Recombinant Escherichia coli Multidrug efflux pump subunit AcrB (acrB), partial, Escherichia coli (strain K12), E.coli, C-terminal 6xHis-tagged, 39.8kDa, purity >95% as determined by SDS-PAGE.

Recombinant Escherichia coli Multidrug efflux pump subunit AcrB (acrB), partial

Recombinant Escherichia coli Multidrug efflux pump subunit AcrB (acrB), partial — (Microbial infection) Involved in contact-dependent growth inhibition (CDI), acts downstream of BamA, the receptor for CDI. Purity >95%.

SKU: BCRECP-002010 Category:
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Product Specifications

Product SkuBCRECP-002010
Product DescriptionRecombinant Escherichia coli Multidrug efflux pump subunit AcrB (acrB) Protein is expressed from E.coli with C-terminal 6xHis-tagged. It contains 29-336aa. [Accession | P31224].
Uniprot No.P31224
Gene NamesacrB
PurityGreater than 95% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region29-336aa
SpeciesEscherichia coli (strain K12)
Tag InfoC-terminal 6xHis-tagged
Molecular weight39.8kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasOthers

Function

(Microbial infection) Involved in contact-dependent growth inhibition (CDI), acts downstream of BamA, the receptor for CDI. Its role in CDI is independent of the AcrAB-TolC efflux pump complex.

Biological Context

Subcellular Location: Cell inner membrane (Multi-pass membrane protein)

Product Specifications

Recombinant Escherichia coli Multidrug efflux pump subunit AcrB (acrB), partial is a recombinant protein from Escherichia coli (strain K12), expressed in E.coli, covering amino acids 29-336aa, with C-terminal 6xHis-tagged tag, molecular weight 39.8kDa, purity Greater than 95% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

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Protein Biology

Function

(Microbial infection) Involved in contact-dependent growth inhibition (CDI), acts downstream of BamA, the receptor for CDI (PubMed:18761695). Its role in CDI is independent of the AcrAB-TolC efflux pump complex (PubMed:18761695)

Subcellular Location

Cell inner membrane (Multi-pass membrane protein)

Subunit

Homotrimer, with large porter and funnel domains (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:19023693, PubMed:28355133, PubMed:31201302). Extends into the periplasm, where the trimer interacts with AcrA and TolC (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:19023693, PubMed:28355133, PubMed:31201302). Component of the AcrAB-TolC multidrug efflux complex, composed of six AcrA subunits forming a hexameric tube, binding to an AcrB trimer, which interact with the trimeric TolC outer membrane channel protein (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:24747401, PubMed:28355133, PubMed:31201302). TolC is thought to not contact AcrB stably; instead, AcrA joins AcrB and TolC by forming a funnel-like hexamer anchored to the inner membrane (PubMed:15228545, PubMed:24747401, PubMed:28355133, PubMed:31201302). AcrA may initially form a hexameric ring complex with AcrB, in a bipartite complex, which may be stabilized by binding of AcrA with the peptidoglycan layer, prior to forming the full AcrAB-TolC efflux pump complex (PubMed:22308040, PubMed:28355133, PubMed:31201302). Contact between AcrA-AcrB and TolC may prompt a conformational change in the presence of substrate, allowing the periplasmic gate to open (PubMed:28355133, PubMed:31201302). Each AcrB protomer adopts one of three different conformational states, probably cycling between access, binding, and extrusion of substrate (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17015667, PubMed:17194213, PubMed:19023693, PubMed:19425588, PubMed:25248080, PubMed:28355133, PubMed:31201302). Several charged residues in the transmembrane region of AcrB may constitute a proton translocation pathway, playing a key energetic role in the conformational changes driving efflux (PubMed:17015667, PubMed:19425588, PubMed:25248080). It is thought that, under high intracellular substrate concentration, AcrB ejects substrate into the tunnel formed by AcrA-TolC; as the substrate level declines, conformational changes in AcrB cause efflux to reduce and stop and the whole complex shifts to the closed state (PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:25248080, PubMed:28355133, PubMed:31201302). Interacts with AcrZ; the interaction is direct (PubMed:23010927, PubMed:32348749). Component of the AcrABZ-TolC efflux pump complex, composed of six AcrA subunits forming a hexameric tube binding to an AcrB trimer, which interact with the trimeric TolC outer membrane channel protein; AcrZ interacts directly with AcrB, probably in 1:1 stoichiometry (PubMed:23010927, PubMed:24747401, PubMed:28355133, PubMed:32348749)

Gene: acrB  |  Organism: Escherichia coli (strain K12)  |  Synonyms: AcrAB-TolC multidrug efflux pump subunit AcrB; Acridine resistance protein B
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