GST Protein (AA 1-218) (His tag)
Kurzübersicht für GST Protein (AA 1-218) (His tag) (ABIN666898)
Target
Alle GST Proteine anzeigenProtein-Typ
Biologische Aktivität
Spezies
Quelle
Applikation
Reinheit
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Proteineigenschaft
- AA 1-218
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Aufreinigungstag / Konjugat
- Dieses GST Protein ist gelabelt mit His tag.
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Sequenz
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MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK -
Produktmerkmale
- GST, 1-224aa, Schistosoma japonicum, His-tag, E.coli
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Aufreinigung
- > 90% by SDS-PAGE
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Endotoxin-Niveau
- < 1 EU per 1ug of protein (determined by LAL method)
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Biological Activity Comment
- Specific activity is > 10unit/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.
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Applikationshinweise
- Optimal working dilution should be determined by the investigator.
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Beschränkungen
- Nur für Forschungszwecke einsetzbar
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Format
- Liquid
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Konzentration
- 1 mg/mL
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Buffer
- Phosphate-Buffered Saline ( pH 7.4) 10 % glycerol
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Lagerung
- 4 °C,-20 °C,-80 °C
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Informationen zur Lagerung
- Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
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- GST (Glutathione S Transferase (GST))
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Andere Bezeichnung
- Glutathione S-transferase/GST
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Hintergrund
- Glutathione S-transferase (GST) represents a major group of detoxification enzymes. This enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form an S-substituted glutathione (S=sulfur). The reactions utilizing glutathione contribute the transformation of a wide range of compounds, including carcinogens, therapeutic drugs, and products of oxidative stress. As well as its enzymatic activities, GST may also bind toxins and function as transport protein. Because of this, an early term for GSTs was ligandin. Glutathione S-transferase was originally separated from Schistosoma japonicum but currently isolated from recombinant E. coli source. Recombinant Schistosoma japonicum GST, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.
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Molekulargewicht
- 28.3 kDa (244aa) confirmed by MALDI-TOF
Target
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