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344146 FPTase, GST-Fusion, His•Tag®, Rat, Recombinant, E. coli

FPTase, GST-Fusion, His•Tag, Rat, Recombinant, E. coli, is composed of an74 kDa α- and 47 kDa β-subunit. The α-subunit is expressed as a GST-fusion construct with an N-terminal His•Tag sequence.

SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.

Synonyme: FTase, Farnesyl Proteintransferase

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344146
Preis & Verfügbarkeit

Übersicht

Replacement Information

Preis & Verfügbarkeit

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344146-100UG
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      		 Kst.-Ampulle 100 μg
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      Description
      OverviewRecombinant, rat FPTase composed of an α- and a β-subunit (74 and 46 kDa, respectively). The α-subunit is expressed as a GST-fusion construct with an N-terminal His•Tag® sequence. Both the GST moiety and the His•Tag® sequence can be utilized to facilitate enzyme capturing in prenylation and binding studies or, when desired, can also be cleaved off by TEV protease. Requires Zn2+ and Mg2+ for optimal activity.
      Catalogue Number344146
      Brand Family Calbiochem®
      SynonymsFTase, Farnesyl Proteintransferase
      References
      ReferencesZimmerman, K.K., et al. 1998. Protein Expr. Purif. 14, 395.
      Reiss, Y., et al. 1990. Cell 62, 81.
      Product Information
      FormLiquid
      FormulationIn 40 mM NaCl, 25 mM HEPES, 5 mM DTT, pH 7.2.
      Quality LevelMQ100
      Applications
      ApplicationFPTase, GST-Fusion, His•Tag, Rat, Recombinant, E. coli, is composed of an74 kDa α- and 47 kDa β-subunit. The α-subunit is expressed as a GST-fusion construct with an N-terminal His•Tag sequence.
      Biological Information
      Biological activity1 pmol FTase will transfer ≥1 pmol farnesyl to H-Ras in 10 min at 37°C, pH 7.2.
      Purity≥90% by SDS-PAGE
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Dry Ice Only
      Toxicity Standard Handling
      Storage ≤ -70°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Bestellnummer GTIN
      344146-100UG 04055977215236

      Documentation

      FPTase, GST-Fusion, His•Tag®, Rat, Recombinant, E. coli SDB

      Titel

      Sicherheitsdatenblatt (SDB) 

      FPTase, GST-Fusion, His•Tag®, Rat, Recombinant, E. coli Analysenzertifikate

      TitelChargennummer
      344146

      Literatur

      Übersicht
      Zimmerman, K.K., et al. 1998. Protein Expr. Purif. 14, 395.
      Reiss, Y., et al. 1990. Cell 62, 81.
      Datenblatt

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision26-June-2008 RFH
      SynonymsFTase, Farnesyl Proteintransferase
      DescriptionRecombinant, rat FPTase composed of an α- and a β-subunit (74 and 46 kDa, respectively). The α-subunit is expressed as a GST-fusion protein with an N-terminal His•Tag® sequence. Both the GST moiety and the His•Tag® sequence can be utilized to facilitate enzyme capturing in prenylation and binding studies or, when desired, can also be cleaved off by TEV protease. Requires Zn2+ and Mg2+ for optimal activity.
      FormLiquid
      FormulationIn 40 mM NaCl, 25 mM HEPES, 5 mM DTT, pH 7.2.
      Purity≥90% by SDS-PAGE
      Biological activity1 pmol FTase will transfer ≥1 pmol farnesyl to H-Ras in 10 min at 37°C, pH 7.2.
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesZimmerman, K.K., et al. 1998. Protein Expr. Purif. 14, 395.
      Reiss, Y., et al. 1990. Cell 62, 81.