Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

surA

Uniprot No.

P0ABZ6

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 may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

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.

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

Protein 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.

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

SurA cycles between distinct conformational and functional states during the bacterial outer membrane assembly process. PMID: 26728192
These findings suggest an autoinhibitory mechanism for regulation of SurA chaperone activity through interdomain interactions involving a proline isomerase domain. PMID: 23943764
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
The results indicate that FimD usher follows the SurA-BamB pathway for its assembly. PMID: 21784935
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
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
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
SurA was shown to be involved in the assembly of pili PMID: 16267292
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
SurA is the primary chaperone responsible for the periplasmic transit of the bulk mass of OMPs to the YaeT complex. PMID: 17908933
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

KEGG: ecj:JW0052

STRING: 316385.ECDH10B_0054

Code	CSB-EP359693ENV
Abbreviation	Recombinant E.coli surA protein
MSDS	MSDS Datasheet
Size	US$388
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Escherichia coli Chaperone surA (surA)

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