Recombinant Human GTF2F2 protein (ab81892)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Suitable for: GSA, SDS-PAGE
Description
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Product name
Recombinant Human GTF2F2 protein
See all GTF2F2 proteins and peptides -
Biological activity
1 unit equals 1 nanogram of purified protein. -
Purity
> 95 % SDS-PAGE. -
Expression system
Escherichia coli -
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 ab81892 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
Gel Supershift Assays
SDS-PAGE
EMSA
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Form
Liquid -
Additional notes
1 unit equals 1 nanogram of purified protein. -
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: 7.9
Constituents: 0.75% Potassium chloride, 0.0154% DTT, 0.316% Tris HCl, 0.00584% EDTA, 20% Glycerol (glycerin, glycerine)
General Info
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Alternative names
- ATP dependent helicase GTF2F2
- ATP-dependent helicase GTF2F2
- BTF4
see all -
Function
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity. -
Sequence similarities
Belongs to the TFIIF beta subunit family. -
Post-translational
modificationsPhosphorylated upon DNA damage, probably by ATM or ATR. -
Cellular localization
Nucleus. - 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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SDS download
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Datasheet download
References (0)
ab81892 has not yet been referenced specifically in any publications.