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| Specifications |
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| Appearance (Form) | Liquid | | Appearance (Colour) | Dark Blue | | Appearance (Clarity) | Clear | | Concentration | 2X | | pH of solution | 6.8 | | SDS-PAGE Analysis | Good resoulution of individual proteins and optimum visibility of tracking dye during electrophoresis. |
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Description:
A ready-to-use 2X solution with beta-mercaptoethanol as a reducing agent. Used in SDS-PAGE for loading of conventional proteins. The use of Laemmli sample buffer ensures optimal band resolution when preparing proteins for SDS-PAGE with Tris-glycine-SDS running buffer.
Role of 2X SDS PAGE Sample buffer :
1 .Tris-HCl is a buffer and it’s pH plays an essential role in preserving peptide bonds from breaking apart.
2. Sodium dodecyl sulphate is an anionic detergent that helps in linearizing (by denaturing) the proteins and bringing a net negative charge to the proteins irrespective of the initial charge.
3. The high density of glycerol ensures the sample moves down into the well.
4. Beta-mercaptoethanol, along with SDS, ensure the bands are individual polypeptide instead of molecular complexes.
5. The dye visually indicates the location (tracking) of the sample in the gel.
Recommended volume:
Equal volume to the protein sample (1:1) or with the working concentration of 1X.
Notes:
Mercaptoethanol is irritating and toxic if swallowed or inhaled, so it is advised to handle it in an active fumigation hood.
Heating simply speeds up the process of denaturation by increasing molecular motion. Insufficient heating can leave some proteins incompletely denatured. It may require trial and error to achieve the best results. If samples are heated without first mixing with sample buffer, they will indeed be denatured, but not in the intended manner.
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| Available Packages |
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| Size |
Price |
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| 5 ml |
INR 390.00
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Add to Cart |
| 20 ml |
INR 1500.00
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Add to Cart |
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Prices indicative & subject to additional charges.
(Indian Rupees (INR))
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