Recombinant Human Methionine Sulfoxide Reductase B protein (ab99522)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE
Description
-
Product name
Recombinant Human Methionine Sulfoxide Reductase B protein -
Purity
> 90 % SDS-PAGE.
ab99522 was purified using conventional chromatography. -
Expression system
Escherichia coli -
Accession
-
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
-
Species
Human -
Sequence
MGSSHHHHHHSSGLVPRGSHMSFCSFFGGEVFQNHFEPGVYVCAKCGYEL FSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGH EFLNDGPKPGQSRFCIFSSSLKFVPKGKETSASQGH -
Predicted molecular weight
15 kDa including tags -
Amino acids
1 to 116 -
Tags
His tag N-Terminus
-
Associated products
-
Related Products
Specifications
Our Abpromise guarantee covers the use of ab99522 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
-
Applications
SDS-PAGE
-
Mass spectrometry
MALDI-TOF -
Form
Liquid -
Concentration information loading...
Preparation and Storage
-
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
pH: 7.50
Constituents: 0.00174% PMSF, 0.0154% DTT, 0.316% Tris HCl, 0.0584% EDTA, 10% Glycerol (glycerin, glycerine)
General Info
-
Alternative names
- Annexin A2 like
- EC 1 8 4
- HSPC 270
see all -
Sequence similarities
Belongs to the MsrB Met sulfoxide reductase family. -
Cellular localization
Cytoplasm. 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
-
SDS download
-
Datasheet download
References (1)
ab99522 has been referenced in 1 publication.
- Yin Y et al. Surf4 (Erv29p) binds amino-terminal tripeptide motifs of soluble cargo proteins with different affinities, enabling prioritization of their exit from the endoplasmic reticulum. PLoS Biol 16:e2005140 (2018). PubMed: 30086131