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ROTI®Load 2

4x conc., unreducing
Icon_ready-to-use Ready-to-use products and reagents
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H318
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VE
Verp.
Gel loading buffer, Laemmli buffer
Density (D) 1,158 g/cm³
Storage temp. +15 to +25 °C
Transport temp. ambient temp.
WGK 2

Protein gel loading buffer, modified formulation acc. to Laemmli. For protein complexes, secondary structures, and for native gels.
Contains SDS (approx. 8 % w/v), glycerol (approx. 40 % v/v) and bromophenol blue (approx. 0,015 % w/v). Phosphate buffered.

ROTI®Load 1 (reducing) as well as ROTI®Load 2 and 3 (non-reducing) represent special gel loading buffers for protein gel electrophoresis. They have been designed to protect your proteins during sample preparation and to stabilise sensitive peptide bonds. Protein degradation is efficiently prevented by those buffer systems. ROTI®Load are 4x concentrated ready-to-use solutions, which may be used directly for sample loading.
Productdetails

17,75 €/VE 

Excl. btw | 10 ml Per VE

Bestelnr. K930.1

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Vanaf 6 VE 16,86 €/VE
Vanaf 24 VE 15,98 €/VE
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Productdetails


ROTI®Load 1 (reducing) as well as ROTI®Load 2 and 3 (non-reducing) represent special gel loading buffers for protein gel electrophoresis. They have been designed to protect your proteins during sample preparation and to stabilise sensitive peptide bonds. Protein degradation is efficiently prevented by those buffer systems. ROTI®Load are 4x concentrated ready-to-use solutions, which may be used directly for sample loading.



ROTI®Load 2 4x conc., unreducing

Well tested and proven sample buffer for protein gel electrophoresis that has been modified and further developed based on the original formulation acc. to Laemmli (Nature 227, 1970). For depiction of protein complexes, secondary structures, and for native gels.

  • Formulation acc. to Laemmli (modified)
  • Stabilises peptide bands
  • For protein complexes and secondary structures
  • For native gels

Gebruiksinstructies

ROTI®Load protein gel loading buffers are usually used as 1x concentrated solution. ROTI®Load can either be added to the prepared sample or the precipitated proteins are dissolved directly into ROTI®Load. Optionally, heat the ROTI®Load mixed sample to 95 °C for 5 minutes to break hydrogen bonds and stretch the peptide chains.


ROTI®Load 2 prevents degradation of proteins while heating during sample preparation, additionally keeping the sample pH value constant during gel electrophoresis. Being a phosphate-buffered ready-to-use solution, ROTI®Load 2 already contains all necessary denaturing reagents, bromophenol blue as dye and glycerol as density increasing reagent. ROTI®Load 2 may be supplemented with 20 µl/ml DTT solution (1 M), in order to gain a loading buffer using DTT as reducing reagent rather than β-Mercaptoethanol.



ROTI®Load 2
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Bestelnr. VE Verp. Prijs Hoeveelheid
K930.1 10 ml glass

17,75 €

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Geselecteerde hoeveelheid:   0
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Downloads / MSDS


Algemene informatie

Selecting a Suitable ROTI®Load Gel Loading Buffer for Proteins

ROTI®Load 1 is suitable for all PAGE standard gels. It has denaturing and reducing properties.
ROTI®Load 2 is suitable for protein complexes, secondary structures and native gels. It has denaturing properties, but it does not have reducing properties. It is possible to enrich the buffer solution with reducing agents such as β-Mercaptoethanol or DTT.
ROTI®Load 3 is suitable for native gels, precast gels and cooled gels. The buffer solution contains LDS. Unlike SDS, LDS does not crystallise out at low temperatures. In addition, the buffer solution is optimally adapted for precast gels. ROTI®Load 3 has denaturing properties, but does not have reducing properties. It is possible to enrich the buffer solution with reducing agents such as ß-Mercaptoethanol or DTT.

Glycerine is the standard reagent for increasing the density of samples.
SDS (sodium dodecyl sulphate), LDS (lithium dodecyl sulphate) are anionic surfactants. They form a negatively charged mantle around the protein molecules, which results in a denaturing effect. This process is reversible. Irreversible denaturation only occurs if the samples are boiled. Negative charging allows the molecules to be separated during electrophoresis.
β-mercaptoethanol, DTT (dithiothreitol) are reducing agents which split disulphide bridges in protein molecules. Increased unfolding of the molecule occurs. This process is reversible.


Analysecertificaten

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Type analysis

Appearancedark blue, clear solution
pH value (1x sol.)6.7-7.2
Remark: Contains SDS. Can be redissolved by heating (max. 45 °C).