It's common to see multiple bands even when using affinity-purified antibody. This doesn't mean that there's a problem with the antibody’s specificity. Rather, this typically occurs for the following reasons: The native protein shows a different molecular weight than previously predicted. The antibody recognizes either cleaved fragments of the native protein at lower molecular weights, or post-translational modification or aggregated dimers/trimers of the native protein at higher molecular weights. The anti-peptide antibody recognizes a homologous protein in the sample that shares one or more epitopes with the peptide sequence. Unknown protein in lysate sample non-specifically binds to primary antibody or secondary antibody.
Articles in this section
- How do you validate the coverage of the HCP antibody? What is the sensitivity of HCP ELISA kit?
- Can you perform HCP antigen preparation? How do you validate?
- Do you have relevant experiences in ELISA kit development?
- Does GenScript have your own animal facility?
- How many positive hits could we guarantee in our beacon single b cell platform?
- Is GenScript able to keep the remaining positive B cells to backup?
- What are the benefits of express immunization compared to conventional immunization?
- What are the benefits of GenScript's MonoRab B cell cloning platform?
- How to decide what kind of immunogen format to use for antibody development?
- What kind of immunogens can we accept in upgraded TurboMab?