Size : 50mg
| Reference | Short Name | Common Name | Inhibitory Carbohydrate | Glycans Structures Specifities |
|---|---|---|---|---|
| L1223 | PNA | Arachis hypogaea | ßGal | ß-D-Gal(1-3)-D-galNAc |
Arachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each (1, 2). PNA is a carbohydrate-free protein that displays specificity towards ß-D-Gal(1-3)-D-galNAc (3). It has potent anti-T activity and can be used to distinguish between human lymphocyte subsets. PNA has been used in tumour tissue determination for transitional mucosa malignancies. The lectin also agglutinates neuraminidase-treated human erythrocytes at < 0.1 μg/ml after trypsin treatment of cells and its activity is inhibited by lactose and galactose (1). PNA lectin is provided as a white to light yellow lyophilized powder from a buffer containing 10 mM NH4HCO3. The purity is determined by SDS-PAGE, which generates one band at 25-27 kDa. The lectin is available in vialscontaining 50 mg or 10 mg lyophilized powder and the product is to be used for laboratory work only.
Probe in histochemistry and immuno-histochemistry
Human erythrocyte/lymphocyte studies
Ultrapure quality
Strong anti-T activity
Sugar specificity: ß-D-Gal-(1-3)-D-GalNAc
Agglutinates rabbit erythrocytes at < 0.1 μg/ml after trypsin treatment of the cells
Lyophilized powder
| Reference | Name | Quantity |
|---|---|---|
| L1223-50 | PNA lectin | 50 mg |
| L1223-10 | PNA lectin | 10 mg |
(1) The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). R Lotan, E Skutelsky, D Danon and N Sharon. JBiol. Chem Vol. 250, No. 21
(2) Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin- lactose complex. Banerjee, R., Das, K., Ravishankar, R., Suguna, K., Surolia, A., Vijayan, M. (1996) J.Mol.Biol. 259: 281–96.
(3) Liener I. E., Sharon N., Goldstein I. J., (1986) The Lectins – Properties, Functions and Applications in Biology and Medicine.
| Reference | Short Name | Common Name | Inhibitory Carbohydrate | Glycans Structures Specifities | |
|---|---|---|---|---|---|
| L1222 | ABA | Agaricus Bisporus | Gal/GalNAc | Gal(β-1,3) GaINAc | |
| L1221 | AIA / Jacalin | Artocarpus intergrifolia | Gal | Galα1-6 or Galβ1-3GalNAc (T-antigen)>> lactose, more specific for T-antigen than PNA | |
| L1367 | AML | Astragalus membranaceus | Gal | Galβ | |
| L1205 | ASA | Allium sativum agglutinin | α(1,3)Man | Mannose | |
| L1889 | BanLec | Musa acuminata | Mannose, Glucose | αMan | |
| L1255 | BC2L-A | Burkholderia cenocepacia | α(1,3)Man | Mannose-containing ligands | |
| L1256 | BC2L-C | Burkholderia cenocepacia | Lewis b / Lewis Y | Fucose containing ligands | |
| L1254 | CJA | Crotalaria juncea | lactose | Gal > GalNAc | |
| L1366 | cMol | Moringa oleifera | fetuin, thyroglobuline | GlcNAc, Complex carbohydrate-binding specificity | |
| L1201 | Con A | Concanavalin A | MeαMan | α-Man, Glc | See
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