| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | TPN-Q, Kir3.2 K+ channels |
| Cas No. | |
| Concentration | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Solubility | Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. The product is soluble in pure water at high micromolar concentrations (100 µM - 1 mM). For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in double-distilled water (ddH2O) at a concentration between 100-1000x of the final working concentration. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. Centrifuge all product preparations before use. It is recommended to prepare fresh solutions in working buffers just before use. Avoid multiple freeze-thaw cycles to maintain biological activity. |
| Source | Synthetic peptide |
| Species | |
| Storage | |
| Target |
Overview
Tertiapin-Q is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to Kir1.1, Kir3.2 K+ channels biology and/or assay development. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Electrophysiology, Electrophysiology.
Key elements and design rationale
- Molecular identity: CAS: 910044-56-3, MW: 2452 Da, Formula: C106H175N35O24S4.
- Source / origin: Apis mellifera (Honeybee).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys3-Cys14, Cys5-Cys18 Lys21 - C-terminal amidation ATTO Fluor-488
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological background
Tertiapin, the native toxin, was originally isolated from European honey bee Apis mellifera venoM Native and synthetic Tertiapin blocks a range of inward rectifier K+ channels (Kir), in particular ROMK1 (Kir1.1, IC50 = 2 nM) and GIRK (Kir3 family, IC50 for the Kir3.1/3.4 heteromer was 8.6 nM) but with no effect on the Kir2 family member1. In accordance, it was shown to inhibit acetylcholine induced K+ currents in mammalian cardiomyocytes2,3.Tertiapin-Q is a derivative of Tertiapin in which Met13 is substituted by a Gln residue. However, unlike native Tertiapin, Tertiapin-Q is non-oxidizable and therefore is more stable4.Tertiapin-Q inhibits the above-mentioned channels with similar affinities and also inhibits Ca2-activated large conductance BK-type K+ channels in a concentration and voltage-dependent manner5.
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Electrophysiology: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Electrophysiology: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
Jin, W. and Lu, Z.
(1998) Biochemistry 37, 13291.
Drici, M.D.
et al. (2000) Br. J. Pharmacol. 131, 569.
Kitamura, H.
et al. (2000) J. Pharmacol. Exp. Ther. 293, 196.
Peleg, S.
et al. (2002) Neuron 33, 87.
Kanjhan, R.
et al. (2005) J. Pharmacol. Exp. Ther.314, 1353.
Jin, W. and Lu, Z.
(1998) Biochemistry 37, 13291.
Drici, M.D.
et al. (2000) Br. J. Pharmacol. 131, 569.
Kitamura, H.
et al. (2000) J.Pharmacol. Exp. Ther. 293, 196.
