Recombinant human REP-2 protein (ab91088)
Key features and details
- Expression system: Saccharomyces cerevisiae
- Purity: > 90% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Description
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Product name
Recombinant human REP-2 protein -
Biological activity
Activity: 1 pmol of REP-2 will mediate transfer of 2 pmol of geranylgeraniol by RabGGTase onto 1 pmol of Rab7 in 3 minutes.
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Purity
> 90 % SDS-PAGE. -
Expression system
Saccharomyces cerevisiae -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab91088 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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Applications
SDS-PAGE
Functional Studies
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Form
Liquid -
Additional notes
Previously labelled as CHML.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.20
Constituents: 0.077% DTT, 0.595% HEPES, 0.232% Sodium chlorideThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- CHM like
- Chml
- Choroideraemia like protein
see all -
Function
Binds unprenylated Rab proteins, presents it to the catalytic Rab GGTase dimer, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Less effective than REP-1 in supporting prenylation of Rab3 family. -
Sequence similarities
Belongs to the Rab GDI family. - Information by UniProt
Protocols
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.
Datasheets and documents
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Datasheet download
References (0)
ab91088 has not yet been referenced specifically in any publications.