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low molecular mass standards  (Amersham Life Sciences Inc)

 
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    Amersham Life Sciences Inc low molecular mass standards
    Low Molecular Mass Standards, supplied by Amersham Life Sciences Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/low+molecular+mass+standards/protein+standards/10__1016_slash_j__jfoodeng__2025__112882-100-0-4
    Average 86 stars, based on 1 article reviews
    low molecular mass standards - by Bioz Stars, 2026-09
    86/100 stars

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    other:

    Article Title: Hydrocolloid interaction with water, protein, and starch in wheat dough.
    Article Snippet: NATALIA LINLAUD, EVELINA FERRER, MARÍA CECILIA PUPPO, AND CRISTINA FERRERO* CIDCA,Facultad deCiencias Exactas,UniversidadNacional deLa Plata, 47 y 116 (1900) La Plata, Provincia Buenos Aires, Argentina, ‡ CEQUINOR, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, 47 y 115 (1900) La Plata, Provincia BuenosAires, Argentina, and # Facultad de Ciencias Agrarias y Forestales, Universidad Nacional de La Plata, 60 y 119 (1900), La Plata, Provincia da Buenos Aires, Argentina

    Article Title: Enhancing aquafaba from lentils and common beans functionality: the role of ultrasound and pH on their microstructure, molecular, and foaming properties
    Article Snippet: Aquafaba is a valuable yet underutilized resource, and due to its complex composition, it holds many potential applications, mainly as a foaming agent.. Post-treatments can be applied to enhance its technofunctional properties, requiring an assessment of their effects on its microstructure and molecular characteristics.. This study evaluates the physicochemical, structural, and functional properties of aquafaba from lentils and beans, focusing on ultrasound and pH adjustments (pH = 3.5).

    Article Title: Effect of glutens of different quality on dough characteristics and breadmaking performance
    Article Snippet: Glutens of different quality were extracted from commercial flours of distinct breadmaking performance and employed as improvers at a level of 1 g/100 g. The same flours used as a source of gluten were employed for testing the gluten effect.. Flours were characterized by farinographic and alveographic assays and their protein profile was determined by SDS-PAGE.. Rheology of each dough without and with gluten addition was studied by empirical and fundamental assays.



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    Figure 1. Localization of Mefp-2 in Mytilis edutilis foot and byssus. (A) AU-PAGE analysis of acid-urea soluble proteins from a serially sectioned mussel foot. Lanes 1-5 correspond to the indicated foot sections and were stained with Coomassie Blue. Lanes 1'-5' correspond to the same sections run on a parallel gel stained by the NBT redox cycling assay. The drawn parallel bars indicate position of Mefp-I (upper) and Mefp-2 (lower) proteins. Schematic codes are: S, stem of the byssus; CG, collagen gland; AG, accessory gland; VG, ventral groove; DD, distal depression; and PG, phenol gland. (B) SDS-PAGE ( 15% polyacrylamide) of proteins extracted from threads and plaques in SDS and neutral buffer. Gels stained as indicated; symbols P, T, M-2 and St refer to: plaque extract, thread extract, pure Mefp-2, and <t>molecular</t> weight <t>standards,</t> respectively; arrows indicate Mefp-2. (C) AU-PAGE analysis of acetic acid-urea soluble proteins from threads and plaques. Gels stained as indicated; symbols are as in (B); arrows indicate Mefp-2. The higher molecular weight aggregates apparent in pure Mefp-2 in (B) and (C) were artefactual results of prolonged storage in water at -20?C and were never found in freshly isolated <t>protein.</t> Arnow tests were not performed in (B) and (C). (D) Dot blots of pure DOPA proteins, and thread and plaque acetic acid-urea soluble proteins, stained as indicated. The amount of total protein blotted is given in the center; symbols are as in (B).
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    Figure 1. Localization of Mefp-2 in Mytilis edutilis foot and byssus. (A) AU-PAGE analysis of acid-urea soluble proteins from a serially sectioned mussel foot. Lanes 1-5 correspond to the indicated foot sections and were stained with Coomassie Blue. Lanes 1'-5' correspond to the same sections run on a parallel gel stained by the NBT redox cycling assay. The drawn parallel bars indicate position of Mefp-I (upper) and Mefp-2 (lower) proteins. Schematic codes are: S, stem of the byssus; CG, collagen gland; AG, accessory gland; VG, ventral groove; DD, distal depression; and PG, phenol gland. (B) SDS-PAGE ( 15% polyacrylamide) of proteins extracted from threads and plaques in SDS and neutral buffer. Gels stained as indicated; symbols P, T, M-2 and St refer to: plaque extract, thread extract, pure Mefp-2, and <t>molecular</t> weight <t>standards,</t> respectively; arrows indicate Mefp-2. (C) AU-PAGE analysis of acetic acid-urea soluble proteins from threads and plaques. Gels stained as indicated; symbols are as in (B); arrows indicate Mefp-2. The higher molecular weight aggregates apparent in pure Mefp-2 in (B) and (C) were artefactual results of prolonged storage in water at -20?C and were never found in freshly isolated <t>protein.</t> Arnow tests were not performed in (B) and (C). (D) Dot blots of pure DOPA proteins, and thread and plaque acetic acid-urea soluble proteins, stained as indicated. The amount of total protein blotted is given in the center; symbols are as in (B).
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    Image Search Results


    BOX-PCR patterns of the seven TRS isolates of Bacillus genus. (L–R) Lane 1, DNA molecular mass standard (Generuler 2-Log DNA Ladder, New England Biolabs, USA; size indicated in the left-hand margin); lane 2, no DNA control (sterile water); lanes 3–9, Bacillus spp. TRS-2, TRS-4, TRS-7, TRS-8, TRS-1, TRS-3 and TRS-5. Full, non-adjusted gel images are provided in Supplementary File 1.

    Journal: Heliyon

    Article Title: Functional and molecular characterization of plant growth promoting Bacillus isolates from tomato rhizosphere

    doi: 10.1016/j.heliyon.2020.e04734

    Figure Lengend Snippet: BOX-PCR patterns of the seven TRS isolates of Bacillus genus. (L–R) Lane 1, DNA molecular mass standard (Generuler 2-Log DNA Ladder, New England Biolabs, USA; size indicated in the left-hand margin); lane 2, no DNA control (sterile water); lanes 3–9, Bacillus spp. TRS-2, TRS-4, TRS-7, TRS-8, TRS-1, TRS-3 and TRS-5. Full, non-adjusted gel images are provided in Supplementary File 1.

    Article Snippet: BOX-PCR patterns of the seven TRS isolates of Bacillus genus. (L–R) Lane 1, DNA molecular mass standard (Generuler 2-Log DNA Ladder, New England Biolabs, USA; size indicated in the left-hand margin); lane 2, no DNA control (sterile water); lanes 3–9, Bacillus spp.

    Techniques:

    Figure 1. Localization of Mefp-2 in Mytilis edutilis foot and byssus. (A) AU-PAGE analysis of acid-urea soluble proteins from a serially sectioned mussel foot. Lanes 1-5 correspond to the indicated foot sections and were stained with Coomassie Blue. Lanes 1'-5' correspond to the same sections run on a parallel gel stained by the NBT redox cycling assay. The drawn parallel bars indicate position of Mefp-I (upper) and Mefp-2 (lower) proteins. Schematic codes are: S, stem of the byssus; CG, collagen gland; AG, accessory gland; VG, ventral groove; DD, distal depression; and PG, phenol gland. (B) SDS-PAGE ( 15% polyacrylamide) of proteins extracted from threads and plaques in SDS and neutral buffer. Gels stained as indicated; symbols P, T, M-2 and St refer to: plaque extract, thread extract, pure Mefp-2, and molecular weight standards, respectively; arrows indicate Mefp-2. (C) AU-PAGE analysis of acetic acid-urea soluble proteins from threads and plaques. Gels stained as indicated; symbols are as in (B); arrows indicate Mefp-2. The higher molecular weight aggregates apparent in pure Mefp-2 in (B) and (C) were artefactual results of prolonged storage in water at -20?C and were never found in freshly isolated protein. Arnow tests were not performed in (B) and (C). (D) Dot blots of pure DOPA proteins, and thread and plaque acetic acid-urea soluble proteins, stained as indicated. The amount of total protein blotted is given in the center; symbols are as in (B).

    Journal: The Biological bulletin

    Article Title: Characterization of a Cystine-Rich Polyphenolic Protein Family from the Blue Mussel Mytilus edulis L.

    doi: 10.2307/1542413

    Figure Lengend Snippet: Figure 1. Localization of Mefp-2 in Mytilis edutilis foot and byssus. (A) AU-PAGE analysis of acid-urea soluble proteins from a serially sectioned mussel foot. Lanes 1-5 correspond to the indicated foot sections and were stained with Coomassie Blue. Lanes 1'-5' correspond to the same sections run on a parallel gel stained by the NBT redox cycling assay. The drawn parallel bars indicate position of Mefp-I (upper) and Mefp-2 (lower) proteins. Schematic codes are: S, stem of the byssus; CG, collagen gland; AG, accessory gland; VG, ventral groove; DD, distal depression; and PG, phenol gland. (B) SDS-PAGE ( 15% polyacrylamide) of proteins extracted from threads and plaques in SDS and neutral buffer. Gels stained as indicated; symbols P, T, M-2 and St refer to: plaque extract, thread extract, pure Mefp-2, and molecular weight standards, respectively; arrows indicate Mefp-2. (C) AU-PAGE analysis of acetic acid-urea soluble proteins from threads and plaques. Gels stained as indicated; symbols are as in (B); arrows indicate Mefp-2. The higher molecular weight aggregates apparent in pure Mefp-2 in (B) and (C) were artefactual results of prolonged storage in water at -20?C and were never found in freshly isolated protein. Arnow tests were not performed in (B) and (C). (D) Dot blots of pure DOPA proteins, and thread and plaque acetic acid-urea soluble proteins, stained as indicated. The amount of total protein blotted is given in the center; symbols are as in (B).

    Article Snippet: Low molecular mass protein standards ranged from 14.4-97.4 kDa (BioRad, California).

    Techniques: Staining, SDS Page, Molecular Weight, Isolation