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LECTIN FROM BANDEIRAEA SIMPLICIFOLIA BS-
Кат. №: L2895-.2MG
Производитель: Sigma-Aldrich
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LECTIN FROM BANDEIRAEA SIMPLICIFOLIA BS-
Main image
Кат. №: L2895-.2MG
Производитель: Sigma-Aldrich
Кол-во:
Цена по запросу
Товар оформляется под заказ
Main image
Печать
LECTIN FROM BANDEIRAEA SIMPLICIFOLIA BS-
Кат. №: L2895-.2MG
Производитель: Sigma-Aldrich
Кол-во:
Цена по запросу
Товар оформляется под заказ
Description_x000D_ General description_x000D_ 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 possesses carbohydrate binding sites on the surface._x000D_ Application_x000D_ Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has been used for microglia detection in murine astrocytes culture by staining the culture with lectin BS1-B4. It has also been used in the preparation of staining solution to incubate the tissue sections._x000D_ Packaging_x000D_ 0.2, 1 mg in serum bottle_x000D_ Biochem/physiol Actions_x000D_ Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling, 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._x000D_ BS-I has a major affinity for terminal α-D-galactosyl residues with a secondary affinity for terminal N-acetyl-α-D-galactosaminyl residues._x000D_ Packaging_x000D_ Package size based on protein content by Lowry._x000D_ Other Notes_x000D_ BS-I is a tetrameric lectin consisting of two types of subunits designated A and B. There are five BS-I isolectins with different subunit composition: BSI-B4, BSI-AB3, BSI-A2B2, BSI-A3B and BSI-A4. BSI-B4 is blood group B specific and has an exclusive affinity for terminal α-D-galactosyl residues, whereas BSI-A4 has blood group A specificity and has a major affinity for terminal N-acetyl-α-D-galactosaminyl residues._x000D_ Analysis Note_x000D_ Agglutination activity is expressed in μg/mL and is determined from serial dilutions of a 1 mg/mL solution using phosphate buffered saline, pH 6.8, containing, for each lectin, calcium, magnesium, and manganese at different concentrations. This activity is the lowest concentration to agglutinate a 2% suspension of appropriate erythrocytes after 1 hr incubation at 25 °C.
Related Categories
Bandeiraea simplicifolia (Griffonia simplicifolia), Cell Biology, Cell Signaling and Neuroscience, Glycan Recognizing Proteins, Glycobiology, Immune Cell Signaling and Blood, Immune System Regulation, Lectins, Lectins and Lectin Antibodies, Molecular Biology, Post-Translational Modification, ProteomicsMore... Quality Level
Дорогой клиент, на сайте внедрена нейросеть для сбора информации о товаре. Это может привести к незначительным расхождениям в характеристиках продукции.
Description_x000D_ General description_x000D_ 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 possesses carbohydrate binding sites on the surface._x000D_ Application_x000D_ Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has been used for microglia detection in murine astrocytes culture by staining the culture with lectin BS1-B4. It has also been used in the preparation of staining solution to incubate the tissue sections._x000D_ Packaging_x000D_ 0.2, 1 mg in serum bottle_x000D_ Biochem/physiol Actions_x000D_ Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling, 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._x000D_ BS-I has a major affinity for terminal α-D-galactosyl residues with a secondary affinity for terminal N-acetyl-α-D-galactosaminyl residues._x000D_ Packaging_x000D_ Package size based on protein content by Lowry._x000D_ Other Notes_x000D_ BS-I is a tetrameric lectin consisting of two types of subunits designated A and B. There are five BS-I isolectins with different subunit composition: BSI-B4, BSI-AB3, BSI-A2B2, BSI-A3B and BSI-A4. BSI-B4 is blood group B specific and has an exclusive affinity for terminal α-D-galactosyl residues, whereas BSI-A4 has blood group A specificity and has a major affinity for terminal N-acetyl-α-D-galactosaminyl residues._x000D_ Analysis Note_x000D_ Agglutination activity is expressed in μg/mL and is determined from serial dilutions of a 1 mg/mL solution using phosphate buffered saline, pH 6.8, containing, for each lectin, calcium, magnesium, and manganese at different concentrations. This activity is the lowest concentration to agglutinate a 2% suspension of appropriate erythrocytes after 1 hr incubation at 25 °C.
Related Categories
Bandeiraea simplicifolia (Griffonia simplicifolia), Cell Biology, Cell Signaling and Neuroscience, Glycan Recognizing Proteins, Glycobiology, Immune Cell Signaling and Blood, Immune System Regulation, Lectins, Lectins and Lectin Antibodies, Molecular Biology, Post-Translational Modification, ProteomicsMore... Quality Level
Дорогой клиент, на сайте внедрена нейросеть для сбора информации о товаре. Это может привести к незначительным расхождениям в характеристиках продукции.