Analytical Data
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Gene name
SlyD
- Application
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Alternative Names
slyD;FKBP-type peptidyl-prolyl cis-trans isomerase SlyD
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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
P0A9K9
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Expression Region
1-196aa
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AA Sequence
MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH
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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
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Protein Description
SlyD is a highly conserved protein found in various organisms, including bacteria and eukaryotes, and plays a crucial role in protein folding and quality control within the cellular environment. This protein is known for its unique domain structure, which combines a peptidyl-prolyl isomerase (PPIase) domain with a tetratricopeptide repeat (TPR) domain. The PPIase activity of SlyD facilitates the proper folding of substrate proteins by catalyzing the isomerization of proline residues, which can be a rate-limiting step in protein folding. Additionally, the TPR domain is involved in protein-protein interactions, allowing SlyD to act as a molecular chaperone that assists in the assembly and stabilization of multi-protein complexes. Research has implicated SlyD in various cellular processes, including stress responses, and its dysfunction has been linked to diseases such as cancer and neurodegenerative disorders. Recent studies have focused on characterizing SlyD's molecular mechanisms, understanding its interactions with other cellular components, and exploring its potential as a therapeutic target. As a result, SlyD is gaining attention not only for its fundamental biological roles but also for its potential applications in biotechnology and medicine.
