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345852 Geranylgeranyltransferase I, GST-Fusion, His•Tag®, Rat, Recombinant, E. coli

345852
Purchase on Sigma-Aldrich

Descripción

Replacement Information

Tabla espec. clave

Products

Número de referenciaEmbalaje Cant./Env.
345852-50UG Ampolla de plást. 50 μg
Description
OverviewRecombinant, rat GGTase I composed of an α- and a β-subunit (74 and 43 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+ for optimal activity.
Catalogue Number345852
Brand Family Calbiochem®
SynonymsGGTase I
References
ReferencesKalinin, A., et al. 2001. Protein Expr. Purif. 22, 84.
Zhang, F.L., et al. 1994. J. Biol. Chem. 269, 23465.
Moomaw, J.F., and Casey, P.J., 1992. J. Biol. Chem. 267, 17438.
Product Information
FormLiquid
FormulationIn 40 mM NaCl, 25 mM HEPES, 5 mM DTT, pH 7.2.
Applications
ApplicationGeranylgeranyltransferase I, GST-Fusion, His•Tag®, Rat, Recombinant, E. coli, contains a 74 kDa α- & 43 kDa β-subunit. The α-subunit is expressed as a GST-fusion construct with an N-terminal His•Tag.
Biological Information
Biological activity1 pmol enzyme will transfer ≥3 pmol geranylgeranyl to RhoA 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

Documentation

Geranylgeranyltransferase I, GST-Fusion, His•Tag®, Rat, Recombinant, E. coli Ficha datos de seguridad (MSDS)

Título

Ficha técnica de seguridad del material (MSDS) 

Geranylgeranyltransferase I, GST-Fusion, His•Tag®, Rat, Recombinant, E. coli Certificados de análisis

CargoNúmero de lote
345852

Referencias bibliográficas

Visión general referencias
Kalinin, A., et al. 2001. Protein Expr. Purif. 22, 84.
Zhang, F.L., et al. 1994. J. Biol. Chem. 269, 23465.
Moomaw, J.F., and Casey, P.J., 1992. J. Biol. Chem. 267, 17438.
Ficha técnica

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.

Revision30-June-2008 RFH
SynonymsGGTase I
DescriptionRecombinant, rat GGTase I composed of an α- and a β-subunit (74 and 43 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 by TEV protease. Requires Zn2+ for optimal activity. The enzyme is purified with Zn2+ tightly bound, so addition of Zn2+ to the reaction mix is not necessary unless further manipulation of the enzyme results in release of the ions.
FormLiquid
FormulationIn 40 mM NaCl, 25 mM HEPES, 5 mM DTT, pH 7.2.
Recommended reaction conditions50 mM HEPES, pH 7.2, 5 mM MgCl2, 1 mM DTT, 3 mM NP-40 alternative, 5.5 µM [3H]GG pyrophosphate, 30 pmol acceptor protein of choice, and desired amount of enzyme; incubate at 37°C for 20 min.; quench the reaction with 10% HCl in 90% Ethanol.
Purity≥90% by SDS-PAGE
Biological activity1 pmol enzyme will transfer ≥3 pmol geranylgeranyl to RhoA in 10 min at 37°C, pH 7.2.
Storage ≤ -70°C
Avoid freeze/thaw
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesKalinin, A., et al. 2001. Protein Expr. Purif. 22, 84.
Zhang, F.L., et al. 1994. J. Biol. Chem. 269, 23465.
Moomaw, J.F., and Casey, P.J., 1992. J. Biol. Chem. 267, 17438.