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| Product Name | Proteinase K (Recombinant, Molecular Biology Grade) |
| Catalog No. | IEC-HMM-0055 |
| Description | A recombinant serine protease with broad substrate specificity, produced as the recombinant form of the Tritirachium album enzyme. This protease cleaves peptide bonds adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha-amino groups. It maintains activity in the presence of detergents, chelating agents, and denaturants, making it the enzyme of choice for protein removal from nucleic acid preparations. |
| Intended Use | For digestion and removal of proteins from nucleic acid samples during DNA and RNA purification; inactivation of nucleases; tissue digestion for genomic DNA extraction; prion protein research; and decontamination of laboratory surfaces and equipment. |
| Principle / Technology | Serine protease catalytic mechanism involving the catalytic triad (Ser-His-Asp). The enzyme binds substrate through extended subsite interactions and cleaves peptide bonds preferentially at the carboxyl side of hydrophobic amino acids. Requires no specific cofactors and tolerates SDS, urea, EDTA, and moderate concentrations of guanidine salts. |
| Detection Method | Activity measured by release of Folin-positive amino acids from denatured hemoglobin substrate at 37 °C, pH 7.5. One Anson unit releases the equivalent of 1 umol tyrosine per minute. |
| Sample Type | Tissues, cells, bacteria, yeast, blood, forensic samples, paraffin-embedded specimens — any biological material requiring protein digestion for nucleic acid purification. |
| Performance Range / Specifications | Active over 20-65 °C (optimum 50-65 °C), pH 4.0-12.5 (optimum pH 7.5-8.0). Maintains >80% activity in 0.5% SDS and 4 M urea. |
| Sensitivity / LOD | Effective at concentrations as low as 0.05 mg/mL for most applications; typical working concentration 0.1-0.5 mg/mL. |
| Specificity | Broad specificity for peptide bonds adjacent to hydrophobic and aromatic amino acid residues. Does not require a specific recognition sequence. |
| Reaction Conditions / Protocol | For DNA extraction: add to final 0.1-0.2 mg/mL in lysis buffer with 0.5% SDS. Incubate at 56 °C 30-60 min. For tissue digestion: 0.5 mg/mL, 56 °C 1-4 h or overnight. |
| Components / Formulation | Recombinant Proteinase K, lyophilized or in solution (20 mg/mL) in 50 mM Tris-HCl (pH 8.0), 5 mM CaCl₂, 50% glycerol. Supplied with or without storage buffer depending on format. |
| Storage Conditions | Lyophilized: store at -20 °C, stable. Solution: store at -20 °C, protect from repeated freeze-thaw. |
| Shelf Life | 36 months (lyophilized) or 24 months (solution) at -20 °C. |
| Package Specifications | 100 mg, 1 g, 5 g, 25 g (lyophilized); 1 mL, 5 mL, 25 mL (20 mg/mL solution). Custom packaging available. |
| Product Form | Lyophilized white powder or clear liquid (20 mg/mL in glycerol buffer). |
| Quality Control | Each lot tested for: protease specific activity; absence of contaminating DNase and RNase after 16-hour incubation with DNA/RNA substrates; sterility (solution format); endotoxin levels (for sensitive applications). |
| Key Features | Broad substrate specificity; active in presence of denaturants (SDS, urea) and chelators (EDTA); recombinant source ensures consistent quality; essential reagent for nucleic acid purification workflows worldwide. |
| Purity | >= 95% by SDS-PAGE. No detectable nuclease contamination after extended incubation with nucleic acid substrates and sensitive detection methods. |
| Concentration | 20 mg/mL (solution); lyophilized powder for reconstitution at desired concentration. |
| Activity / Unit Definition | >= 30 Anson units per gram (lyophilized). Solution: >= 600 U/mL at 20 mg/mL. |
| Molecular Weight | ~28.9 kDa (mature processed enzyme). |
| Source / Origin | Recombinant enzyme expressed in Pichia pastoris. Gene sequence derived from Tritirachium album limber (Engyodontium album) with codon optimization for yeast expression. |
| pH Range / Optimal pH | Active range: pH 4.0-12.5. Optimal: pH 7.5-8.0. Calcium ions (1-5 mM) enhance thermostability but are not essential for catalytic activity. |
| Shipping Conditions | Lyophilized: ship at ambient temperature. Solution: ship with cold packs to maintain below 10 °C. |
| Expiration Date / Stability | Lyophilized: >36 months at -20 °C. Working solution (1-10 mg/mL in water or Tris buffer): 2-4 weeks at 4 °C or aliquot and freeze at -20 °C. |
| Regulatory / Compliance | ISO 9001 and ISO 13485 certified manufacturing. Recombinant source preferred for IVD kit development. Certificate of Analysis and regulatory support documents available. |
| Compatibility | Compatible with all common nucleic acid extraction buffers including those containing SDS (≤2%), Triton X-100, Tween-20, guanidine hydrochloride (≤1 M), urea (≤4 M), EDTA (≤50 mM), and DTT (≤10 mM). |
| Recommended Buffer System | Storage buffer: 50 mM Tris-HCl (pH 8.0), 5 mM CaCl₂, 50% glycerol (for solution format). For working dilutions: 10-50 mM Tris-HCl (pH 7.5-8.0) with 1-5 mM CaCl₂. |
| Application Notes / Precautions | For RNA work, prepare working aliquots and store single-use to prevent RNase introduction. Pre-incubate at 56 °C for maximum activity. Extend digestion time for fibrous tissues. For complete inactivation: heat at 95 °C 10 min or add PMSF/AEBSF. |
| Batch-to-Batch Consistency | Specific activity consistent within +/- 10% between production lots. Nuclease-free certification verified for each batch. |
For research use only, not for clinical use.
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