Rad1 Antibody

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Description

DNA Damage Response and Repair

  • RAD1 forms the 9-1-1 complex with Rad9 and Hus1, which stabilizes DNA repair enzymes like FEN1 and DNA ligase I .

  • The complex is recruited to double-strand breaks (DSBs) during S phase, facilitating homologous recombination .

  • Sumoylation at lysine 32 (K32) regulates RAD1’s dissociation from DNA post-repair, enhancing efficiency in high-damage conditions .

Cancer and Genomic Stability

  • Knockout studies in mice show that RAD1 deletion increases susceptibility to skin tumors (e.g., DMBA-induced papillomas) .

  • Overexpression of Rad9 (a binding partner) correlates with poor prognosis in ovarian and prostate cancers .

  • Jab1/CSN5-mediated degradation of the 9-1-1 complex suppresses checkpoint signaling, accelerating genomic instability .

Table 1: Experimental Models and Outcomes

Study FocusModel SystemKey FindingSource
Sumoylation MechanismS. cerevisiaeSumoylation reduces RAD1’s DNA affinity by 40%, enabling lesion turnover .
Checkpoint SignalingMouse keratinocytesRAD1 loss increases tumor size by 2.5-fold in DMBA-treated mice .
Protein InteractionsHuman cell linesJab1 binds directly to RAD1, triggering 9-1-1 complex degradation .
Structural AnalysisFission yeastRAD1’s N-terminal domain is essential for Hus1-Rad9 binding .

Applications in Research

  • DNA Repair Studies: Rad1 antibodies identify RAD1 localization at DSBs via IF/ICC .

  • Cancer Biomarker Screening: Used to correlate RAD1 expression levels with tumor progression .

  • Mechanistic Studies: Detect sumoylation or phosphorylation states in response to UV/CPT treatment .

Technical Considerations

  • Storage: Stable at -20°C in PBS with 0.02% sodium azide .

  • Controls: Recommended cell lines include HeLa, A431, and 293T for WB validation .

  • Limitations: Cross-reactivity with RAD1 isoforms (3 splice variants) may require isoform-specific validation .

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
Rad1 antibody; Rec1 antibody; Cell cycle checkpoint protein RAD1 antibody; mRAD1 antibody; EC 3.1.11.2 antibody; DNA repair exonuclease rad1 homolog antibody; Rad1-like DNA damage checkpoint protein antibody
Target Names
Uniprot No.

Target Background

Function
This antibody targets Rad1, a critical component of the 9-1-1 cell-cycle checkpoint response complex. This complex plays a pivotal role in DNA repair. Upon DNA damage, the 9-1-1 complex, facilitated by the RAD17-replication factor C (RFC) clamp loader complex, is recruited to the lesion. It acts as a sliding clamp platform on DNA for various proteins involved in long-patch base excision repair (LP-BER). Notably, the 9-1-1 complex enhances DNA polymerase beta (POLB) activity by boosting its affinity for the 3'-OH end of the primer-template and stabilizes POLB at sites where LP-BER occurs. Additionally, it stimulates endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths, and promotes DNA ligase I (LIG1) activity on long-patch base excision repair substrates. The 9-1-1 complex is essential for recruiting RHNO1 to sites of double-stranded breaks (DSB) during the S phase. Isoform 1 exhibits 3'->5' double-stranded DNA exonuclease activity.
Gene References Into Functions
  1. HUS1 acts as a component of the canonical 9-1-1 complex during meiotic prophase I to promote DSB repair. Further research suggests that RAD1 and TOPBP1 respond to unsynapsed chromatin through an alternative mechanism that does not require RAD9 or HUS1. PMID: 23468651
  2. The rad1 protein is essential for repairing DNA lesions induced by UV-light, HU and gamma rays, and for mediating G(2)/M and S/M checkpoint controls. PMID: 21637962
  3. Data suggests that Mrad1 is crucial for preventing tumor development. PMID: 20334655
Database Links
Protein Families
Rad1 family
Subcellular Location
Nucleus.
Tissue Specificity
Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level). Expressed in brain, testis, kidney, heart, liver and lung.

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