2, or Kv4.3 channel activity.

Specifications

• Formulation: Supplied as a trifluoroacetate salt.
• Target Proteins: ASIC3
• Formula Weight: 4561g/mol
• Content And Storage: Protect from light
• Quantity: 100 μg

• Description: 95% by HPLC
• Molecular Formula: C₁₉₆H₂₈₀N₅₄O₆₁S₆
• Solubility: Aqueous buffer
• Form: Lyophilized