- Home
- IVD
- By Technology Types
- By Diseases Types
- By Product Types
- Research
- Resource
- Distributors
- Company
| Product Name | Urea, 8 M Solution, Deionized, for Protein Solubilization |
| Catalog No. | ATR-SDS-0028 |
| Description | Ready-to-use 8 M urea solution in deionized water for solubilization and denaturation of proteins from inclusion bodies, membrane preparations, and aggregated protein samples. Urea is a chaotropic agent that disrupts hydrogen bonding networks stabilizing protein secondary and tertiary structure, converting compact folded proteins into extended random coil conformations. Deionization treatment removes cyanate ions (which can carbamylate primary amines on proteins, causing charge heterogeneity artifacts in 2D electrophoresis and mass spectrometry) and heavy metal contaminants. Pre-formulated 8 M solution eliminates the time-consuming dissolution process and the exothermic heat generation of preparing solid urea solutions. |
| Intended Use | Solubilization of inclusion body proteins from E. coli; denaturation of proteins for SDS-PAGE sample preparation; dissolution of protein aggregates; protein unfolding for proteolytic digestion; membrane protein solubilization; 2D electrophoresis sample preparation. |
| Principle / Technology | Urea disrupts hydrogen bonds and hydrophobic interactions maintaining protein structure; at 8 M, most proteins are fully denatured; deionization removes cyanate (OCN-) that can carbamylate Lys and N-termini; thiophilic agents and reductants can be added for disulfide reduction. |
| Detection Method | Resuspend protein pellet or inclusion bodies in 8 M urea solution; vortex or homogenize; incubate at room temperature 30-60 minutes; add reducing agent (DTT or TCEP) if disulfide bond reduction required; dilute to ≤2 M urea for downstream enzymatic digestion or refolding. |
| Sample Type | E. coli inclusion bodies; insoluble protein aggregates; membrane protein pellets; lyophilized protein powders; tissue samples requiring complete protein extraction. |
| Performance Range / Specifications | Solubilization of ≥95% of inclusion body protein within 30 minutes at room temperature; effective protein denaturation at 6-8 M urea; urea concentrations >2 M inhibit most proteases. |
| Sensitivity / LOD | Cyanate concentration <0.1 mM in 8 M solution (freshly deionized); heavy metals (Fe, Cu, Ni) <0.1 ppm. |
| Specificity | Chaotropic denaturation is non-specific; all proteins containing hydrogen bonds and hydrophobic interactions are affected; does not break covalent bonds including disulfide bonds. |
| Reaction Conditions / Protocol | Dissolution of inclusion bodies: 5-10 volumes of 8 M urea per pellet weight; homogenize; incubate 30-60 min at RT; centrifuge at 20,000 × g for 20 min to remove insoluble debris. |
| Components / Formulation | Urea 8 M in deionized water (≥18.2 MΩ·cm); deionized with mixed bed ion-exchange resin immediately before packaging; 0.22 µm filtered. |
| Storage Conditions | Store at room temperature (15-25 °C); protect from prolonged heating (>40 °C) which accelerates cyanate formation; do not freeze (urea crystallizes out of solution below ~5 °C). |
| Shelf Life | 12 months from date of manufacture in unopened container. |
| Package Specifications | 100 mL, 500 mL, 1 L HDPE bottles. |
| Product Form | Clear, colorless liquid; may become slightly yellow over time due to trace cyanate and ammonia formation. |
| Quality Control | Each lot tested for urea concentration (refractive index: 8.0 ± 0.2 M), conductivity (<50 µS/cm), cyanate content, pH, and absorbance at 280 nm. |
| Key Features | Ready-to-use 8 M solution; deionized to remove cyanate; 0.22 µm filtered; eliminates weighing and dissolving solid urea; consistent concentration lot-to-lot; reduced protein carbamylation artifacts. |
| Purity | Urea ≥99.5% purity; cyanate <0.1 mM; heavy metals <0.1 ppm; DNase/RNase not detected. |
| Concentration | 8.0 ± 0.2 M (approximately 48% w/v). |
| Activity / Unit Definition | Denaturant m-value: ~1.0-1.5 kcal/mol/M for typical globular proteins (free energy of unfolding per molar urea). |
| Molecular Weight | 60.06 g/mol (CH4N2O). |
| Source / Origin | Synthetic urea from ammonia and carbon dioxide; deionized by mixed-bed resin treatment. |
| pH Range / Optimal pH | Native pH 7.0-9.0 in solution; deionization removes acidic and basic contaminants. |
| Shipping Conditions | Ambient temperature; protect from extreme cold (crystallization below 5 °C). |
| Expiration Date / Stability | 12 months at room temperature; cyanate levels gradually increase — retest before use after 6 months. Discard if solution becomes strongly yellow or develops ammonia odor. |
| Regulatory / Compliance | For research use only; not for therapeutic or diagnostic use. |
| Compatibility | Compatible with Tris, phosphate, and HEPES buffers. Incompatible with SDS-PAGE loading buffer containing bromophenol blue — urea plus heat >70 °C causes protein carbamylation. Add DTT or TCEP ≤50 mM for disulfide reduction (urea does not reduce disulfides). For mass spectrometry, dilute urea to <1 M before trypsin digestion. |
| Recommended Buffer System | Not buffered; urea is uncharged at neutral pH. Can be prepared in any desired buffer by substituting buffer for water in formulation (custom available). |
| Application Notes / Precautions | Work at room temperature to prevent urea crystallization. Do not heat urea solutions >40 °C as this accelerates cyanate formation. For SDS-PAGE, add urea to loading buffer but do NOT boil samples in urea — heat to 37-50 °C maximum. For 2D electrophoresis, supplement with thiourea (2 M) and CHAPS (2-4%) for improved solubilization. For refolding, rapidly dilute or dialyze away from urea. Freshly deionized urea should be colorless and odorless. |
| Batch-to-Batch Consistency | Urea concentration 8.0 ± 0.2 M; conductivity <50 µS/cm; cyanate <0.1 mM; A280 <0.05 AU. |
For research use only, not for clinical use.
|
There is no product in your cart. |
Copyright © 2026 Alta DiagnoTech. All rights reserved.
