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Expression, purification and cellular uptake of a S100A4 protein - stian sjli
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stian sjli:
Expression, purification and cellular uptake of a S100A4 protein - Taschenbuch

ISBN: 9783639173062

[ED: Taschenbuch], [PU: VDM Verlag], Neuware - A recombinant S100A4 protein was produced in Pichia pastoris (Pichia). The expression vector contained parts of the AOX1 promoter and also a secretion signal, making it possible to purify the protein from the yeast media after methanol induction. Attempts were made to purify the protein from the media both by hydrophobic interaction chromatography (HIC) and by anionic ion exchange chromatography (IEC). The binding capacity to the hydrophobic material was rather low, but the eluted protein did however show an acceptable purity for utilization in downstream functional assays. The protein eluted from the hydrophobic column was labelled with the fluorescent dye (Cy3) and used for internalization studies in the human cell line HeLa. Similar to a mouse rS100A4 produced in bacterial cells, the Pichia produced protein was also found internalized into the HeLa cells. The biological significance of these findings is at present not elucidated and will be further studied. - - Besorgungstitel - vorauss. Lieferzeit 3-5 Tage., [SC: 0.00], Neuware, gewerbliches Angebot, 220x150x9 mm, [GW: 243g]

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Expression, purification and cellular uptake of a S100A4 protein - stian sjøli
Vergriffenes Buch, derzeit bei uns nicht verfügbar.
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stian sjøli:
Expression, purification and cellular uptake of a S100A4 protein - Taschenbuch

2009, ISBN: 3639173066

ID: 9852880183

[EAN: 9783639173062], Neubuch, [PU: VDM Verlag Jul 2009], This item is printed on demand - Print on Demand Neuware - A recombinant S100A4 protein was produced in Pichia pastoris (Pichia). The expression vector contained parts of the AOX1 promoter and also a secretion signal, making it possible to purify the protein from the yeast media after methanol induction. Attempts were made to purify the protein from the media both by hydrophobic interaction chromatography (HIC) and by anionic ion exchange chromatography (IEC). The binding capacity to the hydrophobic material was rather low, but the eluted protein did however show an acceptable purity for utilization in downstream functional assays. The protein eluted from the hydrophobic column was labelled with the fluorescent dye (Cy3) and used for internalization studies in the human cell line HeLa. Similar to a mouse rS100A4 produced in bacterial cells, the Pichia produced protein was also found internalized into the HeLa cells. The biological significance of these findings is at present not elucidated and will be further studied. 152 pp. Englisch

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Expression, purification and cellular uptake of a S100A4 protein - stian sjøli
Vergriffenes Buch, derzeit bei uns nicht verfügbar.
(*)
stian sjøli:
Expression, purification and cellular uptake of a S100A4 protein - Taschenbuch

2009, ISBN: 3639173066

ID: 9852880183

[EAN: 9783639173062], Neubuch, [PU: Vdm Verlag Jul 2009], This item is printed on demand - Print on Demand Titel. - A recombinant S100A4 protein was produced in Pichia pastoris (Pichia). The expression vector contained parts of the AOX1 promoter and also a secretion signal, making it possible to purify the protein from the yeast media after methanol induction. Attempts were made to purify the protein from the media both by hydrophobic interaction chromatography (HIC) and by anionic ion exchange chromatography (IEC). The binding capacity to the hydrophobic material was rather low, but the eluted protein did however show an acceptable purity for utilization in downstream functional assays. The protein eluted from the hydrophobic column was labelled with the fluorescent dye (Cy3) and used for internalization studies in the human cell line HeLa. Similar to a mouse rS100A4 produced in bacterial cells, the Pichia produced protein was also found internalized into the HeLa cells. The biological significance of these findings is at present not elucidated and will be further studied. 152 pp. Englisch

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Expression, purification and cellular uptake of a S100A4 protein - Stian Sjøli
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Stian Sjøli:
Expression, purification and cellular uptake of a S100A4 protein - neues Buch

2009, ISBN: 9783639173062

ID: 219265935

A recombinant S100A4 protein was produced in Pichia pastoris (Pichia). The expression vector contained parts of the AOX1 promoter and also a secretion signal, making it possible to purify the protein from the yeast media after methanol induction. Attempts were made to purify the protein from the media both by hydrophobic interaction chromatography (HIC) and by anionic ion exchange chromatography (IEC). The binding capacity to the hydrophobic material was rather low, but the eluted protein did however show an acceptable purity for utilization in downstream functional assays. The protein eluted from the hydrophobic column was labelled with the fluorescent dye (Cy3) and used for internalization studies in the human cell line HeLa. Similar to a mouse rS100A4 produced in bacterial cells, the Pichia produced protein was also found internalized into the HeLa cells. The biological significance of these findings is at present not elucidated and will be further studied. an agent promoting metastasis Bücher > Fremdsprachige Bücher > Englische Bücher Taschenbuch 01.07.2009, VDM, .200

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Expression, purification and cellular uptake of a S100A4 protein - stian sjøli
Vergriffenes Buch, derzeit bei uns nicht verfügbar.
(*)
stian sjøli:
Expression, purification and cellular uptake of a S100A4 protein - Taschenbuch

2009, ISBN: 3639173066

ID: 20014811431

[EAN: 9783639173062], Neubuch, [PU: VDM Verlag Jul 2009], Neuware - A recombinant S100A4 protein was produced in Pichia pastoris (Pichia). The expression vector contained parts of the AOX1 promoter and also a secretion signal, making it possible to purify the protein from the yeast media after methanol induction. Attempts were made to purify the protein from the media both by hydrophobic interaction chromatography (HIC) and by anionic ion exchange chromatography (IEC). The binding capacity to the hydrophobic material was rather low, but the eluted protein did however show an acceptable purity for utilization in downstream functional assays. The protein eluted from the hydrophobic column was labelled with the fluorescent dye (Cy3) and used for internalization studies in the human cell line HeLa. Similar to a mouse rS100A4 produced in bacterial cells, the Pichia produced protein was also found internalized into the HeLa cells. The biological significance of these findings is at present not elucidated and will be further studied. 152 pp. Englisch

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sparbuchladen, Göttingen, Germany [52968077] [Rating: 5 (von 5)]
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