HRP Conjugated Lens culinaris Lectin (Lentil) – LcH
Horseradish peroxidase-conjugated lentil lectin for glycoprotein recognition, carbohydrate-binding studies and glycobiology research.
Product Information
| Product Name | HRP Conjugated Lens culinaris Lectin (Lentil) – LcH |
| Catalog Number | 0235-H-1401-2 |
| Lectin Source | Lens culinaris (Lentil) |
| Conjugate | Horseradish Peroxidase (HRP) |
| Size | 2 mg |
| Dry Ice | No |
| Hazardous | No |
Product Description
HRP Conjugated Lens culinaris Lectin (LcH), also known as lentil agglutinin, is a carbohydrate-binding protein derived from lentils. It is conjugated to horseradish peroxidase (HRP), an enzyme commonly used as a reporter molecule in biochemical detection systems.
Lens culinaris lectin is a member of the plant lectin family and is widely studied for its ability to recognize specific carbohydrate structures on glycoproteins and other glycoconjugates. Its carbohydrate-binding properties make it useful for investigating glycosylation patterns and molecular interactions involving cell-surface and secreted glycoproteins.
The HRP conjugate combines lectin-mediated carbohydrate recognition with the enzymatic signal-generating properties of horseradish peroxidase. In suitable detection systems, HRP catalyzes substrate oxidation to produce a measurable colorimetric or chemiluminescent signal.
Note: Product volume may vary. Please consult the product documentation for specific handling and application recommendations.
Key Features & Benefits
Carbohydrate Recognition
Recognizes specific carbohydrate structures associated with glycoproteins and other glycoconjugates.
HRP Conjugation
Incorporates an enzymatic reporter for signal generation in appropriate detection systems.
Glycoprotein Analysis
Useful for investigating glycosylation characteristics and carbohydrate-associated molecular interactions.
Research Applications
Supports laboratory studies in glycobiology, biochemistry and molecular recognition.
Scientific Background
Lectins are proteins that bind carbohydrates through specific non-covalent interactions. They are important research tools for studying the structural and functional properties of glycans present on proteins, lipids and cell surfaces.
Lens culinaris agglutinin (LCA) is particularly recognized for its affinity toward certain mannose-containing glycan structures, including core-fucosylated N-linked glycans under appropriate assay conditions. These interactions have made lentil lectin valuable in glycoprotein characterization and glycosylation research.
HRP conjugation enables enzymatic detection following lectin binding. The resulting signal depends on the detection substrate, assay conditions and accessibility of the target carbohydrate structures.
Research Applications
- Glycoprotein Detection: Investigation of carbohydrate-containing proteins in biological samples.
- Glycosylation Analysis: Evaluation of glycan structures and glycosylation patterns.
- Lectin-Based Detection: Carbohydrate recognition in HRP-based detection workflows.
- Glycobiology Research: Investigation of lectin-carbohydrate interactions.
- Cell Biology: Research into carbohydrate structures associated with cellular components.
- Biochemical Studies: Characterization of glycoproteins and glycoconjugates.
Technical Specifications
| Lectin Name | Lens culinaris Lectin (LcH) |
| Common Name | Lentil Agglutinin |
| Biological Source | Lentil (Lens culinaris) |
| Conjugated Enzyme | Horseradish Peroxidase (HRP) |
| Product Format | HRP-conjugated lectin |
| Supplied Quantity | 2 mg |
| Catalog Number | 0235-H-1401-2 |
Storage & Handling
- Follow the storage temperature and handling instructions provided in the product documentation.
- Use appropriate laboratory protective equipment when handling biochemical reagents.
- Follow validated assay procedures and recommended HRP detection conditions.
- Product volume may vary.
Product Tags
Lectin LcH Lentil Agglutinin HRP Conjugated Glycoprotein Research H-1401-2Explore Lectins & Glycobiology Research Reagents
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