Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human U2AF35 aa 150 to the C-terminus (Cysteine residue). The exact sequence is proprietary. Database link: Q01081
HeLa, 293T, Ramos and NIH 3T3 cell lysates; HeLa cells; Human endometrial carcinoma and Human pancreas tissues.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMab® patents
We are constantly working hard to ensure we provide our customers with best in class antibodies. As a result of this work we are pleased to now offer this antibody in purified format. We are in the process of updating our datasheets. The purified format is designated 'PUR' on our product labels. If you have any questions regarding this update, please contact our Scientific Support team.
This product is a recombinant rabbit monoclonal antibody.
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000 - 1/5000. Detects a band of approximately 35 kDa (predicted molecular weight: 28 kDa).
1/50 - 1/100. Perform heat mediated antigen retrieval before commencing with IHC staining protocol.
1/50 - 1/100.
1/10 - 1/100.
Is unsuitable for Flow Cyt.
Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron.
Belongs to the splicing factor SR family. Contains 2 C3H1-type zinc fingers. Contains 1 RRM (RNA recognition motif) domain.
The C-terminal SR-rich domain is required for interactions with SR proteins and the splicing regulators TRA and TRA2, and the N-terminal domain is required for formation of the U2AF1/U2AF2 heterodimer.
Phosphorylated upon DNA damage, probably by ATM or ATR.