Recombinant Escherichia coli Chaperone surA (surA)

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Code CSB-EP359693ENV
Size US$388
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
surA
Uniprot No.
Research Area
Others
Alternative Names
surA; b0053; JW0052; Chaperone SurA; Peptidyl-prolyl cis-trans isomerase SurA; PPIase SurA; EC 5.2.1.8; Rotamase SurA; Survival protein A
Species
Escherichia coli (strain K12)
Source
E.coli
Expression Region
21-428aa
Target Protein Sequence
APQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAAQARQQLPDDATLRHQIMERLIMDQIILQMGQKMGVKISDEQLDQAIANIAKQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVESLAQQVGNQNDASTELNLSHILIPLPENPTSDQVNEAESQARAIVDQARNGADFGKLAIAHSADQQALNGGQMGWGRIQELPGIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESKNISVTEVHARHILLKPSPIMTDEQARVKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALTRLNKGQMSAPVHSSFGWHLIELLDTRNVDKTDAAQKDRAYRMLMNRKFSEEAASWMQEQRASAYVKILSN
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
61.1kDa
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
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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

Amino acids 21-428 form the expressed segment for recombinant Escherichia coli (strain K12) surA. This surA protein is theoretically predicted to have a molecular weight of 61.1 kDa. This protein is generated in a e.coli-based system. The N-terminal 6xHis-SUMO tag was smoothly integrated into the coding gene of surA, which enables a simple process of detecting and purifying the surA recombinant protein in the following steps.

The SurA protein in Escherichia coli is a periplasmic chaperone that plays a critical role in the proper folding and stabilization of outer membrane proteins (OMPs). The periplasmic space is a challenging environment for protein folding due to oxidative conditions and the absence of ATP-driven folding machinery. SurA assists in the correct folding of OMPs, preventing their aggregation and facilitating their subsequent integration into the outer membrane. It acts at various stages of OMP biogenesis, aiding in the maintenance of their structural integrity. Additionally, SurA is involved in the quality control of OMPs, targeting misfolded proteins for degradation. This chaperone is crucial for bacterial fitness, membrane integrity, and resistance to environmental stresses. Research on SurA is vital for understanding the intricate mechanisms underlying bacterial protein folding and outer membrane biogenesis, providing potential targets for the development of antibacterial agents and drugs combating bacterial infections.

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Target Background

Function
Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.
Gene References into Functions
  1. SurA cycles between distinct conformational and functional states during the bacterial outer membrane assembly process. PMID: 26728192
  2. These findings suggest an autoinhibitory mechanism for regulation of SurA chaperone activity through interdomain interactions involving a proline isomerase domain. PMID: 23943764
  3. mutational studies on SurA to identify residues that are critical for function were conducted; formation of disulfide bond in mutants has no observable detrimental effect on protein activity, indicating SurA does not undergo large-scale conformational change while performing its function PMID: 23275244
  4. The results indicate that FimD usher follows the SurA-BamB pathway for its assembly. PMID: 21784935
  5. Unfolded protein molecules initially form a highly dynamic complex with the chaperone domain of SlyD, and they are then transferred to the prolyl isomerase domain. PMID: 21147124
  6. The biological importance of SurA was further substantiated by the finding that SurA also affects pathogenicity, being required for full virulence of uropathogenic Escherichia coli. PMID: 20447864
  7. Data found that the periplasmic disulfide isomerase DsbC cooperates with SurA and the thiol oxidase DsbA in the folding of the essential beta-barrel protein LptD. PMID: 20615876
  8. SurA was shown to be involved in the assembly of pili PMID: 16267292
  9. SurA therefore asserts a recognition preference for aromatic amino acids in a variety of sequence configurations by adopting alternative tertiary and quaternary structures to bind peptides in different conformations PMID: 17825319
  10. SurA is the primary chaperone responsible for the periplasmic transit of the bulk mass of OMPs to the YaeT complex. PMID: 17908933
  11. data support role for SurA in assembly of LptD & suggest that LptD is a true SurA substrate; based on results, we propose a revised model in which only a subset of outer membrane (OM) proteins depends on SurA for proper folding & insertion in the OM PMID: 19343722

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Subcellular Location
Periplasm. Note=Is capable of associating with the outer membrane.
Database Links
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