Recombinant Human SMAD5 protein (ab84651)
Key features and details
- Expression system: Escherichia coli
- Purity: > 85% Densitometry
- Suitable for: WB, SDS-PAGE
Description
-
Product name
Recombinant Human SMAD5 protein -
Purity
> 85 % Densitometry. -
Expression system
Escherichia coli -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
-
Species
Human
-
Associated products
-
Related Products
Specifications
Our Abpromise guarantee covers the use of ab84651 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
-
Applications
Western blot
SDS-PAGE
-
Form
Liquid -
Concentration information loading...
Preparation and Storage
-
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.50
Constituents: 0.00174% PMSF, 0.00385% DTT, 0.79% Tris HCl, 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
General Info
-
Alternative names
- DKFZp781C1895
- DKFZp781O1323
- Dwfc
see all -
Function
Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD). -
Tissue specificity
Ubiquitous. -
Sequence similarities
Belongs to the dwarfin/SMAD family.
Contains 1 MH1 (MAD homology 1) domain.
Contains 1 MH2 (MAD homology 2) domain. -
Post-translational
modificationsPhosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase.
Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin ligase SMURF1. -
Cellular localization
Cytoplasm. Nucleus. Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. - Information by UniProt
Images
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
-
SDS download
-
Datasheet download
References (0)
ab84651 has not yet been referenced specifically in any publications.