Purity
Greater than 85% as determined by SDS-PAGE.
Research Area
Epigenetics and Nuclear Signaling
Species
Homo sapiens (Human)
Expression Region
1-207aa
Target Protein Sequence
MAASRCSGLSEMTLLGSQAVSGLSSPLKSPCQVWNSPSPVCVCVCVCVCVCTRVHMRACSAGSAYLKQMKFCRMAASLDKVKKTDRGERGSCVSTTKRQASLSQRDIPSNNMKLATFPSDVNVESVAASLFFTVMKLGATQLEWNTKTPLGNTSSGFESQLYHSPAIDSEQDLSEVISSQSVETRLTSKVLKVEPESMNAKVFTFKL
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Protein Length
Full Length
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that
we have in stock, however, if you have any special requirement for the format, please remark your
requirement when placing the order, we will prepare according to your demand.
Buffer
Tris-based buffer,50% glycerol
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw
cycles.
Shelf Life
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.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description
Constructing a plasmid that codes for the Human MIG7 protein (1-207aa) initiates the generation of the recombinant Human MIG7 protein. The constructed plasmid is transformed into 1-207aa cells. Positive e.coli cells are selected and then cultured under conditions that encourage the expression of the gene of interest. The protein is equipped with a N-terminal 6xHis-SUMO tag. After that, affinity purification is employed to isolate and purify the recombinant MIG7 protein from the cell lysate. The purity of the resulting recombinant MIG7 protein is over 85%, determined by SDS-PAGE.