GeneBio Systems
Recombinant Rickettsia conorii Chaperonin GroEL (groEL), partial, Biotinylated
Recombinant Rickettsia conorii Chaperonin GroEL (groEL), partial, Biotinylated
SKU:Q92H04
Couldn't load pickup availability
Size: 100ug. Other sizes are also available.
Activity: Not tested
Research Areas: Others
Uniprot ID: Q92H04
Gene Names: groEL
Alternative Name(s): 60 kDa chaperonin;Chaperonin-60;Cpn60
Abbreviation: Recombinant Rickettsia conorii groEL protein, partial, Biotinylated
Organism: Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Source: E.coli
Expression Region: 191-340aa
Protein Length: Partial
Tag Info: N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged
Target Protein Sequence: KGMMFDRGYLSPYFVTNSEKMVAELENPFILLFEKKLSNLQPMLPILEAVVQSQRPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMMEDIAILTKGELITEDLGMKLENVSIKSLGTAKRVTISKENTVIVDGNGDKK
MW: 64.2 kDa
Purity: Greater than 85% as determined by SDS-PAGE.
Endotoxin: Not test
Biological_Activity:
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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage: 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℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Relevance: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Reference:
Function:
