The human SUB1 protein is composed of 127 amino acids and has a molecular weight of approximately 16.5 kDa . It is typically expressed in E. coli and purified using conventional chromatography techniques . The recombinant form of this protein often includes an N-terminal His-tag to facilitate purification and detection .
SUB1 functions as a transcriptional coactivator, meaning it enhances the transcription of specific genes by interacting with other transcription factors and components of the transcriptional machinery. It interacts with the activation domain of transcription factor IIA (TFIIA) and TATA-binding protein (TBP)-associated factors (TAFs) to directly bind to double-stranded DNA . Depending on the presence or absence of these transcription factors and holoenzyme components, SUB1 can induce both activation and repression of RNA polymerase II basal transcription .
Recombinant human SUB1 is widely used in research to study its role in transcription regulation and its interactions with other proteins. It is also used in various assays, including ELISA, Western Blot, and protein arrays . However, it is important to note that some recombinant forms of SUB1 may not be active and should not be used for experiments requiring activity .