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Mitogenic lectin purified from the jack bean, C. ensiformis, that selectively cross-links cell-surface glycoproteins and affects the initiation of cell agglutination, mitogenesis, and apoptosis. Concanavalin A (ConA) binds to D-glucose, D-mannose and sterically related sugars in glycoproteins, and glycolipids and has been used in affinity chromatography purifications of various glycoproteins and cellular structures (1).It has potential anticancer effects due to mitogenic activity with lymphocytes and cancer cells (2). When administered, concanavalin A binds to glycoproteins of the cell membrane, inducing autophagy when it eventually enters the cell. Simultaneously, it triggers inflammation of tumorous cells, causing an immune response targeted against those cells. This simultaneous induction of immune response and autophagy makes it a potentially potent and novel cancer treatment. It is also used for studies of immune regulation across various cell types. Mitogenic lectin purified from the jack bean, C. ensiformis, that selectively cross-links cell-surface glycoproteins and affects the initiation of cell agglutination, mitogenesis, and apoptosis. Concanavalin A (ConA) binds to D-glucose, D-mannose and sterically related sugars in glycoproteins, and glycolipids and has been used in affinity chromatography purifications of various glycoproteins and cellular structures (1).It has potential anticancer effects due to mitogenic activity with lymphocytes and cancer cells (2). When administered, concanavalin A binds to glycoproteins of the cell membrane, inducing autophagy when it eventually enters the cell. Simultaneously, it triggers inflammation of tumorous cells, causing an immune response targeted against those cells. This simultaneous induction of immune response and autophagy makes it a potentially potent and novel cancer treatment. It is also used for studies of immune regulation across various cell types.
Product Detail
Modified by reductive methylation, no chymotryptic activity detectable. Specificity verified by digestion of oxidized B-chain of insulin. Trypsin NB Sequencing Grade, modified, is designed for digestion of proteins prior to mass spectrometric analysis. Reductive methylation of the lysine residues in trypsin provides a stable molecule that is extremely resistant to autolytic digest. Trypsin NB Sequencing Grade, modified, is purified by chromatography.A Trypsin Peptide (TP) Standard containing tryptic activity to generate masses m/z 842 and 2211 is delivered with each package. TP Standard allows internal calibration for enhancing mass accuracy.Trypsin, sequencing grade, is suitable for digestion of proteins for subsequent analysis by mass spectrometry and use in protein sequencing. Modification by reductive methylation of the lysine residues of trypsin results in an enzyme stable against autolysis. The trypsin is isolated from porcine pancreas and purified chromatographically. Specificity is tested by degradation of the oxidised ß-chain of insulin, chymotryptic activity is not detectable. Modified by reductive methylation, no chymotryptic activity detectable. Specificity verified by digestion of oxidized B-chain of insulin. Trypsin NB Sequencing Grade, modified, is designed for digestion of proteins prior to mass spectrometric analysis. Reductive methylation of the lysine residues in trypsin provides a stable molecule that is extremely resistant to autolytic digest. Trypsin NB Sequencing Grade, modified, is purified by chromatography.A Trypsin Peptide (TP) Standard containing tryptic activity to generate masses m/z 842 and 2211 is delivered with each package. TP Standard allows internal calibration for enhancing mass accuracy.Trypsin, sequencing grade, is suitable for digestion of proteins for subsequent analysis by mass spectrometry and use in protein sequencing. Modification by reductive methylation of the lysine residues of trypsin results in an enzyme stable against autolysis. The trypsin is isolated from porcine pancreas and purified chromatographically. Specificity is tested by degradation of the oxidised ß-chain of insulin, chymotryptic activity is not detectable.
Product Detail
Cohn-Fraction II. Highly purified. Soluble in saline and standard buffers. Suitable to reduce non-specific adsorption of antibody in immunoassay systems. Starting material for the isolation of IgG subclasses. Cohn-Fraction II. Highly purified. Soluble in saline and standard buffers. Suitable to reduce non-specific adsorption of antibody in immunoassay systems. Starting material for the isolation of IgG subclasses.
Product Detail
Mitogenic lectin purified from the jack bean, C. ensiformis, that selectively cross-links cell-surface glycoproteins and affects the initiation of cell agglutination, mitogenesis, and apoptosis. Concanavalin A (ConA) binds to D-glucose, D-mannose and sterically related sugars in glycoproteins, and glycolipids and has been used in affinity chromatography purifications of various glycoproteins and cellular structures (1).It has potential anticancer effects due to mitogenic activity with lymphocytes and cancer cells (2). When administered, concanavalin A binds to glycoproteins of the cell membrane, inducing autophagy when it eventually enters the cell. Simultaneously, it triggers inflammation of tumorous cells, causing an immune response targeted against those cells. This simultaneous induction of immune response and autophagy makes it a potentially potent and novel cancer treatment. It is also used for studies of immune regulation across various cell types. Mitogenic lectin purified from the jack bean, C. ensiformis, that selectively cross-links cell-surface glycoproteins and affects the initiation of cell agglutination, mitogenesis, and apoptosis. Concanavalin A (ConA) binds to D-glucose, D-mannose and sterically related sugars in glycoproteins, and glycolipids and has been used in affinity chromatography purifications of various glycoproteins and cellular structures (1).It has potential anticancer effects due to mitogenic activity with lymphocytes and cancer cells (2). When administered, concanavalin A binds to glycoproteins of the cell membrane, inducing autophagy when it eventually enters the cell. Simultaneously, it triggers inflammation of tumorous cells, causing an immune response targeted against those cells. This simultaneous induction of immune response and autophagy makes it a potentially potent and novel cancer treatment. It is also used for studies of immune regulation across various cell types.
Product Detail
Cohn-Fraction II. Highly purified. Soluble in saline and standard buffers. Suitable to reduce non-specific adsorption of antibody in immunoassay systems. Starting material for the isolation of IgG subclasses. Cohn-Fraction II. Highly purified. Soluble in saline and standard buffers. Suitable to reduce non-specific adsorption of antibody in immunoassay systems. Starting material for the isolation of IgG subclasses.
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© 2023 Copyright. All Rights Reserved. Unit 19, Euroway House, Roydsdale Way, Bradford, BD4 6SE, UK
