Analytical Data
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Gene name
SurA
- Application
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Alternative Names
SurA；Chaperone SurA
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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
P0ABZ6
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Expression Region
21-428aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH M APQVVDKVA AVVNNGVVLE SDVDGLMQSV KLNAAQARQQ LPDDATLRHQ IMERLIMDQI ILQMGQKMGV KISDEQLDQA IANIAKQNNM TLDQMRSRLA YDGLNYNTYR NQIRKEMIIS EVRNNEVRRR ITILPQEVES LAQQVGNQND ASTELNLSHI LIPLPENPTS DQVNEAESQA RAIVDQARNG ADFGKLAIAH SADQQALNGG QMGWGRIQEL PGIFAQALST AKKGDIVGPI RSGVGFHILK VNDLRGESKN ISVTEVHARH ILLKPSPIMT DEQARVKLEQ IAADIKSGKT TFAAAAKEFS QDPGSANQGG DLGWATPDIF DPAFRDALTR LNKGQMSAPV HSSFGWHLIE LLDTRNVDKT DAAQKDRAYR MLMNRKFSEE AASWMQEQRA SAYVKILSN
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Molecular Weight
47 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
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Protein Description
SurA is a periplasmic chaperone protein crucial for the proper folding and assembly of outer membrane proteins (OMPs) in Gram-negative bacteria. Given the unique structure of their outer membranes, which pose challenges for protein folding, the role of SurA becomes particularly significant. Research has highlighted its involvement in facilitating the maturation of OMPs, which are essential for various cellular functions, including nutrient uptake, signal transduction, and antibiotic resistance. Mutations or deficiencies in SurA can lead to a failure in OMP biogenesis, resulting in compromised bacterial viability and pathogenicity. This makes SurA an attractive target for antibiotic development; inhibiting its function could disrupt the assembly of OMPs, thereby rendering bacteria more susceptible to treatments. Moreover, SurA's potential as a therapeutic target extends beyond antibiotics, as understanding its mechanisms could pave the way for innovative strategies in combating bacterial infections, particularly those caused by multidrug-resistant strains. Consequently, research into SurA and its role in protein dynamics not only furthers our comprehension of bacterial physiology but also opens avenues for novel antimicrobial strategies. The exploration of SurA as a restructured protein is thus a pivotal area of study in microbiology and antibiotic resistance research.
