Cat. #152161
Anti-XPC [RW028]
Cat. #: 152161
Sub-type: Primary antibody
Unit size: 100 ug
Availability: 10-12 weeks
Target: Xeroderma Pigmentosum Group C (XPC)
Class: Polyclonal
Application: IF ; IF ; WB
Reactivity: Human
Host: Rabbit
£300.00
This fee is applicable only for non-profit organisations. If you are a for-profit organisation or a researcher working on commercially-sponsored academic research, you will need to contact our licensing team for a commercial use license.
Contributor
Inventor: Dawn Batty ; Rick Wood
Institute: Cancer Research UK, London Research Institute: Lincoln's Inn Fields
Tool Details
*FOR RESEARCH USE ONLY (for other uses, please contact the licensing team)
- Name: Anti-XPC [RW028]
- Research fields: Genetics
- Clone: RW028
- Tool sub type: Primary antibody
- Class: Polyclonal
- Conjugation: Unconjugated
- Reactivity: Human
- Host: Rabbit
- Application: IF ; IF ; WB
- Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.
- Immunogen: 96-299 of human XPC protein
- Recommended controls: HeLa cell lysate
Target Details
- Target: Xeroderma Pigmentosum Group C (XPC)
- Tissue cell line specificity: HeLa cell lysate
- Target background: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.
Applications
- Application: IF ; IF ; WB
Handling
- Format: Liquid
- Unit size: 100 ug
- Shipping conditions: Dry ice
References
- HCMV-infected cells maintain efficient nucleotide excision repair of the viral genome while abrogating repair of the host genome.
- O'Dowd et al. 2012. PLoS Pathog. 8(11):e1003038. PMID: 23209410.
- O'Dowd et al. 2012. PLoS Pathog. 8(11):e1003038. PMID: 23209410.
- Lange et al. 2009. DNA Repair (Amst). 8(7):865-72. PMID: 19446504.
- Human HMGB1 directly facilitates interactions between nucleotide excision repair proteins on triplex-directed psoralen interstrand crosslinks.
- Louat et al. 2004. FEBS Lett. 574(1-3):121-5. PMID: 15358551.
- Atypical protein kinase C stimulates nucleotide excision repair activity.
- Arajo et al. 2001. Mol Cell Biol. 21(7):2281-91. PMID: 11259578.
- Strong Fn interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome.
- Batty et al. 2000. J Mol Biol. 300(2):275-90. PMID: 10873465.
- Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites.
- Kberle et al. 1999. Curr Biol. 9(5):273-6. PMID: 10074455.
- Defective repair of cisplatin-induced DNA damage caused by reduced XPA protein in testicular germ cell tumours.
