Recombinant Chlamydia trachomatis Chaperonin GroEL (groEL)

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Code CSB-EP314770DSB
MSDS
Size US$388
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP314770DSB could indicate that this peptide derived from E.coli-expressed Chlamydia trachomatis (strain D/UW-3/Cx) groL.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP314770DSB could indicate that this peptide derived from E.coli-expressed Chlamydia trachomatis (strain D/UW-3/Cx) groL.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
groL
Uniprot No.
Alternative Names
groL; groEL; hypB; mopA; CT_11060 kDa chaperonin; 57 kDa chlamydial hypersensitivity antigen; GroEL protein; Heat shock protein 60; HSP60; Protein Cpn60
Species
Chlamydia trachomatis (strain D/UW-3/Cx)
Source
E.coli
Expression Region
2-544aa
Target Protein Sequence
VAKNIKYNEEARKKIQKGVKTLAEAVKVTLGPKGRHVVIDKSFGSPQVTKDGVTVAKEVELADKHENMGAQMVKEVASKTADKAGDGTTTATVLAEAIYTEGLRNVTAGANPMDLKRGIDKAVKVVVDQIRKISKPVQHHKEIAQVATISANNDAEIGNLIAEAMEKVGKNGSITVEEAKGFETVLDIVEGMNFNRGYLSSYFATNPETQECVLEDALVLIYDKKISGIKDFLPVLQQVAESGRPLLIIAEDIEGEALATLVVNRIRGGFRVCAVKAPGFGDRRKAMLEDIAILTGGQLISEELGMKLENANLAMLGKAKKVIVSKEDTTIVEGMGEKEALEARCESIKKQIEDSSSDYDKEKLQERLAKLSGGVAVIRVGAATEIEMKEKKDRVDDAQHATIAAVEEGILPGGGTALIRCIPTLEAFLPMLTNEDEQIGARIVLKALSAPLKQIAANAGKEGAIIFQQVMSRSANEGYDALRDAYTDMLEAGILDPAKVTRSALESAASVAGLLLTTEALIAEIPEEKPAAAPAMPGAGMDY
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
74.0 kDa
Protein Length
Full Length of Mature Protein
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
Troubleshooting and FAQs
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

The expression region of this recombinant Chlamydia trachomatis (strain D/UW-3/Cx) groL covers amino acids 2-544. The calculated molecular weight for this groL protein is 74.0 kDa. Expression of this groL protein is conducted in e.coli. The N-terminal 6xHis-SUMO tag was smoothly integrated into the coding gene of groL, which enables a simple process of detecting and purifying the groL recombinant protein in the following steps.

The Chaperonin GroEL is a protein encoded by the groEL gene in Chlamydia trachomatis. Chaperonins are molecular chaperones that assist in the proper folding of newly synthesized or stress-denatured proteins. GroEL forms a complex with its co-chaperonin GroES, creating a barrel-like structure that provides a confined environment for the folding of substrate proteins. The Chlamydia trachomatis Chaperonin GroEL likely plays a crucial role in the correct folding of proteins within the bacterium, ensuring their functional integrity. Proper protein folding is essential for various cellular processes, including virulence and survival within the host. Understanding the function of Chaperonin GroEL in Chlamydia trachomatis can provide insights into the pathogenic mechanisms of this obligate intracellular bacterium and may contribute to the development of therapeutic strategies.

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Target Background

Function
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.
Subcellular Location
Cytoplasm.
Protein Families
Chaperonin (HSP60) family
Database Links

KEGG: ctr:CT_110

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