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Lectin from Triticum vulgaris

lyophilized, ≥55% (GE), powder

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Synonym(s):
WGA, Wheat germ agglutinin
MDL number:
NACRES:
NA.56

biological source

Triticum vulgaris

form

powder

quality

lyophilized

concentration

≥55% (GE)

technique(s)

agglutination assay: suitable using fresh human erythrocytes

storage temp.

2-8°C

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This Item
L1882L3892L4144
form

powder

form

saline suspension

form

lyophilized powder

form

lyophilized powder

concentration

≥55% (GE)

concentration

-

concentration

-

concentration

-

technique(s)

agglutination assay: suitable using fresh human erythrocytes

technique(s)

-

technique(s)

-

technique(s)

cell culture | mammalian: suitable

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

quality

lyophilized

quality

-

quality

-

quality

-

General description

Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in β-strands and posses a carbohydrate binding sites on the surface.
WGA is not blood group specific but has an affinity for N-acetyl-β-D-glucosaminyl residues and N-acetyl-β-D-glucosamine oligomers. WGA contains no protein-bound carbohydrate.

Application

Lectin from Triticum vulgaris has been used in bone resorption assays.
Wheat germ agglutinin conjugated to the outside surface of PLGA nanoparticles loaded with paclitaxel was used to target cancer cells that overexpress WGA-binding glycoproteins (Caco-2 and HT-29 cell lines). WGA-NP showed 50-60% greater endocytosis and intracellular retention of paclitaxel than unlabeled nanoparticles.

Biochem/physiol Actions

Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling. This is because of its specific interaction with oligosaccharides, glycoproteins and glycolipids. In plants and fungi, lectin defends against pathogens/feeders. Lectin participates in host recognition and tissue adhesion, thereby aids in the pathogenesis of microorganism.

Other Notes

Molecular characteristics and specificity for sugar binding

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding.
Y Nagata et al.
The Journal of biological chemistry, 249(10), 3116-3122 (1974-05-25)
Alternative NF-kB Regulates RANKL-Induced Osteoclast Differentiation and Mitochondrial Biogenesis via Independent Mechanisms
Zeng R, et al.
Journal of Bone and Mineral Research, 30(12), 2287-2299 (2015)
Chunxia Wang et al.
International journal of pharmaceutics, 400(1-2), 201-210 (2010-09-02)
The purpose of this study was to investigate the potentiation of the anticancer activity and enhanced cellular retention of paclitaxel-loaded PLGA nanoparticles after surface conjugation with wheat germ agglutinin (WGA) against colon cancer cells. Glycosylation patterns of representative colon cancer
Yinglong Zhao et al.
Frontiers in cell and developmental biology, 9, 796902-796902 (2022-02-22)
Microgravity prominently affected cardiovascular health, which was the gravity-dependent physical factor. Deep space exploration had been increasing in frequency, but heart function was susceptible to conspicuous damage and cardiac mass declined in weightlessness. Understanding of the etiology of cardiac atrophy
Rong Zeng et al.
Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 30(12), 2287-2299 (2015-06-23)
Mitochondrial biogenesis, the generation of new mitochondrial DNA and proteins, has been linked to osteoclast (OC) differentiation and function. In this study we used mice with mutations in key alternative NF-κB pathway proteins, RelB and NF-κB-inducing kinase (NIK), to dissect

Articles

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