| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | MCa, Maurocalcin |
| 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 | Recombinant, E. coli |
| Species | |
| Storage | |
| Target |
Overview
Maurocalcine is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to Ryanodine receptors 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 Calcium imaging assay.
Key elements and design rationale
- Molecular identity: CAS: 269745-22-4, MW: 3858.6 Da, Formula: C156H270N56O46S6.
- Source / origin: Scorpio maurus palmatus (Israeli golden scorpion).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys3-Cys17, Cys10-Cys21 and Cys16-Cys32
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
Maurocalcine (MCa) is a peptidyl toxin originally isolated from the venom of the scorpion Scorpio maurus palmatus.Native MCa is present at a low concentration in the venom (0.5% of total protein). This 33-mer basic peptide contains three disulfide bridges and has 82% sequence homology to Imperatoxin A (IpTxa), a scorpion toxin from the venom of Pandinus imperator. MCa shares the highly basic structural domain identified in peptide A - a segment of the dihydropyridine receptor and IpTxa which is important for interactions with ryanodine receptors. MCa also appears to share the same features as the so-called cell-penetrating peptides which allows the toxin to efficiently penetrate various cell types without expending metabolic energy or using an endocytotic mechanisM1-4In vitro, electrophysiological experiments based on recordings of single channels incorporated into planar lipid bilayers showed that MCa potently and reversibly modifies channel gating behavior of the ryanodine receptor 1 (RyR1) by inducing prominent subconductance behavior.1,2Similar to IpTxa, MCa-modified channels can reversibly shuttle between subconductance states and fast gating states. The actions of these peptides were also found to be additive with those of ryanodine, resulting in additional sub-states along with the ryanodine-locked half-conducting state. However, the predominant subconductance induced by MCa differs from that of IpTxa. At a holding potential of +40 mV, the predominant substates induced by sMCa and IpTxa are 48 and 28% of the full conductance, respectively, suggesting that the structural difference in these peptides may induce slightly different channel conformations that stabilize different unitary conductances.5
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
- Calcium imaging assay: 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.
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