Subtilisin A from Bacillus licheniformis – Research Use Only

Subtilisin A from Bacillus licheniformis is a highly purified serine protease (subtilisin Carlsberg) supplied as a 100 mg lyophilized powder with a molecular weight of approximately 27,500–30,250 Da. This biotechnology-grade enzyme is widely used as a model protease in protein chemistry, as a reagent for peptide mapping, and in various industrial and research applications requiring broad-spectrum proteolytic activity under alkaline conditions.

Scientific Overview

Subtilisin A (also known as subtilisin Carlsberg) is an alkaline serine protease produced by Bacillus licheniformis. It exhibits broad substrate specificity and high stability under alkaline conditions, making it a classic model enzyme for studying catalysis, protein engineering, and industrial applications. Subtilisin A is frequently used in biochemical research for limited proteolysis, peptide mapping, removal of protein tags, and as a reference protease in kinetic and stability studies.

This Subtilisin A from Bacillus licheniformis is suitable for:

• General protein digestion and limited proteolysis experiments
• Peptide mapping and mass spectrometry sample preparation
• Enzyme kinetics and stability studies
• Removal of affinity tags from recombinant proteins
• Research on serine protease mechanisms and protein engineering

Usage & Handling Guidance

Store the lyophilized powder at −20 °C. Reconstitute in ultrapure water or appropriate buffer (e.g., 50 mM Tris-HCl, pH 8.0) immediately before use. Prepare fresh working solutions or single-use aliquots to maintain maximum activity. The enzyme is most active in the alkaline pH range (pH 7.5–10.0).

• Recommended applications: Protein digestion, peptide mapping, tag removal, and kinetic assays
• Working concentration: Typically 0.1–10 µg/mL or 1–100 U/mL depending on the substrate and desired digestion extent (optimize empirically)
• Stability: Highly stable in alkaline conditions; activity is calcium-dependent in some formulations
• Handling: Avoid strong oxidants and heavy metals that may inhibit serine protease activity

What You Get

• 100 mg Subtilisin A from Bacillus licheniformis as a high-purity lyophilized powder
• Molecular weight approximately 30,250 Da
• Biotechnology-grade protease suitable for precise biochemical applications
• Batch-specific documentation available upon request
• For research use only (RUO)

Why Researchers Choose It

• High-purity subtilisin A with well-characterized proteolytic activity
• Excellent model enzyme for studying serine protease mechanisms and stability
• Useful for limited proteolysis, tag removal, and peptide mapping workflows
• Stable powder format for convenient long-term storage and reconstitution
• Manufactured under strict biotechnology-grade quality controls

Frequently Asked Questions (FAQ)

• What is the optimal pH range for Subtilisin A?
  Subtilisin A is most active in the alkaline range, typically pH 7.5–10.0.
• How should I reconstitute the enzyme?
  Reconstitute in ultrapure water or 50 mM Tris-HCl buffer (pH 8.0). Prepare fresh solutions or aliquots for best activity.
• What is the typical working concentration?
  Use 0.1–10 µg/mL or 1–100 U/mL depending on the substrate and desired degree of digestion. Optimize for your specific application.
• Is calcium required for activity?
  Subtilisin A is generally calcium-independent, but low concentrations of Ca²⁺ can enhance stability in some conditions.
• Can this enzyme be used for removing affinity tags?
  Yes. It is commonly used for limited proteolysis and removal of fusion tags from recombinant proteins.

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