24405C
EX-CELL® 405 Serum-Free Medium for Insect Cells
Protein-free, with L-glutamine, without sodium bicarbonate, dry powder, suitable for insect cell culture
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About This Item
Produtos recomendados
Nível de qualidade
descrição
for research or for further manufacturing use
forma
dry powder
técnica(s)
cell culture | insect: suitable
temperatura de armazenamento
2-8°C
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Aplicação
Baculoviruses are powerful expression systems for production of recombinant proteins. The most well known and highly investigated baculovirus vector expression system (BEVS) uses Spodoptera frugiperda cells (especially Sf9) as the host cell of choice for infection with recombinant Autographa californica nuclear polyhedrosis virus for heterologous protein expression. Recent investigations have shown that other cell lines may be better expression substrates than spodopteran cells. The BTI-TN-5B1-4 clone of Trichoplusia ni, commonly referred to as High Five™, is reported to be a superior host substrate for the expression of selected recombinant proteins using BEVS. This cell line portrays strong adherent characteristics, but can be adapted to suspension growth.
EX-CELL™ 405 is a serum-free medium for optimal growth and viability of BTI-TN-5B1-4 (Tn5, High Five) cells. In addition, EX-CELL 405 supports recombinant protein production in High Five cells to higher levels than reported for Sf9 cells. EX-CELL 405 is a complete medium. No protein supplements need to be added to this medium prior to use.
EX-CELL™ 405 is a serum-free medium for optimal growth and viability of BTI-TN-5B1-4 (Tn5, High Five) cells. In addition, EX-CELL 405 supports recombinant protein production in High Five cells to higher levels than reported for Sf9 cells. EX-CELL 405 is a complete medium. No protein supplements need to be added to this medium prior to use.
Baculoviruses are powerful expression systems for production of recombinant proteins. The most well known and highly investigated baculovirus vector expression system (BEVS) uses Spodoptera frugiperda cells (especially Sf9) as the host cell of choice for infection with recombinant Autographa californica nuclear polyhedrosis virus for heterologous protein expression. Recent investigations have shown that other cell lines may be better expression substrates than spodopteran cells. The BTI-TN-5B1-4 clone of Trichoplusia ni, commonly referred to as High Five™, is reported to be a superior host substrate for the expression of selected recombinant proteins using BEVS. This cell line portrays strong adherent characteristics, but can be adapted to suspension growth.
EX-CELL™ 405 is a serum-free medium for optimal growth and viability of BTI-TN-5B1-4 (Tn5, High Five) cells. In addition, EX-CELL 405 supports recombinant protein production in High Five cells to higher levels than reported for Sf9 cells. EX-CELL 405 is a complete medium. No protein supplements need to be added to this medium prior to use.
EX-CELL™ 405 is a serum-free medium for optimal growth and viability of BTI-TN-5B1-4 (Tn5, High Five) cells. In addition, EX-CELL 405 supports recombinant protein production in High Five cells to higher levels than reported for Sf9 cells. EX-CELL 405 is a complete medium. No protein supplements need to be added to this medium prior to use.
Quantidade
Formulated to contain 42.7 grams of powder per liter of medium.
Informações legais
EX-CELL is a registered trademark of Merck KGaA, Darmstadt, Germany
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Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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M S Donaldson et al.
Biotechnology progress, 14(4), 573-579 (1998-08-08)
The BTI-Tn5B1-4 insect cell line, commercially available as the High Five cell line (Invitrogen), supports higher levels of recombinant protein production compared to existing insect cell lines. Proprietary serum-free media such as ExCell 405 (JRH Biosciences), Express Five (Life Technologies)
R A Taticek et al.
Biotechnology progress, 17(4), 676-684 (2001-08-04)
Culture conditions required for obtaining maximum recombinant protein concentrations from two cell lines, Spodoptera frugiperda (IPLBeta-Sf21-AE) and Trichoplusia ni (Tn 5Beta-1-4), were determined in this work. Conditions studied include mode of culture (suspended vs attached), agitation rates, inoculum sizes, cell
Gulzhakhan Sadvakassova et al.
BMC research notes, 2, 215-215 (2009-10-27)
C21, the C-terminal peptide of thrombospondin-4, has growth promoting activity and was discovered as one of several erythropoietin-dependent endothelial proteins. C21 stimulates red cell formation in anemic mice and is a growth factor for CD34+ and CD36+ hematopoietic cells, skin
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