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Key Documents

L8258

Sigma-Aldrich

Lectin from Wisteria floribunda

lyophilized powder

Sinônimo(s):

Wisteria floribunda agglutinin, WFA

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About This Item

Número MDL:
MFCD00166187
Código UNSPSC:
12352202
NACRES:
NA.32

forma

lyophilized powder

potência

<16 μg/mL agglutination activity

composição

Protein, ~95% E1%/280

temperatura de armazenamento

−20°C

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Descrição geral

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.

Aplicação

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

Ações bioquímicas/fisiológicas

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.

Embalagem

Package size based on protein content

Nota de análise

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.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificados de análise (COA)

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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
Markus Morawski et al.
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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