Anti-CDC45L antibody [EPR5759]

• IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-CDC45L antibody [EPR5759] (AB126762)

ab126762, at 1/100 dilution, staining CDC45L in paraffin-embedded Human colon tissue by Immunohistochemistry.

Perform heat mediated antigen retrieval before commencing with IHC staining protocol.

• ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-CDC45L antibody [EPR5759] (AB126762)

ICC/IF image of ab126762 stained HeLa cells. The cells were 100% methanol fixed (5 min) and then incubated in 1%BSA / 10% normal goat serum / 0.3M glycine in 0.1% PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated with the antibody ab126762 at 1/100 dilution overnight at +4°C. The secondary antibody (pseudo-colored green) was Alexa Fluor® 488 goat anti- rabbit (ab150081) IgG (H+L) preadsorbed, used at a 1/1000 dilution for 1h. Alexa Fluor® 594 WGA was used to label plasma membranes (pseudo-colored red) at a 1/200 dilution for 1h at room temperature. DAPI was used to stain the cell nuclei (pseudo-colored blue) at a concentration of 1.43μM for 1hour at room temperature.

• WB

Unknown

Western blot - Anti-CDC45L antibody [EPR5759] (AB126762)

All lanes:

Western blot - Anti-CDC45L antibody [EPR5759] (ab126762) at 1/1000 dilution

Lane 1:

293T cell lysate at 10 µg

Lane 2:

Jurkat cell lysate at 10 µg

Lane 3:

K562 cell lysate at 10 µg

Secondary

All lanes:

HRP-conjugated goat anti-rabbit at 1/2000 dilution

Predicted band size: 66 kDa

false

• OI-RD Scanning

Unknown

OI-RD Scanning - Anti-CDC45L antibody [EPR5759] (AB126762)

We have systematically measured KD (the equilibrium dissociation constant between the antibody and its antigen), of more than 840 recombinant antibodies to assess not only their individual KD values but also to see the average affinity of antibody. Based on the comparison with published literature values for mouse monoclonal antibodies, Recombinant antibodies appear to be on average 1-2 order of magnitude higher affinity.