L8258
Lectin from Wisteria floribunda
lyophilized powder
Sinonimo/i:
Wisteria floribunda agglutinin, WFA
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About This Item
Prodotti consigliati
Stato
lyophilized powder
Livello qualitativo
Potenza
<16 μg/mL agglutination activity
Composizione
Protein, ~95% E1%/280
Temperatura di conservazione
−20°C
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Descrizione generale
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.
Applicazioni
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
Azioni biochim/fisiol
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.
Confezionamento
Package size based on protein content
Risultati analitici
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.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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
Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 369(1654), 20140046-20140046 (2014-09-17)
Perineuronal nets (PNs) in the brains of tenascin-R-deficient (tn-r(-/-)) mice develop in temporal concordance with those of wild-type (tn-r(+/+)) mice. However, the histological appearance of PNs is abnormal in adult tn-r(-/-) mice. Here, we investigated whether similar defects are also
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