Western blot antibodies
Western blot is a commonly used technique designed to separate and identify proteins from tissue or cell extracts by molecular weight. Western blots can be performed on whole cell lysates to determine total protein expression, or on subcellular fractions in order to determine in which cellular location the protein is expressed (eg lysate, nucleus, chromatin-bound, mitochondrial).
To be confident in your results, you need to be confident in your antibodies. Our portfolio includes a broad range of antibodies validated in western blot, including with knock-outs where possible.
Loading controls
Loading controls are needed for Western blot to make sure loading across samples is even and to ensure any changes in target protein expression you see across different sample types are genuine. This is especially important when looking at negative samples such as knock-out cell lines or cells treated with siRNA to knockdown gene expression. A good loading control gives you confidence that your negative sample is a true negative. This ensures your experimental findings will be to the standard required for publication in peer-reviewed journals, and your work is reproducible by other scientists.
A good loading control is expressed equally in all your samples, so housekeeping genes are often chosen. Some examples for cell lysates are beta-actin, alpha-tubulin and GAPDH. More specific loading controls may also be chosen depending on your experiment, eg nucleophosmin as a nuclear loading control, or Histone H3 for chromatin samples.
Anti-tag antibodies
Anti-tag antibodies are highly specific antibodies that provide a method to localize proteins that have been fused with a tag.
Tags can help you purify proteins, and are also used when studying a novel protein for which antibodies are not yet commonly available. Common tags include FLAG, GST, 6xHis, myc, and many more. We provide a wide range of anti-tag antibodies validated in a wide range of applications, including western blot.
Phospho-specific antibodies
Phosphorylation is a fundamental regulatory mechanism in biology, controlling protein activity, stability, and interactions across nearly every cellular pathway. To study these dynamic changes, researchers rely on phospho-specific antibodies, which are engineered to recognize proteins only when phosphorylated at precise amino acid residues. By distinguishing between active and inactive protein states, these antibodies can be used to study signal transduction pathways, enabling scientists to track pathway activation, measure cellular responses, and uncover mechanisms underlying health and disease.
Our range of antibodies targeting PTMs has been characterized with various techniques, including peptide array, dot blot and ELISA, to confirm both specificity and minimal cross-reactivity with unmodified or related modifications.