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Key Documents

L0543

Sigma-Aldrich

LB Agar Kanamycin-50, Plates

pre-poured LB agar plates with 50 ug/ml kanamycin

Sinonimo/i:

kanamycin agar plates

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About This Item

Codice UNSPSC:
41121800

Grado

for molecular biology

Livello qualitativo

200

Sterilità

sterile; autoclaved

Forma fisica

plates (10 cm)
plates (10cm, 20-25ml each)

Capacità

20-25 mL

Temperatura di conservazione

2-8°C

Compatibilità

selective for Escherichia coli
selective for coliforms

Descrizione generale

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.

Applicazioni

Suitable for selective cultivation of E. coli strains that contain plasmids conferring kanamycin resistance. The bacteria can be used for DNA plasmid production or production of recombinant proteins. LB Agar Kanamycin-50, Plates has been used in the screening of Agrobacterium tumefaciens and E.coli JM83 strain with pGD103 plasmid.

Caratteristiche e vantaggi

Miller′s LB Agar plates provide:
  • Convenient, ready-to-use 10cm format
  • Standard formulation plus antibiotic

Componenti

15g/L Agar
10g/L Tryptone
10g/L NaCl
5g/L Yeast Extract
50μg/ml kanamycin

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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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Articoli

Protein Expression Systems

The development of genetic engineering and cloning has opened many possibilities of expression and isolation of heterologous proteins for research purposes. Considerable advances in technology have enabled expression and isolation of recombinant proteins in large scale.

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