Canavalia ensiformis (Concanavalin A, Con A, Jackbean) (Biotin)
Catalog No : USB-C1045-01A
439.09€
0.00€
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| Product name | Canavalia ensiformis (Concanavalin A, Con A, Jackbean) (Biotin) | ||
|---|---|---|---|
| Catalog No | USB-C1045-01A | ||
| Supplier’s Catalog No | C1045-01A | ||
| Supplier | US Biologicals | ||
| Source antigen | |||
| Reactivity | |||
| Cross reactivity | |||
| Applications | |||
| Molecular weight | |||
| Storage | -20°C | ||
|---|---|---|---|
| Other names | |||
| Grade | Molecular Biology Grade | ||
| Purity | ~95% | ||
| Form | Supplied as a lyophilized powder from 10mM HEPES, 0.15M sodium chloride, pH 7.5, 0.01mM Mn++, 0.1mM Ca++, 0.08% sodium azide. Reconstitute with 1ml sterile ddH2O. Labeled with Biotin | ||
| Reactivity life | 12 months | ||
| Note | For reserch purpose only | ||
| Purity | ~95% | ||
| Description | Con A is one of the most widely used and well characterized lectins. Con A has broad applicability primarily because it recognizes a commonly occurring sugar structure, a-linked mannose. Since a wide variety of serum and membrane glycoproteins have a “core oligosaccharide” structure which includes a-linked mannose residues, many glycoproteins can be examined or purified with Con A and its conjugates. Briefly, Con A has been utilized in hormone receptor studies, mitogenic assays, characterization of normal and malignant cells, glycoprotein purification, viral antigen isolation, dextran and mannan fractionation, cell agglutination studies, bacterial aggregation, membrane fluidity and lateral mobility investigations, turbidimetric assays for sugars, lymphokine production, as well as in many other applications. At neutral and alkaline pH, Con A exists as a tetramer of four identical subunits of approximately 26,000D each. Below pH 5.6, Con A dissociates into active dimers of 52,000D. Acetylation, succinylation or other derivatizations can also produce stable forms with dimeric structures. (See succinylated Con A). “Native” Con A is a mixture of several forms of the lectin due to “nicks” occurring in the polypeptide chains. Although having little or no effect on the saccharide binding activity, these “nicks” in the sequence are often revealed even in the purest lectin preparations as additional bands in SDS-polyacrylamide gel electrophoresis. These hydrolytic cleavage sites appear to exist in the lectin as it occurs in the seeds and are not a function of isolation procedures. Con A has an isoelectric point of about pH 5 and requires calcium or manganese ions at each of its four saccharide binding sites. Although these divalent metal ions are bound tightly to the polypeptide structure, buffers which can bind calcium (such as phosphate) generally should be avoided in diluting Con A, since a gradual loss in activity may occur. This biotinylated lectin conjugate is prepared from affinity-purified lectin and is optimally labeled with biotin. Essentially free of inactive lectin conjugate and containing no free biotin, this biotinylated lectin provides an ideal intermediate for examining glycoconjugates using the Biotin-Avidin System. First the biotin-labeled lectin is added, followed by an ABC Reagent, Avidin D conjugate, or streptavidin derivative. Another possible application is in the isolation of lymphokines and other products of mitogenic stimulation. Applications: Suitable for use in ELISA, Western Blot and Immunohistochemistry. Other applications not tested. Recommended Dilution: 5-20ug/ml freshly prepared Optimal dilutions to be determined by the researcher. Inhibiting/Eluting Sugar: 200mM a-methyl mannoside/200mM a-methyl glucoside Storage and Stability: Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. | ||
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