Arachis hypogaea Lectin (PNA)

Katalog-Nummer L1223-50

Size : 50mg

Marke : GLYcoDiag


Arachis hypogaea lectin (PNA, Peanut Agglutinin)

GlycoSciences reagents, Lectins
ReferenceShort NameCommon NameInhibitory CarbohydrateGlycans Structures Specifities
L1223PNAArachis hypogaeaßGalß-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.

Applications

Probe in histochemistry and immuno-histochemistry
Human erythrocyte/lymphocyte studies

Features

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

Ordering informations

Reference Name Quantity
L1223-50 PNA lectin 50 mg
L1223-10 PNA lectin 10 mg

References

(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.

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ReferenceShort NameCommon NameInhibitory CarbohydrateGlycans Structures Specifities
L1222ABAAgaricus BisporusGal/GalNAcGal(β-1,3) GaINAc
L1221AIA / JacalinArtocarpus intergrifoliaGalGalα1-6 or Galβ1-3GalNAc (T-antigen)>> lactose, more specific for T-antigen than PNA
L1367AMLAstragalus membranaceusGalGalβ
L1205ASAAllium sativum agglutininα(1,3)ManMannose
L1889BanLecMusa acuminataMannose, GlucoseαMan
L1255BC2L-ABurkholderia cenocepaciaα(1,3)ManMannose-containing ligands
L1256BC2L-CBurkholderia cenocepaciaLewis b / Lewis YFucose containing ligands
L1254CJACrotalaria juncealactoseGal > GalNAc
L1366cMolMoringa oleiferafetuin, thyroglobulineGlcNAc, Complex carbohydrate-binding specificity
L1201Con AConcanavalin AMeαManα-Man, Glc