Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.
The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.
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Protein Aliases: Heat shock 70 kDa protein 2; heat shock 70kD protein 2; heat shock 70kDa protein 2; Heat shock protein 70.2; heat shock protein alpha 2; heat shock protein, 70 kDa 2; Heat shock-related 70 kDa protein 2; HST; Testis-specific heat shock protein-related; testis-specific heat shock protein-related gene hst70
Gene Aliases: 70kDa; Hcp70.2; HSP70-2; HSP70-3; HSP70.2; HSP70A2; HSPA2; Hspt70; Hst70