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 DNA damage-binding protein from HeLa cells is associated with polypeptides of relative mass 124,000 (DDB1) and 41,000 (DDB2) as determined by SDS-polyacrylamide gels. To test whether the DNA-repair defect in the subset of XPE patients that lack DNA damage-binding activity is caused by a defect in DDB, Keeney et al. (1994) injected purified human DDB protein into XPE cells.
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Protein Aliases: damage specific DNA binding protein 1; damage-specific DNA binding protein 1, 127kDa; Damage-specific DNA-binding protein 1; damage-specific DNA-binding protein, DNA repair; damaged-DNA recognition protein 1; DDB p127 subunit; DDBa; DNA damage-binding protein 1; DNA damage-binding protein a; DNA repair protein; HBV X-associated protein 1; UV-damaged DNA-binding factor; UV-damaged DNA-binding protein 1; UV-DDB 1; XAP-1; Xeroderma pigmentosum group E-complementing protein; XPCe; XPE-BF; XPE-binding factor
Gene Aliases: 127kDa; AA408517; DDB1; DDBA; p127-Ddb1; UV-DDB1; XAP1; XPCE; XPE; XPE-BF