Anti-Human HIF-1alpha Recombinant Antibody (6A9) (CAT#: TAB-080CT)

Figure 1 Validation of monoclonal antibodies against hydroxylated proline 402 or 564 containing peptides of the HIF-1α ODD region.

Clone 6A9 was specific for hydroxylated proline 564.

Rolfo, A., Many, A., Racano, A., Tal, R., Tagliaferro, A., Ietta, F., ... & Caniggia, I. (2010). Abnormalities in oxygen sensing define early and late onset preeclampsia as distinct pathologies. PloS one, 5(10), e13288.

Figure 2 HIF-1α hydroxylation during normal placentation and in preeclampsia.

Representative immunoblots showing reduced HIF-1a hydroxylation at P564 (6A9) in preeclamptic placentae (E-PE, n = 12) relative to preterm controls (PTC n = 12).

Rolfo, A., Many, A., Racano, A., Tal, R., Tagliaferro, A., Ietta, F., ... & Caniggia, I. (2010). Abnormalities in oxygen sensing define early and late onset preeclampsia as distinct pathologies. PloS one, 5(10), e13288.

Figure 3 SUMO2/3-mediated SUMOylation results in decreased HIF1A stability.

Western blot showing reduced HIF1A hydroxylation at P564 (Clone 6A9) in JEG3 cells exposed to 3% O2 relative to 21% O2 standard conditions.

Bhattacharjee, J., Alahari, S., Sallais, J., Tagliaferro, A., Post, M., & Caniggia, I. (2016). Dynamic regulation of HIF1Α stability by SUMO2/3 and SENP3 in the human placenta. Placenta, 40, 8-17.

Figure 1 Analysis of mAb reactivity with hCD200R by orientation via antibody immobilization.

Shows the mean fluorescence intensity ± SEM for each spot of all replicates. Serial two-fold dilutions of capture human CD200R mAb OX108, DX136 and DX147 and control rat CD4 mAb OX68 were arrayed onto epoxy-coated microscope slides. Each mAb dilution series was arrayed in quadruplicate of 2 rows of 6 spots, ranging in concentration from 80 μg ml-1 (first spot) to 0.16 μg/ml (spot 10), with control spotting buffer containing 0.5 mg/ml BSA in the last two spots.

LETARTE, Michelle, et al. Analysis of leukocyte membrane protein interactions using protein microarrays. BMC biochemistry, 2005, 6.1: 2.