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AB189317

Anti-XPG antibody

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(1 Publication)

Rabbit Polyclonal XPG antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human ERCC5 aa 100-200.

View Alternative Names

ERCM2, XPG, XPGC, ERCC5, DNA excision repair protein ERCC-5, DNA repair protein complementing XP-G cells, Xeroderma pigmentosum group G-complementing protein

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-XPG antibody (AB189317)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-XPG antibody (AB189317)

Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human prostate tissue labeling XPG with ab189317 at 20 μg/ml.

Western blot - Anti-XPG antibody (AB189317)
  • WB

Supplier Data

Western blot - Anti-XPG antibody (AB189317)

All lanes:

Western blot - Anti-XPG antibody (ab189317) at 1/500 dilution

Lane 1:

COLO cell extract

Lane 2:

COLO cell extract with immunizing peptide

Predicted band size: 133 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human ERCC5 aa 100-200. The exact immunogen used to generate this antibody is proprietary information.

P28715

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

XPG also known as ERCC5 is an important player in DNA repair mechanisms specifically involved in nucleotide excision repair (NER). It is an endonuclease meaning it cuts DNA at specific sites to help remove damaged DNA. XPG is known to have a molecular weight of approximately 133 kDa. The protein is expressed in a wide array of human tissues making its function important in maintaining genomic stability across different cell types.
Biological function summary

XPG contributes to the repair of bulky DNA lesions such as those caused by UV light. This protein functions as part of the NER complex where it performs a critical incision on the DNA strand undergoing repair. In this complex XPG works alongside other proteins like XPA and RPA coordinating the removal and repair of damaged nucleotides. Its activity is essential in correcting DNA damage and maintaining cellular health protecting against mutations that might occur from environmental damage.

Pathways

XPG plays integral roles in the nucleotide excision repair pathway. This pathway is significant for correcting DNA damage induced by ultraviolet radiation and chemical agents. XPG works closely with protein ERCC1-XPF to facilitate DNA repair highlighting its collaborative function. Moreover XPG involvement extends to the base excision repair pathway further emphasizing its importance in maintaining DNA integrity.

XPG mutations are associated with disorders such as Xeroderma Pigmentosum (XP) and Cockayne Syndrome (CS). These conditions result from impaired DNA repair due to a dysfunctional NER pathway. In XP for example individuals become highly sensitive to UV exposure leading to increased cancer risk while CS leads to neurological and developmental deficits. XPG's interaction with the protein CSA becomes particularly relevant in Cockayne Syndrome indicating a vital connection in its pathology.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Single-stranded structure-specific DNA endonuclease involved in DNA excision repair (PubMed : 32522879, PubMed : 32821917, PubMed : 7651464, PubMed : 8078765, PubMed : 8090225, PubMed : 8206890). Makes the 3'incision in DNA nucleotide excision repair (NER) (PubMed : 32522879, PubMed : 32821917, PubMed : 8078765, PubMed : 8090225). Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble (PubMed : 32522879). Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA (PubMed : 9927729). Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (PubMed : 16246722). Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II (PubMed : 16246722). Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity (PubMed : 16246722). Required for DNA replication fork maintenance and preservation of genomic stability (PubMed : 26833090, PubMed : 32522879). Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site (PubMed : 26833090). In TFIIH stimulates the 5'-3' helicase activity of XPD/ERCC2 and the DNA translocase activity of XPB/ERCC3 (PubMed : 31253769). During HRR, binds to the replication fork with high specificity and stabilizes it (PubMed : 32522879). Also, acts upstream of HRR, to promote the release of BRCA1 from DNA (PubMed : 26833090).
See full target information ERCC5

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Genome biology 19:37 PubMed29548335

2018

Mutational signatures reveal the role of RAD52 in p53-independent p21-driven genomic instability.

Applications

Unspecified application

Species

Unspecified reactive species

Panagiotis Galanos,George Pappas,Alexander Polyzos,Athanassios Kotsinas,Ioanna Svolaki,Nickolaos N Giakoumakis,Christina Glytsou,Ioannis S Pateras,Umakanta Swain,Vassilis L Souliotis,Alexandros G Georgakilas,Nicholas Geacintov,Luca Scorrano,Claudia Lukas,Jiri Lukas,Zvi Livneh,Zoi Lygerou,Dipanjan Chowdhury,Claus Storgaard Sørensen,Jiri Bartek,Vassilis G Gorgoulis
View all publications

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