Datasheet

Biological Description

Specificity	XRCC1 Rabbit mAb detects endogenous levels of total XRCC1 protein.
Background	XRCC1 (X-ray repair cross-complementing protein 1) is a pivotal scaffold protein involved in the DNA damage response, primarily coordinating the repair of single-strand breaks (SSBs) and facilitating base excision repair (BER). It is composed of three globular domains: the N-terminal domain binds DNA polymerase β, the central BRCT domain contains a poly(ADP-ribose) (PAR)-binding motif for PARP-1–dependent recruitment to DNA damage sites, and the C-terminal BRCT domain interacts with DNA ligase IIIα. These domains are connected by unstructured linker regions enriched with nuclear localization signals and motifs for post-translational modifications. XRCC1 orchestrates the spatial and temporal assembly of multiple DNA repair enzymes, including kinases, phosphatases, polymerases, deadenylases, and ligases, to accelerate the repair process. Post-translational modifications such as phosphorylation regulate XRCC1’s binding to partners like PNKP, APTX, and APLF, while ubiquitylation controls its protein turnover. Additionally, a redox-sensitive disulfide switch within the N-terminal domain modulates the binding affinity to polymerase β, thereby influencing the stability of the complex. XRCC1 also contributes to translesion synthesis via interaction with Rev1, supporting lesion bypass. It acts as a non-enzymatic assembly hub rather than a catalytic component. XRCC1 exhibits significant polymorphism, with variants like Arg194Trp and Arg399Gln influencing its interaction network, recruitment efficiency, DNA repair capability, and susceptibility to diseases, particularly various cancers.

Specificity

XRCC1 Rabbit mAb detects endogenous levels of total XRCC1 protein.

Background

XRCC1 (X-ray repair cross-complementing protein 1) is a pivotal scaffold protein involved in the DNA damage response, primarily coordinating the repair of single-strand breaks (SSBs) and facilitating base excision repair (BER). It is composed of three globular domains: the N-terminal domain binds DNA polymerase β, the central BRCT domain contains a poly(ADP-ribose) (PAR)-binding motif for PARP-1–dependent recruitment to DNA damage sites, and the C-terminal BRCT domain interacts with DNA ligase IIIα. These domains are connected by unstructured linker regions enriched with nuclear localization signals and motifs for post-translational modifications. XRCC1 orchestrates the spatial and temporal assembly of multiple DNA repair enzymes, including kinases, phosphatases, polymerases, deadenylases, and ligases, to accelerate the repair process. Post-translational modifications such as phosphorylation regulate XRCC1’s binding to partners like PNKP, APTX, and APLF, while ubiquitylation controls its protein turnover. Additionally, a redox-sensitive disulfide switch within the N-terminal domain modulates the binding affinity to polymerase β, thereby influencing the stability of the complex. XRCC1 also contributes to translesion synthesis via interaction with Rev1, supporting lesion bypass. It acts as a non-enzymatic assembly hub rather than a catalytic component. XRCC1 exhibits significant polymorphism, with variants like Arg194Trp and Arg399Gln influencing its interaction network, recruitment efficiency, DNA repair capability, and susceptibility to diseases, particularly various cancers.

Usage Information

Application

WB, IP, IHC, IF

Dilution

WB	IP	IHC	IF
1:1000	1:100	1:200 - 1:800	1:800 - 1:3200

Reactivity

Human, Mouse, Rat

Source

Rabbit

MW

82 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/25795425/
https://pubmed.ncbi.nlm.nih.gov/31324530/

XRCC1 Rabbit mAb

Biological Description

Usage Information

References

Application Data