L5667
LB Agar Ampicillin-100, Plates
pre-poured LB agar plates with 100 μg/ml ampicillin
Synonyme(s) :
ampicillin agar plates
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A propos de cet article
UNSPSC Code:
41121800
Sterility:
sterile; autoclaved
Suitability:
selective for Escherichia coli, selective for coliforms
Service technique
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Molecular Biology
Quality Level
sterility
sterile; autoclaved
form
plates (10 cm), plates (10cm, 20-25ml each)
availability
available only in USA
capacity
20-25 mL
storage temp.
2-8°C
suitability
selective for Escherichia coli, selective for coliforms
General description
Miller′s LB is a highly-referenced microbial growth medium used for the cultivation of E. coli. This nutrient-rich microbial broth contains peptides, amino acids, water-soluble vitamins, and carbohydrates in a low-salt formulation. The addition of agar provides a solid medium for microbial growth.
Application
LB Agar Ampicillin-100, Plates has been used to plate and incubate the mixture of thawed bacteria and plasmid solution for vimentin expression. It has also been used in the generation of the Trypanosoma brucei RNAi library.
Features and Benefits
Miller′s LB Agar plates provide:
- Convenient, ready-to-use 10cm format
- Standard formulation plus antibiotic
Other Notes
15g/L Agar
10g/L Tryptone
10g/L NaCl
5g/L Yeast Extract
100μg/ml ampicillin
10g/L Tryptone
10g/L NaCl
5g/L Yeast Extract
100μg/ml ampicillin
The plates must be used within two months of the manufacture date to ensure the antibiotics are fully active. The product may be shipped up until its expiration date but is generally shipped 2-4 weeks before expiration.
Classe de stockage
13 - Non Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Articles
Genetic engineering enables large-scale expression and isolation of recombinant proteins for research purposes.
Viscoelastic properties of vimentin originate from nonequilibrium conformational changes
Block J, et al.
Science advances, 4(6) (2018)
Viscoelastic properties of vimentin originate from nonequilibrium conformational changes
Block J, et al.
Science Advances, 4(6) (2018)
Linfeng Xu et al.
Nature communications, 12(1), 6803-6803 (2021-11-25)
Enzymes are represented across a vast space of protein sequences and structural forms and have activities that far exceed the best chemical catalysts; however, engineering them to have novel or enhanced activity is limited by technologies for sensing product formation.
Numéro d'article de commerce international
| Référence | GTIN |
|---|---|
| L5667-10EA | 04061833958346 |