Purified Membrane Proteins

Multidrug efflux pump subunit AcrB - Transporter

CALIXAR’s Acridine resistance protein B (Multidrug efflux pump subunit AcrB) is a bacterial multidrug exporter that aids in the identification, development, refinement, and validation of new molecules and therapeutic antibodies. Our AcrB transporters are exemplary for therapeutic indications such as bacterial resistance to antibiotics.

Acridine resistance protein B is a powerful therapeutic target especially in the treatment of such conditions as bacterial resistance to antibiotics.

Purchase Multidrug efflux pump subunit AcrB

Acridine resistance protein B is a bacterial multidrug exporter. This membrane protein is a good target for indications of bacterial resistance. Protein has a C-terminal 6X His tag.

Target name: Multidrug efflux pump subunit AcrB (Acridine resistance protein B)

Gene: acrB

Uniprot Accession: P31224 

Origin: Escherichia coli (strain K12)

Class: Multidrug efflux pump

Sequence: Full-length, wildtype sequence, with a C-terminus, 6xHis-tag

Affinity Tag: His-tag (C-terminal)

Catalogue number: PP4

Theor. MW: 114.6 kDa

Shipment temperature: Dry Ice

Storage conditions: Store at -80°C

Expression system: Escherichia coli (BL21C43)

Purity: >95%

Purification: Immobilized Metal Affinity Chromatography

Activity: Confirmed by ligand binding

Concentration: Up to 5mg/ml

Sample buffer: 25mM Na2HPO4 100mM NaCl, 0.01% DDM (also available in optimized thermostable composition)

Available quantity: From 10µg up to mg scale

From €200.00 (10µg)

Ships in 7 business days

First in market

CALIXAR is the first to produce native, wild-type, unmutated and untruncated targets.

Better discovery

Develop reliable and effective drugs and antibodies as they are not locked in any specific conformation.

Why choose us?

Multidrug efflux pump subunit AcrB: We employ a novel & custom-built method to give us an advantage

CALIXAR’s Acridine resistance protein B enables reliable fragment-based drug design (FBDD), structure-based drug discovery (SBDD) and antibody discovery against this specific target.

Unlike CALIXAR’s AcrB transporters, other alternative strategies result in an Acridine resistance protein B that becomes mutated and truncated.

As with all transporters, Acridine resistance protein B is a delicate targets, difficult to manufacture natively without particular know-how. Traditionally, Acridine resistance protein B was frequently developed in a solution that inherently cannot be pure, neither native (truncated, mutated), and consequently very unstable.

With CALIXAR’s expertise, we are capable of producing Multidrug efflux pump subunit AcrB that preserve the native structure and function of the target. Our AcrB transporter is pure, native, unaltered and stable. This is unparalleled on the market and at the vanguard of Membrane Protein technology.

See the application note related to the AcrB optimise thermostable composition: “A collaborative gene-to-structure workflow using cryoEM”

CALIXAR’S Acridine resistance protein B is unaltered, unmutated and untruncated targets that sustain their structural and functional integrity. This membrane protein transporter is purified and stabilized full length and wild-type (native), produced in a prokaryotic arrangement (E.coli).

Calixar’s Acridine resistance protein B is used for (bio)drug discovery and is adapted for application in Pharmaceutical, biotechnology companies, as well as for academic teams that are involved in the life science disciplines.

  • Antibodies (including nanobodies, scaffold proteins, aptamers)
  • Small molecules
  • 3D Structures (classical X-ray or XFEL, Cryo-EM, NMR)
  • Drug discovery (Screening: HTS, FBDD, SBDD; Hit and lead validation)
  • Antibody discovery (Immunization and display technologies)
  • Clinical stage (drug validation on reliable native AcrB)​

Multidrug efflux pump subunit AcrB references

Proc Natl Acad Sci USA

Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop.

Eicher T. et al. 2012 

Acta Crystallogr Biol Crystallogr

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein.

Pos KM. et al. 2002