Canavalia ensiformis (Concanavalin A, Con A, Jackbean) (Rhodamine)
Catalog No : USB-C1045-01C
509.21€
0.00€
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| Product name | Canavalia ensiformis (Concanavalin A, Con A, Jackbean) (Rhodamine) | ||
|---|---|---|---|
| Catalog No | USB-C1045-01C | ||
| Supplier’s Catalog No | C1045-01C | ||
| Supplier | US Biologicals | ||
| Source antigen | |||
| Reactivity | |||
| Cross reactivity | |||
| Applications | |||
| Molecular weight | |||
| Storage | -20°C | ||
|---|---|---|---|
| Other names | |||
| Grade | Molecular Biology Grade | ||
| Purity | |||
| Form | Supplied as a liquid in 10mM HEPES, 0.15M sodium chloride, pH 7.5, 0.1mM Ca++ 0.08% sodium azide, 0.01mM Mn++. Labeled with Rhodamine. | ||
| Reactivity life | 12 months | ||
| Note | For reserch purpose only | ||
| Purity | |||
| 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. Rhodamine labeled Concanavalin A is produced by using the highest quality tetramethylrhodamine isothiocyanate, our affinity-purified lectin, and special conjugation procedures. Rhodamine labeled Concanavalin A has an appropriate number of fluorochromes bound which provide the maximum fluorescence and optimum staining characteristics for this particular lectin. This lectin is supplied essentially free of unconjugated fluorochromes and inactive lectin. Accompanying each fluorescent lectin is an analysis data sheet summarizing the results of our quality control tests and providing pertinent information on the product. All of these reagents are supplied as solutions perserved with sodium azide. Applications: Suitable for use in FLISA. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Inhibiting/Eluting Sugar: 200mM a-methyl mannoside/200mM a-methyl glucoside mixture Absorption: 550nm Emission: 575nm F/P (molar): 3.5 Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months 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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