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Western blot analysis of XPA. A Jurkat cell lysate (Human T-cell leukemia; ATCC TIB-152) was probed with the mouse anti-human XPA antibody (clone 12F5) at a concentration of 1 µg/ml (lane 1), 0.5 µg/ml (lane 2), or 0.25 µg/ml (lane 3).


BD Pharmingen™ Purified Mouse Anti-Human XPA

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Recommended Assay Procedures
Recommended Assay Procedure:
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
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Nucleotide excision repair (NER) is a major pathway by which cells remove UV and chemically induced damage from DNA. The biochemistry of NER is complex and includes recognition of the damaged DNA, formation of incisions ~26-29 nucleotides apart on each side of the damaged DNA, excision of an oligonucleotide carrying the damaged DNA, and synthesis of a repair patch using the opposite DNA strand as a template. The xeroderma pigmentosum (XP) factors are the best characterized components in the NER pathway. They are termed XP-A to -G and are thought to be required for the first steps of the nucleotide excision repair process. XPA is a DNA damage-binding protein and XPC is a single stranded DNA-binding protein. XPB and XPD are DNA helicases that are components of the transcription factor TFIIH. The TFIIH complex is thought to be involved in transcription and NER. XPF is an endonuclease that binds to ERCC1 (for excision repair cross-complementing) and the ERCC1-XPF complex makes the incision 5' to the DNA damage. ERCC1 migrates at a molecular weight of ~36 kDa in SDS-PAGE. XPG is an endonuclease that makes the 3' incision. XPA has been reported to migrate at a molecular weight of 34-40 kDa in SDS-PAGE.
Development References (2)
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Aboussekhra A, Biggerstaff M, Shivji MK, et al. Mammalian DNA nucleotide excision repair reconstituted with purified protein components. Cell. 1995; 80(6):859-868. (Biology). View Reference
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Evans E, Fellows J, Coffer A, Wood RD. Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J. 1997; 16(3):625-638. (Biology). View Reference
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