NYLM-RO
Roche
Nylon Membranes, positively charged
roll W × L 0.3 m × 3 m, sheet W × L 10 cm × 15 cm, sheet W × L 20 cm × 30 cm
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About This Item
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packaging
pkg of 10 sheets (11209272001[20 x 30 cm])
pkg of 20 sheets (11209299001[10 x 15 cm])
Quality Level
manufacturer/tradename
Roche
roll W × L
0.3 m × 3 m
sheet W × L
10 cm × 15 cm
20 cm × 30 cm
storage temp.
20-25°C
General description
Microporous nylon 66 membrane on a polyester support, carrying positively charged (pH 3 - 10) quaternary ammonium groups.
Surface Properties: Pore size of 0.45μm
Surface Properties: Pore size of 0.45μm
Application
- The physical and chemical properties of the nylon membranes make them specifically useful as a matrix for hybridization with nonradioactively (e.g., digoxigenin or biotin) and radioactively (e.g., [32P], [35S], an [3H])-labeled DNA, RNA, or oligonucleotide probes: Southern blots
- Northern blots
- Dot blots
Features and Benefits
Microporous nylon 66 membrane on a polyester support, carrying positively charged quaternary ammonium groups.
Contents: Membranes
Contents: Membranes
Quality
Function tested for homogenous DNA detection in Southern blot procedures using the DIG System.
Other Notes
For life science research only. Not for use in diagnostic procedures.
Certificates of Analysis (COA)
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The production of antimicrobial peptides is a common defense strategy of living cells against a wide range of pathogens. Plant snakin peptides inhibit bacterial and fungal growth at extremely low concentrations. However, little is known of their molecular and ecological
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Histoplasma capsulatum is a fungal respiratory pathogen that survives and replicates within the phagolysosome of macrophages. The molecular factors it utilizes to subvert macrophage antimicrobial defenses are largely unknown. Although the ability of H. capsulatum to prevent acidification of the
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Proceedings of the National Academy of Sciences of the United States of America, 108(8), 3276-3281 (2011-02-09)
JmjC domain-containing proteins play a crucial role in the control of gene expression by acting as protein hydroxylases or demethylases, thereby controlling histone methylation or splicing. Here, we demonstrate that silencing of Jumonji domain-containing protein 6 (Jmjd6) impairs angiogenic functions
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