miniprotean iii cell vertical slab gel electrophoresis apparatus (Bio-Rad)
95
Structured Review
Bio-Rad
miniprotean iii cell vertical slab gel electrophoresis apparatus
Miniprotean Iii Cell Vertical Slab Gel Electrophoresis Apparatus, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 681 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/miniprotean+iii+cell+apparatus/Mini-PROTEAN+3+Dodeca+Cell/pmc07341071-75-1-9
Average 95 stars, based on 681 article reviews
Miniprotean Iii Cell Vertical Slab Gel Electrophoresis Apparatus, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 681 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/miniprotean+iii+cell+apparatus/Mini-PROTEAN+3+Dodeca+Cell/pmc07341071-75-1-9
Average 95 stars, based on 681 article reviews
miniprotean iii cell vertical slab gel electrophoresis apparatus - by Bioz Stars,
2026-10
95/100 stars
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SDS Page:Article Title: Purification of antifreeze protein from wheat bran (Triticum aestivum L.) based on its hydrophilicity and ice-binding capacity. Article Snippet: Wheat-bran (Triticum aestivum L.) antifreeze protein (TaAFP) was purified 323-fold to electrophoretic homogeneity with an overall yield of 1.64% from wheat-bran protein by a specific three-step procedure.. The three-step procedure was quicker, cheaper, and more effective than the five-step procedure we used earlier.. First, TaAFP was concentrated by a phosphate buffer, on the basis of its strong hydrophilicity that was validated by thermal gravimetric analyses and a surface hydrophobicity analysis. Electrophoresis:Article Title: Purification of antifreeze protein from wheat bran (Triticum aestivum L.) based on its hydrophilicity and ice-binding capacity. Article Snippet: Wheat-bran (Triticum aestivum L.) antifreeze protein (TaAFP) was purified 323-fold to electrophoretic homogeneity with an overall yield of 1.64% from wheat-bran protein by a specific three-step procedure.. The three-step procedure was quicker, cheaper, and more effective than the five-step procedure we used earlier.. First, TaAFP was concentrated by a phosphate buffer, on the basis of its strong hydrophilicity that was validated by thermal gravimetric analyses and a surface hydrophobicity analysis. |