Analytical Data
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Gene name
groL
- Application
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Alternative Names
groL；groL；mopA；Tp4；Chaperonin GroEL
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
B6J2I0
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Expression Region
326-502aa
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AA Sequence
TKDDTTIIDGSGDAGDIKNRVEQIRKEIENSSSDYDKEKLQERLAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALIRVLKSLDSVEVENEDQRVGVEIARRAMAYPLSQIVKNTGVQAAVVADKVLNHKDVNYGYNAATGEYGDMIEMGILDPTKVTR
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Molecular Weight
26.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of groL recombinant proteins is rooted in the significance of chaperonin proteins in cellular processes. GroL, part of the chaperonin family, plays a crucial role in assisting the proper folding of newly synthesized proteins, particularly under stress conditions, such as heat shock. Found in various organisms, including bacteria and mitochondria, GroL forms a complex with GroS to create a molecular machine that facilitates the folding of misfolded proteins, thereby preventing aggregation and maintaining cellular homeostasis. Research into groL recombinant proteins has expanded in the context of biotechnology and medicine, particularly for developing protein-based therapeutics and vaccines. By producing groL in a recombinant form, researchers can better study its structure-function relationships, understand its chaperone mechanism, and explore its potential applications in protein misfolding diseases, such as Alzheimer's and cystic fibrosis. Furthermore, the ability to use groL as a fusion partner for enhancing the solubility and stability of recombinant proteins has made it a valuable tool in protein engineering. Overall, the investigation of groL and its recombinant forms continues to provide insights into protein biochemistry, with promising implications for therapeutic development and biotechnological applications.
