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About This Item
Form:
lyophilized powder
form
lyophilized powder
Quality Level
potency
<16 μg/mL agglutination activity
composition
Protein, ~95% E1%/280
storage temp.
−20°C
General description
Lectin is a carbohydrate-binding protein found in plant roots, rhizomes, leaves, seeds, and stems. Lectin is located in the cytoplasm as well as in the nucleus.
Application
Lectin from Wisteria floribunda has been used:
- to study the perineuronal nets and parvalbumin nets in mouse brain by immunofluorescence
- to evaluate the amount of N-acetylgalactosamine (GalNAc) transferred to Gaussia luciferase (GLuc) substrates by microplate assay
- to study its binding effects on perineuronal nets
Biochem/physiol Actions
Lectin binds with high affinity to the glycans of polysaccharides, glycolipids, and glycoproteins. It is involved in plant defense.
WFA is not blood group specific, but has an affinity for N-acetyl-D-galactosamine.
Packaging
Package size based on protein content
Analysis Note
Agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, of a 1 mg/ml solution. This activity is the lowest concentration to agglutinate a 2% suspension of human blood group A erythrocytes after 1 hr incubation at 25 °C.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Nausicaä Lannoo et al.
Frontiers in plant science, 5, 397-397 (2014-08-29)
Plants are under constant attack from pathogens and herbivorous insects. To protect and defend themselves, plants evolved a multi-layered surveillance system, known as the innate immune system. Plants sense their encounters upon perception of conserved microbial structures and damage-associated patterns
Lectins, lectin genes, and their role in plant defense.
M J Chrispeels et al.
The Plant cell, 3(1), 1-9 (1991-01-01)
Dorothy Fiete et al.
The Journal of biological chemistry, 287(34), 29194-29203 (2012-06-23)
Two closely related β1,4-N-acetylgalactosaminyltransferases, β4GalNAc-T3 and β4GalNAc-T4, are thought to account for the protein-specific addition of β1,4-linked GalNAc to Asn-linked oligosaccharides on a number of glycoproteins including the glycoprotein hormone luteinizing hormone and carbonic anhydrase-6 (CA6). We have utilized soluble