Triticum vulgare, Succinylated (WGA, Wheat Germ, Agglutinin) (Agarose)
Catalog No : USB-T8653-45A
489.67€
0.00€
Shipping cost plus VAT not included , delivery in 7-14 business days
| Product name | Triticum vulgare, Succinylated (WGA, Wheat Germ, Agglutinin) (Agarose) | ||
|---|---|---|---|
| Catalog No | USB-T8653-45A | ||
| Supplier’s Catalog No | T8653-45A | ||
| Supplier | US Biologicals | ||
| Source antigen | |||
| Reactivity | |||
| Cross reactivity | |||
| Applications | |||
| Molecular weight | |||
| Storage | 4°C Do Not Freeze | ||
|---|---|---|---|
| Other names | |||
| Grade | Molecular Biology Grade | ||
| Purity | |||
| Form | Supplied as a liquid in 10mM HEPES, pH 7.5, 0.15M sodium chloride, 20mM GlcNAc, 0.08% sodium azide. Labeled with Agarose. | ||
| Reactivity life | 12 months | ||
| Note | For reserch purpose only | ||
| Purity | |||
| Description | This derivative has been reported to have properties distinct from the native lectin. Evidence suggests that succinylated wheat germ agglutinin does not bind to sialic acid residues, unlike the native form, but retains its specificity toward N-acetylglucosamine (Eur. J. Biochem. 98, 39, 1979 and Eur. J. Biochem. 104, 147, 1980). Using conjugates of the native lectin and the succinylated form can provide a system to distinguish between sialylated glycoconjugates and those containing only N-acetylglucosamine structures. Agarose bound, succinylated Wheat Germ Agglutinin is prepared from affinity-purified lectin. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10e7 are used as the solid-phase matrix to which the lectin is covalently bound. The attachment of the lectin to the solid phase is carefully controlled in order to preserve the activity of the lectin as well as to minimize conformational changes of the bound lectin which might result in nonspecific ionic or hydrophobic interactions. The technique developed to couple lectins to agarose provides a very hydrophilic spacer arm between the protein and the matrix. This ensures maximum expression of the carbohydrate binding activity of the lectin. The linkage is very stable over a range of pH values and, unlike cyanogen bromide linkages, proteins are not leached off the gel by Tris or other routinely used buffers. In addition, residual charges generated during cyanogen bromide conjugation which can produce nonspecific binding are not present on the gel following our coupling procedure. Binding Capacity: ≥4mg of N-acetylglucosaminyl glycoprotein/ml gel Inhibiting/Eluting Sugar: Chitin Hydrolysate or 500mM N-acetylglucosamine with salt and/or acid elution generally required 3mg lectin/ml gel Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. 500mM N-Acetyl-D-Glucosamine can be used to elute glycoconjugates which bind to this immobilized lectin. For those glycoconjugates having very high affinity for WGA, it may be necessary to lower the pH of the eluting sugar solution to pH 3.0 with acetic acid and increase the concentration of the GlcNAc. Storage and Stability: May be stored at 4°C. For long-term storage, aliquot and store at 4°C. Do not freeze. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer. | ||
Product Details
© 2020 Imugex All Rights Reserved