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T8782

Sigma-Aldrich

Tryptose Phosphate Broth

buffered powder, Microbiologically tested.

Synonyme(s) :

Tryptose Broth

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About This Item

Code UNSPSC :
41106507
Nomenclature NACRES :
NA.75

Forme

buffered powder

Niveau de qualité

200

Qualité

Microbiologically tested.

Catégories apparentées

Description générale

The tryptose component of Tryptose Phosphate Broth is a peptone (mixture of amino acids and short peptides) derived by the mixed enzymatic hydrolysis (pancreatic enzymes) of the milk protein casein.

Application

In addition to its use for the growth of fastidious micro-organisms, Tryptose Phospate Broth (TPB) has been studied as supplement for the preparation of media that supports vaccine production in BHK-21 cells and the growth of SF21 insect cells in high-density perfusion culture stirred-tank bioreactors.
Tryptose Phosphate Broth has been used as a component:
  • of Leibovitz L-15 medium for the culture of BME26 tick embryo cell line
  • of M199 medium for the preparation of chick embryo fibroblasts (CEFs)
  • of Glasgow′s minimum essential medium (GMEM) for culturing baby hamster kidney (BHK-21) before transfection

Actions biochimiques/physiologiques

Tryptose Phosphate Broth provides a source of amino acid based nutrients and survival factors that support the growth of fastidious micro-organisms such as Brucella, Streptococcus, and Neisseria; as well as eukaryotic cells such as insect and animal cells. Dextrose provides a fermentable carbohydrate that can be used by fastidious micro-organisms. Sodium chloride maintains the osmotic and ionic equilibrium and disodium phosphate provides the basic buffering capacity.

Composants

Tryptose Phosphate Broth (TPB) is composed of four components: Tryptose (20g/L); Dextrose (2g/L); NaCl (5g/L) and Disodium Phosphate (2.5g/L) typically adjusted to pH 7.3. The tryptose component is a peptone (mixture of amino acids and short peptides) derived by the mixed enzymatic hydrolysis (pancreatic enzymes) of the milk protein casein. This hydrolysate provides a source of amino acid based nutrients and survival factors that support the growth of fastidious micro-organisms such as Brucella, Streptococcus, and Neisseria; as well as eukaryotic cells such as insect and animal cells. Dextrose provides a fermentable carbohydrate that can be used by fastidious mico-organisms. Sodium chloride maintains the osmotic and ionic equilibrium and disodium phosphate provides the basic buffering capacity.

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Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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The use of sonicated lipid vesicles for mass spectrometry of membrane protein complexes
Chorev DS, et al.
Nature Protocols, 15(5), 1690-1706 (2020)
Generating recombinant avian herpesvirus vectors with crispr/cas9 gene editing
Tang NA, et al.
Journal of Visualized Experiments, 143, e58193-e58193 (2019)
Christiano Calixto Conceição et al.
Scientific reports, 11(1), 19202-19202 (2021-09-30)
In the present work, we established two novel embryonic cell lines from the mosquito Aedes fluviatilis containing or not the naturally occurring symbiont bacteria Wolbachia, which were called wAflu1 and Aflu2, respectively. We also obtained wAflu1 without Wolbachia after tetracycline
S M Deutschmann et al.
Enzyme and microbial technology, 16(6), 506-512 (1994-06-01)
Spodoptera frugiperda insect cells (IPLB-Sf21-AE) (Sf21), infected with baculovirus expression vectors during their exponential growth phase, are commonly used to produce a variety of heterologous recombinant proteins. In the present study the culture conditions of these insect cells were studied
Dror S Chorev et al.
Nature protocols, 15(5), 1690-1706 (2020-04-03)
Recent applications of mass spectrometry (MS) to study membrane protein complexes are yielding valuable insights into the binding of lipids and their structural and functional roles. To date, most native MS experiments with membrane proteins are based on detergent solubilization.
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