Recombinant E.Coli Chaperone Sura (SURA) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09621P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant E.Coli Chaperone Sura (SURA) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09621P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant E.Coli Chaperone Sura (SURA) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P0ABZ6
Target Symbol SURA
Synonyms 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)
Expression System Yeast
Tag N-6His
Target Protein Sequence APQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAAQARQQLPDDATLRHQIMERLIMDQIILQMGQKMGVKISDEQLDQAIANIAKQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVESLAQQVGNQNDASTELNLSHILIPLPENPTSDQVNEAESQARAIVDQARNGADFGKLAIAHSADQQALNGGQMGWGRIQELPGIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESKNISVTEVHARHILLKPSPIMTDEQARVKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALTRLNKGQMSAPVHSSFGWHLIELLDTRNVDKTDAAQKDRAYRMLMNRKFSEEAASWMQEQRASAYVKILSN
Expression Range 21-428aa
Protein Length Full Length of Mature Protein
Mol. Weight 47.1kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

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

Gene Functions References

  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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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