Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Active: Yes
- Tags: GST tag N-Terminus
- Suitable for: Functional Studies, SDS-PAGE
Product nameRecombinant rat FNTA + FNTB protein
Biological activityActivity: 1 pmol of FNTA + FNTB will transfer 1 pmol of farnesyl to H-Ras in 15 min at 37°C.
Purity> 90 % SDS-PAGE.
Expression systemEscherichia coli
Protein lengthFull length protein
TagsGST tag N-Terminus
Our Abpromise guarantee covers the use of ab90512 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.077% DTT, 2.38% HEPES, 0.58% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- CAAX box, alpha
RelevanceFNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTB, farnesyltransferase subunit beta, catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab90512 has not yet been referenced specifically in any publications.