surA Antibody, Biotin conjugated

Code CSB-PA359693HD01ENV
Size US$166
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Product Details

Full Product Name
Rabbit anti-Escherichia coli (strain K12) surA Polyclonal antibody
Uniprot No.
Target Names
surA
Alternative Names
surA antibody; b0053 antibody; JW0052 antibody; Chaperone SurA antibody; Peptidyl-prolyl cis-trans isomerase SurA antibody; PPIase SurA antibody; EC 5.2.1.8 antibody; Rotamase SurA antibody; Survival protein A antibody
Raised in
Rabbit
Species Reactivity
Escherichia coli
Immunogen
Recombinant Escherichia coli Chaperone SurA protein (21-428AA)
Immunogen Species
Escherichia coli (strain K12)
Conjugate
Biotin
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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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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