Recombinant Lactobacillus delbrueckii subsp. bulgaricus 60 kDa chaperonin (groL), partial

SKU: Q1G937

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: Q1G937

Gene Names: groEL

Alternative Name(s): (60 kDa chaperonin)(Chaperonin-60)(Cpn60)

Abbreviation: Recombinant Lactobacillus delbrueckii subsp. bulgaricus groEL protein, partial

Organism: Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14)

Source: E.coli

Expression Region: 182-374aa

Protein Length: Partial

Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged

Target Protein Sequence: ETELSVVEGMQFDRGYLSQYMVTDNDKMEADLENPYILITDKKISNIQDILPMLQEIVQQGRSLLIIADDVTGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKEQLADIAALTGGTVISEDLGLELKDTQLSQLGQARRVTITKDSTTIVDGSGAKEAIQERVDTIRKQIEDTSSDFDKKKLQERLAKLTGGV

MW: 26.3 kDa

Purity: Greater than 90% 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: "The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution." van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. Maguin E. Proc. Natl. Acad. Sci. U.S.A. 103: 9274-9279(2006)

Function: