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Specifications:
| Application | Cell culture, molecular biology | ||
| Storage Temperature | 2-8°C | ||
| Product Type | Enzymes and Substrates | Forms | Liquid |
| Product Brand | ROCHE | ||
| Product Grade | Cell Culture | ||
Papain from Carica papaya is a highly active cysteine protease enzyme widely used in biochemistry, cell biology, and molecular biology laboratories for protein digestion, tissue dissociation, and enzymatic hydrolysis studies. Papain is a single-chain proteolytic enzyme derived from papaya latex and belongs to the papain family of cysteine proteases.
With a molecular weight of approximately 23 kDa, papain exhibits strong proteolytic activity capable of cleaving amide bonds, peptides, proteins, and amino acid esters. The enzyme preferentially hydrolyzes peptide bonds involving residues such as lysine, arginine, and phenylalanine, making it useful in controlled protein digestion and biochemical research.
Papain is commonly used for tissue dissociation, protein digestion, immunoglobulin cleavage, and membrane protein solubilization. In neuroscience and cell culture research, it is frequently applied for dissociation of brain tissue and neural cells to prepare viable cell suspensions for downstream studies.
This preparation is supplied as a crystalline suspension derived from papaya, providing reliable enzymatic activity for laboratory applications.
Key Features
- Proteolytic enzyme derived from Carica papaya
- Member of the cysteine protease (EC 3.4.22.2) family
- High enzymatic activity (~30 U/mg protein)
- Effective for protein digestion and peptide hydrolysis
- Suitable for tissue dissociation and cell isolation workflows
- Useful in enzymatic cleavage of immunoglobulins
- Supports membrane protein solubilization and glycopeptide generation
Applications
- Enzymatic digestion of proteins and peptides
- Tissue dissociation for cell culture preparation
- Brain cell and neural tissue dissociation
- Immunoglobulin cleavage studies
- Membrane protein solubilization
- Proteoglycan analysis and glycopeptide production
- Biochemical and enzymology research
Technical Specifications
| Parameter | Specification |
|---|---|
| Enzyme Name | Papain |
| Biological Source | Carica papaya |
| Enzyme Classification | Cysteine protease |
| EC Number | 3.4.22.2 |
| Molecular Weight | ~23 kDa |
| Specific Activity | ~30 U/mg protein |
| Substrate | BAEE (benzoyl-L-arginine ethyl ester) |
| Optimal pH | 6.0–7.0 |
| Form | Suspension, crystalline |
| Concentration | 10–100 mg/mL |
| Working Concentration | 0.05–0.5 mg/mL |
| Packaging | 10 mL (100 mg) |
| Manufacturer | Roche |
Enzymatic Activity
Papain catalyzes several biochemical reactions including:
- Proteolytic hydrolysis of peptide bonds
- Transferase reactions involving protein substrates
- Cleavage of proteins and peptides at specific amino acid residues
- Generation of peptide fragments and glycopeptides
The enzyme’s activity requires the presence of reducing agents such as cysteine (~0.5% w/v) to maintain optimal catalytic performance.
Storage and Handling
- Store at 2–8°C
- Activity may decrease by approximately 20% after six months of storage
- Ship under wet ice conditions to maintain stability
Papain from Carica papaya is a versatile and widely used proteolytic enzyme suitable for numerous biochemical and cell biology applications. Its strong protease activity, reliability, and compatibility with tissue dissociation and protein digestion protocols make it an essential reagent for protein research, enzymology studies, and cell isolation workflows in modern laboratories.