Name: Heparinase II from Flavobacterium heparinum
Brand: Molecular Depot
SKU: B2016743
Price: 895.00 USD
Availability: InStock

<h2>What are research biochemical enzymes?</h2>
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Research biochemical enzymes in this category are purified, characterized enzyme preparations used as laboratory tools for specific biochemical transformations: proteases that cleave peptide bonds for protein processing, cell dissociation, or mass spectrometry sample preparation; nucleases that degrade DNA or RNA for sample cleanup or to remove contaminating nucleic acids; glycosidases and glycan-processing enzymes for structural glycan analysis; oxidoreductases for metabolic assays; and lytic enzymes like lysozyme for bacterial cell wall digestion. These differ from the specialized epigenetics enzymes (DNMTs, TETs, HDACs) in the Epigenetics category in being general biochemical tools rather than specific chromatin regulatory enzymes.
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<h2 dir="ltr">What you will find:</h2>
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Cell Lysis Enzymes: High-potency digestive proteins optimized for breaking down tough bacterial, fungal, or plant cell walls.
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Nucleic Acid Modifiers: Precision enzymes engineered for cutting, ligating, or modifying DNA and RNA strands in cloning workflows.
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Proteolytic Enzymes: High-grade proteases calibrated for targeted protein digestion and tissue cell separation protocols.
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Analytical Enzymes: Stable reporter and marker enzymes prepared for conjugation and signal amplification in diagnostic assays.
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<h2>How to choose research enzymes</h2>
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Choose trypsin for routine protein digestion and cell dissociation
Trypsin is a serine protease that cleaves peptide bonds specifically after lysine and arginine residues, making it the standard enzyme for mass spectrometry-compatible proteomics sample preparation, and it is also the standard enzyme for detaching adherent mammalian cells from culture vessels in TrypLE or trypsin-EDTA formats.
Choose proteinase K for broad-spectrum protein digestion in sample preparation
Proteinase K is a subtilisin-type serine protease with very broad substrate specificity, active across a wide pH and temperature range and resistant to SDS and other denaturants, making it the enzyme of choice for protein removal from DNA and RNA preparations, tissue digestion, and any application requiring complete protein digestion under denaturing conditions.
Use DNase I to remove contaminating DNA from RNA preparations
DNase I is the standard enzyme for removing contaminating genomic DNA from RNA preparations, particularly important before RT-PCR and other RNA-based applications where residual DNA could produce false signals. It is active on both double-stranded and single-stranded DNA and requires calcium and magnesium cofactors.
Use RNase A to remove contaminating RNA from DNA preparations or protein samples
RNase A degrades single-stranded RNA at high efficiency and is commonly used to remove RNA from DNA preparations, eliminate RNA background in protein crystallography samples, and as a control enzyme in RNase protection assays.
Choose lysozyme for bacterial cell wall digestion during lysis
Lysozyme cleaves beta-1,4-glycosidic bonds in the peptidoglycan layer of bacterial cell walls, particularly effective against gram-positive bacteria where the peptidoglycan layer is more accessible, and is commonly used as a first-step cell disruption agent in bacterial protein expression and purification workflows.
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<h2>Specifications context</h2>
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Proteinase K is notable for its resistance to denaturation by SDS, urea, and other denaturants that would inactivate most other proteases, and this stability makes it uniquely useful for protein removal from samples in the presence of these reagents, including direct application to tissue samples containing endogenous proteases that would degrade normal protease preparations. As of 2026, sequence-grade modified trypsin, optimized for mass spectrometry proteomics with minimal autolysis peptide background, remains the most widely used enzyme for proteomics sample preparation, while PNGase F continues to be the standard enzyme for N-linked glycan removal from glycoproteins.
<a href="https://mbpinc.net/contact-us">Contact the helpful team at MBP</a> today to request a quote for your specific research requirements.

Enzymes

Molecular Depot

Key Specifications

Heparinase II from Flavobacterium heparinum

Heparinase II from Flavobacterium heparinum by Molecular Depot is a heparinase II (heparin lyase II), an enzyme produced by the bacterium Flavobacterium heparinum. It degrades heparin, a glycosaminoglycan found in the body, by cleaving the glycosidic linkages in the chain. It is used to depolymerise heparin and heparan sulfate for disaccharide analysis, to remove heparin from samples and in glycosaminoglycan research. Each unit contains 10 U. MBP supplies Molecular Depot enzyme reagents to research labs in the United States, Canada and worldwide.