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Chromatein Prestained Protein Ladder (ready-to-use)
品牌:Vivantis Technologies
貨號:PR0602
規(guī)格:2 x 250 μl
貨期:
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Home Ladders/ Markers/Nucleic Acids/ Nucleotides Protein Ladders & Markers Chromatein Prestained Protein Ladder Chromatein Prestained Protein Ladder Description Chromatein Prestained Protein Ladder contains 11 proteins that resolve into sharp, tight bands in the range of 10-175 kDa. It is supplied in a loading buffer for direct loading on gels. Allows monitoring molecular weight separation d

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Home  Ladders/ Markers/Nucleic Acids/ Nucleotides  Protein Ladders & Markers  Chromatein Prestained Protein Ladder

Chromatein Prestained Protein Ladder

Description
Chromatein Prestained Protein Ladder contains 11 proteins that resolve into sharp, tight bands in the range of 10-175 kDa. It is supplied in a loading buffer for direct loading on gels. Allows monitoring molecular weight separation during electrophoresis, estimation of molecular weights of interest and evaluate western transfer efficiency.

Feature
Broad Range: 10-175kDa 
Convenient: Supplied in a loading buffer for direct loading
Easy Identification: ~10, ~40, and ~90kDa reference bands coupled with a blue dye

Quality Control
Tested in SDS-polyacrylamide gel electrophoresis and western blotting

Storage

  • Stable at 4°C for 3 months
  • Store at -20°C for 24 months

 

Ordering Information

Catalog No Description Pack Size
PR0602 Chromatein Prestained Protein Ladder (ready-to-use) 2 x 250 μl

Download
Manual

Chromatein Prestained Protein Ladder

Publication
This Product Has Been Used In: 
Dehnaiv, E., Fathi-Roudsari,M., Mirzaie, S., Arab., S.S., Siadat, S.O.R., Khajeh, K. (2017) Engineering disulfide bonds in Selenomonas ruminantium B-xylosidase by experimental and computational methods. International Journal of Biological Macromolecules. 95. Pp.248-255 
Karimi, M., Biria, D. (2016) ) The synergetic effect of starch and alpha amylase on the biodegradation of n-alkanes 
Golshani, M., et al. (2016) In silico Analysis of Brucella abortus 0mp2b and In vitro Expression of S0mp2b. Clinical and Experimental Vaccine Research. 5(1), p.75-82. 
Golshani, M., Rafati, S., Siadat, S.D.,Nejati-Moheimani, M., Shahcheraghi, F., Arsang, A., Bouzari, S. (2015) Improved immunogenicity and protective efficacy of a divalent DNA vaccine encoding Brucella L7/L12-truncated Omp31 fusion protein by a DNA priming and protein boosting regimen. Molecular Immunology 66. Pp.384-391. 
Ungcharoenwiwat, P., H-Kittikun A. (2015) Purification and characterization of lipase from Burkholderia sp. EQ3 isolated from wastewater from a canned fish factory and its application for the synthesis of wax esters. Journal of Molecular Catalysis B: Enzymatic.115. Pp..96-104 
Thongsaiklaing, T., et al. (2014)Analysis of the α-amylase Gene Sequence and the Enzyme Activity of Indian Rock Oyster Saccostrea forskali . Fisheries ScienceProQuest. p. 589-601. 
Gharajelar, S.N., Ahmadi, M., & Hosseini, B. (2012) 2015) Cloning and Expression of the Immunogenic Moiety of Pseudomonas aeruginosa Exotoxin A Biological Journal of Microorganism1(4), p. 7-14.

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