SNX482, Gating inhibitor of Ca v2.3, CAS No.rp174996, Gating inhibitor of Ca v2.3

CAS: rp174996 Cat. No.: rp174996
DISPONIBLE À COMMANDE
GRADE & PURITY Moligand™ ? Moligand™ — Aladdin's line of ligands and bioactive small molecules. Use for receptor, pathway, and binding studies needing defined small-molecule tools.
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Size
USA
Allemagne (EU)*
Price
Qty
500μg
rp174996-500μg
Fabrication sur commande aux États-Unis · 2–4 semaines ·
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2 399,90$US
1mg
rp174996-1mg
Fabrication sur commande aux États-Unis · 2–4 semaines ·
—
3 999,90$US
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Why this grade

Moligand™ Moligand™ for sensitive chromatographic and analytical workflows requiring minimal baseline interference.

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Storage & shipping

Room temperature Ships Check lot-specific COA for exact specifications.

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Quality documents

SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.

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Literature proof

Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.

Specifications

Product Name
SNX482, Gating inhibitor of Ca v2.3, CAS No.rp174996
Synonymes
SNX-482;toxin SNX-482
Grade
Moligand™
Spécifications et pureté
Moligand™
Type d'action
GATING INHIBITOR
Mécanisme d'action
Gating inhibitor of Ca v2.3
CAS
rp174996
Type de molécule
Peptide
Product Line
Produits biologiques
Stockage et expédition
Conditions de stockage de stockage
Room temperature

Documentation

📋 Safety Data Sheet (SDS)

Comprehensive hazard, handling, storage, and regulatory compliance document.

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✅ Certificate of Analysis (COA)

Lot-specific quality data. Enter your lot number to retrieve the exact COA.

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📊 Datasheet

Quick-reference summary of product specifications and applications.

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🔬 Specification Sheet

Full quality attributes and acceptance criteria for this grade.

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Advanced Data

Cibles associées (humaines)
CACNA1E Tchem Voltage-dependent R-type calcium channel subunit alpha-1E (0 Activities)
Activity TypeActivity Value -log(M)Mechanism of ActionActivity ReferencePublications (PubMed IDs)
Certificats (CoA, COO, BSE/TSE et tableau d'analyse)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Informations génétiques
Alternate NamesSNX-482;toxin SNX-482
Reference
  • 1. Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration., The Journal of biological chemistry, Steegborn, C C and 7 more authors.
  • 2. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences., Proceedings of the National Academy of Sciences of the United States of America, Strausberg, Robert L RL and 83 more authors.
  • 3. Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH)., Human genetics, Wang, Jian J and Hegele, Robert A RA.
  • 4. Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase., Biochemical and biophysical research communications, Lu, Y Y, O'Dowd, B F BF, Orrego, H H and Israel, Y Y.
  • 5. Single nucleotide polymorphism in CTH associated with variation in plasma homocysteine concentration., Clinical genetics, Wang, J J, Huff, A M AM, Spence, J D JD and Hegele, R A RA.
  • 6. Cystathionine gamma-lyase overexpression inhibits cell proliferation via a H2S-dependent modulation of ERK1/2 phosphorylation and p21Cip/WAK-1., The Journal of biological chemistry, Yang, Guangdong G, Cao, Kun K, Wu, Lingyun L and Wang, Rui R.
  • 7. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)., Genome research, Gerhard, Daniela S DS and 115 more authors.
  • 8. Towards a proteome-scale map of the human protein-protein interaction network., Nature, Rual, Jean-François JF and 37 more authors.
  • 9. The DNA sequence and biological annotation of human chromosome 1., Nature, Gregory, S G SG and 178 more authors.
  • 10. Polymorphisms in one-carbon metabolism and trans-sulfuration pathway genes and susceptibility to bladder cancer., International journal of cancer, Moore, Lee E LE and 14 more authors. more
Calculateurs de solution
Avis

Avis des clients

Application Protocols
  • Item-specific tested applications and dilutions: Not specified for this item; refer to CoA/Spec Sheet.
  • Example workflows (literature/general; adapt to your system)
    • Whole-cell patch clamp on Cav2.3-expressing HEK293 cells
      1. Prepare external solution (e.g., 10 mM HEPES, 140 mM TEA-Cl/NaCl mix, 2 mM CaCl2, pH 7.3). Internal solution with Cs-based salts and EGTA/BAPTA.
      2. Establish baseline I–V curves. Apply SNX-482 by bath at 50–200 nM. Record time course until steady inhibition (several minutes). Wash and assess reversibility.
      3. Fit concentration–response to estimate IC50 and Hill slope.
    • Neuronal calcium imaging
      1. Load cells with Ca2+ indicator (e.g., Fluo-4 AM). Acquire baseline responses to depolarization (KCl or field stimulation).
      2. Preincubate with SNX-482 at 50–500 nM for 10–20 minutes.
      3. Compare ΔF/F0 to determine R-type contribution; combine with blockers for N-, P/Q-, and L-type channels for subtype parsing.
    • Binding/biochemical assays
      1. Coat membranes/cells expressing Cav2.3; incubate with labeled SNX-482 analog or indirect detection format.
      2. Include nonspecific binding controls and perform competition with unlabeled peptide.
  • Notes
    • Use low-bind labware and carrier proteins to minimize adsorption. Keep vehicle controls matched and document temperature and voltage protocols.
Biological Roles
  • Nature and origin (literature/general)
    • SNX-482 is a spider-venom peptide toxin in the inhibitory cystine-knot (knottin) family. Such peptides evolved for rapid, high-affinity modulation of ion channels in prey nervous systems.
  • Molecular target (literature/general)
    • Predominant pharmacological target: Cav2.3 (α1E) voltage-gated calcium channels, mediating R-type Ca2+ currents. SNX-482 typically produces potent inhibition of Cav2.3-mediated currents with nanomolar to low-micromolar functional potencies depending on system and conditions.
    • Off-target considerations: at elevated concentrations, partial effects on other Cav subtypes or certain Kv channels have been reported; specificity depends on channel composition and membrane potential (literature).
  • Functional consequences in cells (literature/general)
    • Reduces R-type calcium influx, thereby modulating neuronal firing, dendritic Ca2+ signaling, and synaptic transmission where Cav2.3 is expressed (cortex, hippocampus, cerebellum, certain endocrine cells).
    • Useful as a tool to assign the proportion of R-type current in mixed Cav currents and to interrogate physiological roles of Cav2.3 in excitability and plasticity.
  • Experimental notes (literature/general)
    • Onset and reversibility can be slow and state-dependent; consistent holding potentials and adequate incubation improve reproducibility.
    • Combine with genetic tools (e.g., Cav2.3 knockout/knockdown) for orthogonal validation of specificity.
Buffer Applications
  • Applicability
    • SNX-482 does not serve as a buffering agent. This section addresses buffer preparation for its use in biological assays.
  • General buffer systems (literature/general)
    • Electrophysiology: HEPES-buffered saline (e.g., 10 mM HEPES, 140 mM NaCl, 2–5 mM KCl, 1–2 mM CaCl2/MgCl2, pH 7.3–7.4) with glucose; internal pipette solutions with EGTA/BAPTA as needed.
    • Calcium imaging: HEPES- or bicarbonate-buffered physiological saline; maintain consistent osmolarity and pH. Include 0.1% BSA to reduce adsorption of peptide at nM levels.
    • Biochemical binding assays: phosphate- or HEPES-based buffers at pH 7.2–7.5 with 0.01–0.05% nonionic surfactant to mitigate nonspecific binding.
  • Practical tips (literature/general)
    • Prepare concentrated SNX-482 stock in water or DMSO; dilute into final buffer immediately before use. Keep vehicle controls matched.
    • Avoid strong reducing agents (e.g., DTT at high mM) and high pH, which can disrupt disulfide bonds or promote deamidation.
    • Use low-bind tubes and precoated reservoirs to minimize peptide loss. For perfusion, pre-flush lines with peptide-containing buffer to saturate surfaces.
Green Alternatives
  • Context
    • Green chemistry considerations are not typically applied to peptide ligands used at nanomolar to micromolar levels in biological assays. Nevertheless, solvent and consumable choices can reduce environmental impact.
  • Greener handling options (literature/general)
    • Prefer aqueous buffers over organic co-solvents whenever assay-compatible.
    • Minimize DMSO usage by preparing the most concentrated practical stock and executing accurate micro-dilutions. Capture and segregate DMSO waste for appropriate disposal.
    • Use reusable glass reservoirs for perfusion systems where feasible, or certified low-bind plastics to prevent excessive overage.
  • Comparison (general)
    • DMSO vs aqueous buffer: DMSO enables higher stock concentrations but increases solvent waste and potential assay vehicle effects; aqueous buffers are more benign but may require carrier proteins.
  • Packaging/waste
    • Consolidate aliquoting to reduce repeated thawing and minimize discarded residuals. Implement institutional programs for solvent recycling and sharps minimization.
  • Trade-offs
    • Extremely low working concentrations can increase adsorption losses; adding minimal carrier proteins improves recovery but introduces biological waste streams—balance recovery versus waste burden per assay need.
Pharmaceutical Uses
  • This product is designated For research use only and is not intended for human or veterinary use.
  • No pharmacopeial monograph or excipient designation is provided for this item.
  • Typical pharmaceutical formulation roles are not applicable to SNX-482; it is used as a research ligand/toxin tool rather than a manufacturing excipient.
  • If formulation-like handling is required for in vivo research models (preclinical), investigators typically evaluate stability, vehicle compatibility, and adsorption independently; such activities fall outside the scope of this catalog entry and must comply with institutional policies and regulations.
Physical Properties
  • Item-specific values
    • Appearance: Not specified for this item; refer to CoA/Spec Sheet.
    • Molecular weight (exact), elemental analysis, water content, residual solvents: Not specified for this item; refer to CoA/Spec Sheet.
  • Literature/general properties for peptide toxins like SNX-482 (for context only; not specifications for this lot)
    • Physical state: typically supplied as lyophilized solid or film; readily forms clear solutions upon reconstitution in water, dilute acid, or DMSO depending on sequence and counter-ions.
    • Solubility: peptides of this class are commonly soluble in aqueous buffers (pH 3–7) and in polar aprotic solvents (DMSO) at stock concentrations ranging from 0.1–5 mM (literature). Final working dilutions are usually made into physiological buffers (e.g., HEPES- or phosphate-buffered saline with carrier protein) to minimize adsorption.
    • pI/logP: not meaningful in the classic small-molecule sense; amphipathic surface with net charge dependent on sequence and pH.
    • Stability: ICK/knottin peptides exhibit notable thermal and protease resistance due to the disulfide-knot topology; however, prolonged exposure to high pH, reducing agents, or repeated freeze–thaw can degrade activity (literature).
    • Hygroscopicity/adsorption: small peptides may adsorb to plastics at low nM–µM levels; loss can be mitigated by low-binding plastics and carrier proteins (literature).
Quality and Grades
  • Item-specific grade
    • Grade/Purity: Moligand™ (as listed). No additional purity metrics, additives, or formulation details are provided for this SKU.
  • Interpretation and implications (general)
    • Moligand™ is typically used to denote materials prepared/selected for ligand-screening and molecular pharmacology workflows. In practice, this often emphasizes identity authentication and performance in binding/functional assays rather than chromatographic purity benchmarks associated with small-molecule solvents or bulk reagents. Exact acceptance criteria are vendor-defined.
  • What is and is not specified for this item
    • Purity percentage, counter-ions, residual solvent/volatile content, sequence verification method, peptide content, and endotoxin/bioburden: Not specified for this item; refer to CoA/Spec Sheet.
    • Stabilizers, carrier proteins, or formulation excipients: Not specified for this item; refer to CoA/Spec Sheet.
  • Recommended user actions
    • Request and review the lot-specific CoA/SDS for sequence/identity confirmation (e.g., MS, HPLC traces), residual solvent, water content, and any stabilizers.
    • If using for quantitative pharmacology, independently verify concentration by amino acid analysis or UV absorbance where applicable, and functionally qualify in a known assay (positive control channel/cell line).
Reaction and Applications
  • Applicability
    • SNX-482 is not used as a stoichiometric/synthetic reagent. Its primary value is as a pharmacological probe in ion-channel research.
  • Research applications (literature/general)
    • Selective inhibition of Cav2.3 (R-type) voltage-gated calcium channels in heterologous expression systems (e.g., Cav2.3/β/α2δ triads in HEK293) and native neurons to dissect R-type current components.
    • Use in patch-clamp electrophysiology (whole-cell, perforated-patch) and calcium imaging to quantify R-type current contribution to neuronal excitability and synaptic transmission.
    • Pharmacological dissection: combined with other toxins/blockers (e.g., ω-conotoxin GVIA for N-type, ω-agatoxin IVA for P/Q-type, nifedipine for L-type) to parse Cav subtype mixtures (literature).
    • Structure–function studies: evaluating toxin–channel interaction surfaces, recovery from block, state-dependence, and on/off kinetics.
  • Practical tips (literature/general)
    • Prepare concentrated stocks (e.g., 10–100 µM) and store aliquots to avoid repeated freeze–thaw if frozen; include carrier protein in working solutions to minimize adsorption.
    • Allow adequate equilibration time for channel block; washout may be slow or incomplete depending on membrane potential and channel state.
    • Verify expression of Cav2.3 splice variants; sensitivity can vary by auxiliary subunit composition and holding potential.
  • Manufacturer Applications
    • None provided in the catalog entry beyond general categorization; see above for typical literature uses.
Reaction Conditions
  • Not applicable to chemical synthesis. This section provides general experimental conditions for functional assays (literature/general), not product specifications.
  • Electrophysiology conditions (typical literature practice)
    • Temperature: room temperature to physiological (22–35°C), controlled as needed.
    • Holding potentials: −70 to −90 mV for neuronal Cav currents; depolarizing steps to activate Cav2.3.
    • Toxin application: bath perfusion or local superfusion; allow several minutes for equilibration. Washout may be slow or incomplete.
    • Concentration ranges: commonly 10–500 nM for robust Cav2.3 inhibition; higher concentrations may increase off-target effects. Determine IC50 under your specific conditions.
  • Calcium imaging/binding assays
    • Buffers: HEPES-/phosphate-buffered saline at pH 7.2–7.4.
    • Incubation: 5–30 minutes pre-treatment is typical to achieve steady-state block before stimulation.
  • Controls
    • Include vehicle controls and orthogonal blockers for other Cav subtypes to confirm specificity. Validate with known Cav2.3-expressing cells or tissues.
Safety and Handling
  • Item-specific hazard data
    • GHS classification, pictograms, signal word, and H-statements: Not specified for this item; refer to SDS.
  • General safety considerations for peptide neurotoxins (literature/general)
    • Avoid inhalation of powders/aerosols and contact with skin/eyes. Handle in a chemical fume hood or biosafety cabinet appropriate for laboratory toxins.
    • Personal protective equipment (PPE): laboratory coat, nitrile gloves, and safety glasses. Change gloves frequently when handling concentrated stocks.
    • Prevent accidental exposure via sharps; use closed-tube manipulations where feasible. Decontaminate work surfaces with suitable detergents and dispose of waste following institutional toxin-handling procedures.
  • Incompatibilities (general)
    • Avoid strong oxidants or reducing agents that can alter disulfide patterns; avoid high-pH solutions that promote deamidation/aggregation.
  • First-aid overview (general; not a substitute for SDS)
    • Skin/eye contact: rinse with water for ≥15 minutes. Inhalation: move to fresh air. Ingestion/accidental exposure: seek medical attention immediately and provide SDS.
  • Emergency preparedness
    • Maintain spill kits for solids and liquids. For small dry spills, gently dampen before collection to minimize dust. Dispose following local regulations.
  • Always consult the current SDS for authoritative safety data and institutional approvals before use.
Solvent Selection
  • Applicability
    • As a peptide ligand, SNX-482 is not a conventional solvent or solute for synthetic transformations; solvent selection pertains to reconstitution and assay preparation.
  • General solvent guidance (literature/general)
    • Primary solvents: water, buffered aqueous solutions (e.g., HEPES, phosphate), or DMSO for preparing concentrated stocks. Many peptide toxins dissolve readily in slightly acidic aqueous media (pH 3–6) before dilution into physiological buffers.
    • Miscibility: DMSO stocks are fully miscible with aqueous buffers; keep final DMSO ≤0.1–0.5% v/v in sensitive electrophysiology/patch-clamp assays to minimize vehicle effects.
    • Adsorption mitigation: include carrier proteins (e.g., 0.1% BSA) or 0.05–0.1% nonionic surfactant for very low working concentrations to reduce loss to plastics and tubing (literature). Use low-bind polypropylene tubes.
  • When to choose alternatives
    • If solubility is poor in pure buffer, briefly sonicate or first dissolve in minimal DMSO before aqueous dilution. Avoid high-pH buffers and strong reducing conditions that may compromise disulfides.
  • Practical comparison (literature/general)
    • Water/buffer: physiologically relevant, minimal vehicle effects; may need carrier protein.
    • DMSO: high stock concentrations, excellent wetting; vehicle controls required.
    • Acidified water (e.g., 0.1% TFA or acetic acid): can enhance initial dissolution; ensure compatibility with downstream assays.
Storage and Reconstitution
  • Item-specific conditions
    • Storage Conditions: Room temperature (as listed). No additional details on formulation, lyophilization state, or container are provided.
    • Shipped In: Not specified for this item; refer to CoA/Spec Sheet.
  • Reconstitution (not specified for this item; general guidance only—verify with CoA/SDS before use)
    • Initial dissolution: use sterile water or assay buffer; if needed, dissolve first in minimal DMSO then dilute into buffer. Target high-concentration stocks (e.g., 10–100 µM) to minimize freeze–thaw.
    • Adsorption mitigation: prepare aliquots in low-bind tubes; include 0.1% BSA or suitable carrier for working solutions at nM concentrations when assay-compatible.
    • Avoid high pH and strong reducing agents that may disrupt disulfide bonds.
  • Handling and stability (general)
    • Protect from repeated temperature cycling and light where possible. If long-term storage is required post-reconstitution, many labs store aliquots at −20 to −80°C and avoid multiple freeze–thaw cycles (literature best practice).
  • Always defer to the lot-specific CoA and SDS for definitive storage, shipping, and reconstitution instructions.
Structure and Identity
  • Item-specific identifiers
    • SKU: rp174996
    • Product Name: SNX482 (also written SNX-482)
    • CAS: rp174996 (catalog placeholder)
    • Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
    • Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
    • SMILES / InChI / InChIKey: Not specified for this item; refer to CoA/Spec Sheet.
  • Structural features (literature/general)
    • SNX-482 is a disulfide-rich peptide toxin isolated from tarantula venom (Hysterocrates gigas). It belongs to the inhibitory cystine-knot (ICK/knottin) family typical of many spider toxins.
    • Typical architecture: ~40–45 amino acids forming a compact, β-sheet–stabilized core with three disulfide bridges that confer high thermal and proteolytic stability (literature).
    • Functional motif: surface-exposed residues mediate high-affinity binding to voltage-gated calcium channels (Cav), particularly Cav2.3 (R-type) (literature).
  • 2D description in words (literature/general)
    • A single-chain polypeptide with multiple cysteines forming an interlaced disulfide knot. Side chains include several basic and hydrophobic residues distributed over a rigid scaffold, creating a pharmacophore patch that interacts with extracellular channel loops.
  • Stereochemistry (literature/general)
    • As a ribosomally encoded peptide, amino acids are L-configured; multiple chiral centers are present at each residue’s α-carbon. Disulfide connectivity defines the tertiary fold (literature).
Synthetic Utility
  • Not a synthetic building block or reagent. SNX-482 is a biologically active peptide used as a functional probe in ion-channel research.
  • For completeness (literature/general)
    • Chemical synthesis: Solid-phase peptide synthesis (SPPS) with directed oxidative folding is used in research to prepare knottin peptides. Disulfide connectivity control and folding conditions (redox buffers, air oxidation) are critical to obtain the active ICK topology.
    • Bioconjugation: When modified, peptides of this class can be site-specifically labeled (e.g., with fluorophores or biotin) via Lys, N-terminus, or engineered tags for binding/trafficking studies; such derivatives are distinct products and outside this listing.
  • Retrosynthetic value: Not applicable for routine small-molecule retrosynthesis.
Target Specificity
  • Item-specific target data: Not specified for this item; refer to CoA/Spec Sheet.
  • Literature/general specificity profile
    • Primary target: Cav2.3 (α1E) voltage-gated calcium channels mediating R-type currents.
    • Selectivity: SNX-482 shows high functional potency against Cav2.3; at elevated concentrations and/or under certain voltage protocols, partial effects on other Cav subtypes or some Kv channels have been observed. Specificity depends on channel auxiliary subunits (β, α2δ), splice variants, and membrane potential.
    • Mechanism: extracellular peptide–channel interaction leading to inhibition of current; block can be state- and use-dependent with variable reversibility (literature).
  • Recommendation
    • Confirm target expression and assess concentration–response in your system. Employ orthogonal pharmacology/genetics to substantiate target attribution.

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