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| Product Name | Elastase (Lyophilized) |
| Catalog No. | IVDRM-0285 |
| Description | Elastase is a serine protease that can also hydrolyze amides and esters. Because elastin is most concentrated in the elastic fibers of connective tissue, elastase is commonly used to dissociate tissues containing extensive intercellular fiber networks. The viscous extracellular matrix in which connective tissue cells and fibers are embedded is a complex mixture of various glycoproteins. Given the complexity of this matrix, proteolytic digestion works best when elastase is used in combination with other enzymes such as collagenase, trypsin, and chymotrypsin. This product is derived from porcine pancreas. Porcine pancreatic elastase consists of a single peptide chain of 240 residues containing four disulfide bonds, with a molecular weight of approximately 25.9 kDa and an optimal pH of about 8.5. It shares high sequence homology with pancreatic elastases from other species, such as 86% homology with rat. The elastase I and elastase II genes are similar in sequence, particularly in the 5' proximal flanking region, including a TATA box and a putative tissue-specific enhancer sequence. Porcine elastase I is specific for Ala-Ala and Ala-Gly bonds, whereas elastase II has broad specificity for substrates with medium to large hydrophobic amino acids at the P1 position. Porcine elastase is the most potent elastase, with a rate 20 times higher than that of human leukocyte elastase. Among proteases, porcine pancreatic elastase is unique in its ability to hydrolyze native elastin, a substrate that is not attacked by trypsin, chymotrypsin, or pepsin. Soybean trypsin inhibitor and kallikrein inhibitor suppress proteolytic activity but do not inhibit elastin hydrolysis by elastase. This product is supplied as a lyophilized powder and is widely used in tissue and cell dissociation procedures, with particularly notable performance in type II lung cell isolation. |
| Intended Use | For tissue dissociation, membrane protein solubilization, and protein sequence studies. Commonly used to dissociate tissues containing extensive intercellular fiber networks, and especially suitable for type II lung cell isolation. |
| Principle / Technology | Serine protease that hydrolyzes native elastin as well as amides and esters. Porcine elastase I is specific for Ala-Ala and Ala-Gly bonds, while elastase II has broad specificity for substrates with medium to large hydrophobic amino acids at the P1 position. |
| Sample Type | Tissues containing extensive intercellular fiber networks (e.g., lung tissue for type II pneumocyte isolation); also applicable to membrane protein solubilization and protein samples for sequence studies. |
| Performance Range / Specifications | Appearance: lyophilized powder. Molecular weight: approximately 25.9 kDa. Enzyme activity: >=3 U/mg protein. Optimal pH: 8.0-8.5. Isoelectric point: 9.5. Inhibitors: DFP, alkyl isocyanates, PMSF, alpha1-antitrypsin, alpha2-macroglobulin, dipeptide derivatives of alanine, valine, leucine, and isoleucine, sulfate-modified lipids, etc. Source: porcine pancreas. |
| Specificity | Uniquely able to hydrolyze native elastin, a substrate not attacked by trypsin, chymotrypsin, or pepsin. Soybean trypsin inhibitor and kallikrein inhibitor suppress proteolytic activity but do not inhibit elastin hydrolysis by elastase. Porcine elastase I is specific for Ala-Ala and Ala-Gly bonds; elastase II has broad specificity for substrates with medium to large hydrophobic amino acids at the P1 position. |
| Reaction Conditions / Protocol | The following instructions are for reference only; please adjust according to relevant literature and actual experimental conditions. 1. Preparation of elastase stock solution: 1.1 Elastase can be dissolved in common balanced salt solutions, such as 0.05 M Tris-HCl buffer (pH 8.0-8.5). This pH range is the optimal environment for the enzyme, maintaining enzyme activity and avoiding inactivation at pH <=3.5. Adjust the concentration according to the specific application. Note: the product has poor solubility at concentrations above 0.25% in neutral pH environments and tends to form insoluble material. If a high-concentration buffer system is required, it is recommended to first prepare the solution in an alkaline buffer and then dilute it into the neutral pH buffer system. 1.2 After preparation, sterilize by filtration through a 0.22 um filter membrane, and aliquot into small volumes as needed to avoid repeated freeze-thaw cycles. The filtered stock solution can be stored at 2-8 °C for about 1-2 weeks. For long-term storage, aliquot and store at -25 to -15 °C or -85 to -65 °C; adjust the buffer pH to around 8.5 before freezing to stabilize enzyme activity. 2. Animal models (e.g., COPD mouse model): a working dose of 6 units per mouse can be considered, administered by nebulization for 15-20 min each time, once a week for 4 months, followed by anesthesia with 0.3% sodium pentobarbital (50 mg/kg, intraperitoneal injection) and pulmonary function testing via tracheal intubation connected to a pulmonary function instrument. |
| Components / Formulation | Lyophilized powder. |
| Storage Conditions | Powder: store at 2-8 °C protected from light. Stock solution: store frozen at -25 to -15 °C protected from light. |
| Shelf Life | Powder: 1 year when stored at 2-8 °C protected from light. |
| Package Specifications | 5 mg / 10 mg / 100 mg / 1 g |
| Product Form | Lyophilized powder |
| Activity / Unit Definition | Activity: >=3 U/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1 umol of N-succinyl-L-alanyl-L-alanyl-L-alanine-p-nitroanilide per minute at 25 °C, pH 8.0. |
| Molecular Weight | Approximately 25.9 kDa |
| Source / Origin | Porcine pancreas |
| pH Range / Optimal pH | Optimal pH 8.0-8.5. Relatively stable between pH 4.0 and 10.4; unstable below pH 3-4. |
| Expiration Date / Stability | Filtered stock solutions can be stored at 2-8 °C for about 1-2 weeks. For long-term storage, aliquot and store at -25 to -15 °C or -85 to -65 °C, and adjust the buffer pH to around 8.5 before freezing to stabilize enzyme activity. Elastase is unstable when the pH is below 3-4. |
| Regulatory / Compliance | For research use only. |
| Compatibility | For tissue dissociation, proteolytic digestion works best when elastase is used in combination with other enzymes such as collagenase, trypsin, and chymotrypsin. |
| Recommended Buffer System | Dissolve in common balanced salt solutions such as 0.05 M Tris-HCl buffer (pH 8.0-8.5). For high-concentration stock solutions, it is recommended to first dissolve in KCl or an alkaline buffer (e.g., pH 9-10) and, after complete dissolution, dilute with a neutral buffer to the working concentration or add directly to the reaction mixture or culture medium to compensate for changes in ionic strength or pH. |
| Application Notes / Precautions | 1. Elastase is unstable at pH below 3-4. The lyophilized powder has low solubility at neutral pH (e.g., pH 7-8) and concentrations above 0.25% (w/v), and tends to form flocculent or insoluble material. If the solution becomes turbid, insufficient solubility may be the cause; re-prepare the solution or dissolve in a higher-pH buffer. 2. For high-concentration stock solutions, first dissolve in KCl or an alkaline buffer (e.g., pH 9-10), then dilute to the working concentration with a neutral buffer, or add to the reaction mixture or culture medium to compensate for ionic strength or pH changes. The enzyme is relatively stable between pH 4.0 and 10.4. 3. For your safety and health, wear a lab coat and disposable gloves during operation. 4. This product is for research use only. |
For research use only, not for clinical use.
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