MuLV Core Antigen ELISA Kit

QuickTiter™ MuLV Core Antigen ELISA Kit
  • Measures the MuLV core protein (p30) as low as 300 pg/mL
  • Quantitation is performed on a standard microplate reader 
  • Recombinant MuLV p30 Standard included

 

Video: Color Development in an ELISA

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QuickTiter™ MuLV Core Antigen ELISA Kit
Catalog Number
VPK-156
Size
96 assays
Detection
Colorimetric
Manual/Data Sheet Download
SDS Download
Price
$795.00
Product Details

An anti-MuLV p30 monoclonal coating antibody is adsorbed onto a microtiter plate. MuLV core antigen (p30) present in the sample or standard binds to the antibodies adsorbed on the plate; an anti-MuLV p30 polyclonal antibody is added and binds to the antigen captured by the first antibody.

Following incubation and wash steps, a HRP-conjugated secondary antibody is added and binds to the anti-MuLV p30 polyclonal. Unbound HRP-conjugated secondary antibody is removed during the wash steps, and substrate solution reactive with HRP is added to the wells.

A colored product is formed in proportion to the amount of MuLV core antigen present in the sample. The reaction is terminated by addition of acid and absorbance is measured at 450 nm. A standard curve is prepared from recombinant MuLV p30 core antigen and sample concentration is then determined.

MuLV Core Antigen ELISA Standard Curve.

Purification of Recombinant MuLV p30 Protein. Lane 1: MW STDs; Lane 2: E.Coli Whole Lysate (-IPTG); Lane 3: E.Coli Whole Lysate (+IPTG); Lane 4: Crude Lysate; Lane 5: Lysate after Ni-NTA beads; Lane 6: Bead Wash; Lane 7: Elution Fraction for Recombinant MuLV p30 Standard.

Recent Product Citations
  1. Banskota, S. et al. (2022). Engineered virus-like particles for efficient in vivo delivery of therapeutic proteins. Cell. 185(2):250-265.e16. doi: 10.1016/j.cell.2021.12.021.
  2. Silva, R.J.S. et al. (2020). A Flow-Through Chromatographic Strategy for Hepatitis C Virus-Like Particles Purification. Processes. 8(1):85. doi: 10.3390/pr8010085.
  3. Silva, R.J.S. et al. (2020). Continuous Chromatography Purification of Virus-Based Biopharmaceuticals: A Shortcut Design Method. Methods Mol Biol. 2095:367-384. doi: 10.1007/978-1-0716-0191-4_21.
  4. Renner, T.M. et al. (2018). Full-Length Glycosylated Gag of Murine Leukemia Virus Can Associate with the Viral Envelope as a Type I Integral Membrane Protein. J Virol. 92(6). pii: e01530-17. doi: 10.1128/JVI.01530-17.
  5. Rosales Gerpe, M. C. et al. (2015). N-linked glycosylation protects gammaretroviruses against deamination by APOBEC3 proteins. J Virol. 89:2342-2357.
  6. Aydin, H. et al. (2014).  Crystal structures of beta-and gammaretrovirus fusion proteins reveal a role for electrostatic stapling in viral entry. J Virol. 88:143-153.
  7. Nityanandam, R. & Serra-Moreno, R.  (2014). BCA2/Rabring7 targets HIV-1 Gag for lysosomal degradation in a tetherin-independent manner. PLoS Pathog. 10:e1004151.
  8. Kirchmeier, M. et al. (2014). Enveloped Virus-Like Particle Expression of Human Cytomegalovirus Glycoprotein B Antigen Induces Antibodies with Potent and Broad Neutralizing Activity. Clin. Vaccine Immunol. 21:174-180.
  9. Belanger, K. et al. (2013). Binding of RNA by APOBEC3G Controls Deamination-Independent Restriction of Retroviruses. J. Exp. Biol. 216:2213-2220.