Allium sativum Lectin (ASA) - DyLight 488

Price: Regular price $396.25

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Product Description

Allium sativum lectin (ASA) is isolated from garlic and purified with affinity chromatography. It is a dimer of two subunits. ASA binds to several α1-2-linked mannose residues. The lectin recognizes internal mannose and binds to the core pentasaccharide of N-linked glycans. In addition, the removal of sialic acids enhances binding activity.  ASA has shown antiproliferative and apoptosis-inducing activity, making it a relative subject in cancer research

Dylight 488 can be used to visualize the binding pattern of Allium sativum Lectin (ASA) in cellular imaging and flow cytometry. DyLight 488 is a green-fluorescent dye that works over a broad pH range (pH 4-9). It is brighter and more photostable than many other green-fluorescent dyes, including FITC.

Recommended Usage: 1XPBS can be used for reconstitution/dilution. Recommended dilution is 0.5 - 10 µg /ml in 1XPBS.

Technical Specifications

Abbreviation: ASA
Material Source:: Garlic Bulb
Conjugate:: DyLight 488
Concentration:: 1 mg/ml
Molecular Weight:: 25, 48 kDa
Appearance Form:: Liquid
Appearance Color:: Green
Purity:: High Grade Purity
Shelf Life:: 1 year
Blood Group Specificity:: Rabbit Erythrocytes
Preferred Sugar Specificity:: D-Mannose
Inhibiting or Eluting Sugar:: (Man)2(GlcNAc)2
Fluorescence:: Green
Divalent Ions:: None
Excitation:: 493
Emission:: 518
Lyophilized or Liquid: Liquid
Storage Temperature:: -20°C
Hazardous Shipping:: Non-hazardous

Applications

Immunofluorescence, Immunocytochemistry, Immunohistochemistry, Blotting, ELISA, ELLA, Bioconjugation, Cell typing, Glycobiology.

References

1. Ghosh, P., Sen, S., Chakraborty, J., & Das, S. (2016). Monitoring the efficacy of utated Allium sativum leaf lectin in transgenic rice against Rhizoctonia solani. BMC biotechnology, 16, 24. https://doi.org/10.1186/s12896-016-0246-0.

 2. Kumar, S., Jitendra, K., Singh, K., Kapoor, V., Sinha, M., Xess, I., Das, S. N., Sharma, S., Singh, T. P., & Dey, S. (2015). Biological Properties and Characterization of ASL50 Protein from Aged Allium sativum Bulbs. Applied biochemistry and biotechnology, 176(7), 1914–1927.

Technical Documentation

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