Name: Recombinant Escherichia coli Chaperone surA(surA)
Brand: CUSABIO
SKU: CSB-EP359693ENV

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 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	Protein FAQs
Storage Condition	Store at -20°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	Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
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.

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Target Data

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 Show More Hide All
Subcellular Location	Periplasm
Database Links	KEGG: ecj:JW0052 STRING: 316385.ECDH10B_0054

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Check Code：

Code	CSB-EP359693ENV
Size	US$2466
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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Target Data

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