Product Details

Full Product Name Rabbit anti-Escherichia coli (strain K12) fimH Polyclonal antibody
Uniprot No. P08191
Target Names fimH
Alternative Names fimH antibody; b4320 antibody; JW4283Type 1 fimbrin D-mannose specific adhesin antibody; Protein FimH antibody
Raised in Rabbit
Species Reactivity Escherichia coli
Immunogen Recombinant Escherichia coli Type 1 fimbrin D-mannose specific adhesin (fimH) (22-300AA)
Immunogen Species Escherichia coli (strain K12)
Conjugate Non-conjugated
Clonality Polyclonal
Isotype IgG
Purification Method Protein A/G
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, WB (ensure identification of antigen)
Protocols ELISA Protocol
Troubleshooting and FAQs Antibody FAQs
Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables ① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee ① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time Made-to-order (12-14 weeks)
FimH-based display of functional eukaryotic proteins

FimH-based display of functional eukaryotic proteins

Abstract

The demand for recombinant proteins for analytic and therapeutic purposes is increasing; however, most currently used bacterial production systems accumulate the recombinant proteins in the intracellular space, which requires denaturating procedures for harvesting and functional testing.

We here present a novel FimH-based expression system that enables display of fully functional eukaryotic proteins while preventing technical difficulties in translocating, folding, stabilizing and isolating the displayed proteins. As examples, Gaussia Luciferase (GLuc), epidermal growth factor (EGF), transforming growth factor-α (TGF-α) and epiregulin (EPRG) were expressed as FimH fusion proteins on the surface of E. coli bacteria.

The fusion proteins were functionally active and could be released from the bacterial surface by specific proteolytic cleavage into the culture supernatant allowing harvesting of the produced proteins. EGFR ligands, produced as FimH fusion proteins and released by proteolytic cleavage, bound to the EGF receptor (EGFR) on cancer cells inducing EGFR phosphorylation.

In another application of the technology, GLuc-FimH expressed on the surface of bacteria was used to track tumor-infiltrating bacteria by bioluminescence imaging upon application to mice, thereby visualizing the colonization of transplanted tumors. The examples indicate that the FimH-fusion protein technology can be used in various applications that require functionally active proteins to be displayed on bacterial surfaces or released into the culture supernatant.

Introduction

Bacterial surface display of recombinant proteins has become an attractive strategy for a broad range of applications such as production of bioadsorbents, generation of cellular biosensors, development of novel vaccine platforms, screening of antibody libraries and whole-cell biocatalysis. Generally, the procedure requires the fusion of the protein-of-interest (POI) to a bacterial surface protein to display the POI on the surface of the genetically modified bacteria. Several surface-anchoring motifs like LPP-OmpA, LamB, PhoE, ice nucleation protein (INP) and auto-transporter are employed as carrier proteins for crossing the bacteria membrane.

Despite the successful approaches, several problems remain to be solved, including the substantially reduced functional activity of the displayed proteins. Compared with their soluble form, surface-anchored β-lactamase fused to the translation unit (TU) of an auto-transporter shows substantially reduced catalytic activities. A similar experience was made when displaying sorbitol dehydrogenase.

A major problem in the use of auto-transporters arises from the tertiary structure of the passenger domains and the size of the central cavity that permits translocating only small proteins. It seems not only to be a matter of size since even the 62 amino acids protein aprotinin is not efficiently translocated through the outer membrane. Translocation by auto-transporters is very sensitive to structure of the passenger proteins that consist of a β-strands backbone with at least 300 amino acids thereby substantially limiting the applicability to variety of potential cargos.

 

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  • 100ug
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