Recombinant Escherichia phage MS2 Capsid protein
Product Specifications
Product Name Alternative
Coat protein; CP
Abbreviation
Recombinant Escherichia phage MS2 Capsid protein
UniProt
P03612
Expression Region
2-130aa
Organism
Escherichia phage MS2 (Bacteriophage MS2)
Target Sequence
ASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQNRKYTIKVEVPKVATQTVGGVELPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY
Tag
C-terminal 10xHis-tagged
Type
Developed Protein
Source
E.coli
Field of Research
Others
Relevance
Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) . Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid also contains 1 copy of the A2 maturation protein
Endotoxin
Not test
Purity
Greater than 85% as determined by SDS-PAGE.
Activity
Not Test
Form
Liquid or Lyophilized powder
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Molecular Weight
23.5 kDa
Storage Conditions
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Protein Length
Full Length of Mature Protein
Available Sizes
Curated Selection
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