Recombinant Anti-GABRA5 Vesicular Antibody, EV Displayed (VS-0425-YC394)

CAT#: VS-0425-YC394

The Recombinant Anti-GABRA5 Vesicular Antibody, EV Displayed (VS-0425-YC394) is an antibody-displaying extracellular vesicle (Ab-EV). The product combines the benefits of both extracellular vesicle (EV) and antibody (Ab) which can guide the decorated EVs to GABRA5-expressed cells or tissues. The GABRA5 is a subunit of the GABA-A receptor involved in inhibitory neurotransmission, with its chlorinated conductance modulated by agents binding to the GABA-A receptor.

Gene Expression
Figure 1 IF staining of human cell line A549 Figure 2 RNA cell line category: Group enriched (A549, HAP1, NTERA-2, U-2 OS)

Recombinant Antibody

  • Application
  • ELISA, FC, Cell-uptake
  • Product Type
  • Ab-Fc-EVs
  • Antibody Quantification (Ab/EV)
  • ~100 Ab/EV
  • Target
  • GABRA5
  • Host Animal
  • Human
  • Antibody Isotype
  • IgG1
  • Species Reactivity
  • Human
  • Expression Cell
  • Mammalian cell

Engineered EVs

  • EV-sorting domain
  • CD63
  • Fc-binding domain
  • z domain
  • EV Size
  • 30~150 nm
  • Producing Cell
  • HEK293F
  • Isolation Method
  • Gradient centrifugation
  • Purification
  • qEV size exclusion chromatography
  • Binding Affinity
  • Kd = 0.85 µg/mL
  • Concentration
  • 1 x 10¹⁰
  • Size
  • 1 mL
  • Buffer
  • PBS
  • Storage
  • Store at -80°C for 12 months

Target

  • Full Name
  • Gamma-aminobutyric acid type A receptor subunit alpha5
  • Biological Process
  • Ion transport, Transport
  • Molecular Function
  • Chloride channel, Ion channel, Ligand-gated ion channel, Receptor
  • Cellular Localization
  • Plasma membrane, Nucleoplasm, Actin filaments, Cytosol
  • Introduction
  • GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. Transcript variants utilizing three different alternative non-coding first exons have been described.
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