Code | CSB-RA192026A0HU |
Size | US$210 |
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Application | Recommended Dilution |
---|---|
WB | 1:500-1:5000 |
IHC | 1:50-1:200 |
IF | 1:20-1:200 |
B cells were generated by immunization of an animal with a synthetic peptide obtained from human USP7. The B cells were then fused with myeloma cells to form hybridomas. The variable light (VL) and variable heavy (VH) domains of the USP7 antibody-producing hybridomas' cDNA were sequenced, and this sequencing data was used to construct a vector for the recombinant generation. The USP7 monoclonal antibody gene-containing vector was transfected into cells, and the USP7 recombinant monoclonal antibody was collected and purified from the cell culture supernatant using affinity chromatography. The purified antibody was then tested for specificity in ELISA, WB, IHC, and IF applications, and this antibody was found to specifically detect human USP7 protein.
The USP7 protein is an enzyme that plays an important role in regulating protein turnover and stability within cells. As a deubiquitinase, USP7 can remove ubiquitin molecules from proteins that have been marked for degradation. In addition to its role in protein degradation, USP7 is involved in other cellular processes, including DNA repair, regulation of cell cycle progression, and modulation of signaling pathways. It has also been implicated in various disease states, including cancer and neurodegenerative disorders.
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