1. Recombinant Proteins
  2. Enzymes & Regulators Ubiquitin Related Proteins
  3. Transferases (EC 2) Ubiquitin Enzymes
  4. E3 Ligases
  5. RNF8 Protein, Human

RNF8 Protein, Human

Cat. No.: HY-P701564
Handling Instructions

RNF8 protein is an important E3 ubiquitin protein ligase that participates in the recruitment of repair proteins through "Lys-63" linked histone ubiquitination and "Lys-48" linked ubiquitination to clear damage sites. target protein, thereby participating in DNA damage signaling. RNF8 is recruited by ATM-phosphorylated MDC1 to form ionizing radiation-induced foci of TP53BP1 and BRCA1 at double-strand breaks. RNF8 Protein, Human is the recombinant human-derived RNF8 protein, expressed by E. coli , with tag free. The total length of RNF8 Protein, Human is 484 a.a., .

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Description

RNF8 protein is an important E3 ubiquitin protein ligase that participates in the recruitment of repair proteins through "Lys-63" linked histone ubiquitination and "Lys-48" linked ubiquitination to clear damage sites. target protein, thereby participating in DNA damage signaling. RNF8 is recruited by ATM-phosphorylated MDC1 to form ionizing radiation-induced foci of TP53BP1 and BRCA1 at double-strand breaks. RNF8 Protein, Human is the recombinant human-derived RNF8 protein, expressed by E. coli , with tag free. The total length of RNF8 Protein, Human is 484 a.a., .

Background

RNF8 Protein, an E3 ubiquitin-protein ligase, assumes a pivotal role in DNA damage signaling through two distinct mechanisms: firstly, by catalyzing 'Lys-63'-linked ubiquitination of histones H2A and H2AX to facilitate the recruitment of DNA repair proteins at double-strand break (DSB) sites, and secondly, by promoting 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. In response to DSBs, RNF8 is recruited by ATM-phosphorylated MDC1, leading to the 'Lys-63'-linked ubiquitination of histones and the subsequent formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). It also plays a role in non-homologous end joining (NHEJ) by facilitating the 'Lys-48'-linked ubiquitination and degradation of KU80/XRCC5. Additionally, RNF8 modulates chromatin structure, promoting extensive chromatin decondensation and activating ATM by inducing histone H2B ubiquitination, indirectly triggering histone H4 'Lys-16' acetylation. In the testis, RNF8 contributes to histone replacement during spermatogenesis, and at uncapped telomeres, it induces H2A ubiquitination and TP53BP1 recruitment, potentially exacerbating telomere-induced genome instability. Moreover, RNF8 is implicated in RAD51 assembly at DSBs, class switch recombination in the immune system, proper exit from mitosis, cytokinesis regulation, and may play a role in the regulation of RXRA-mediated transcriptional activity. This extensive functionality underscores the multifaceted contributions of RNF8 in orchestrating DNA damage responses and maintaining genomic integrity.

Species

Human

Source

E. coli

Tag

Tag Free

Accession

O76064 (G2-F485)

Gene ID

9025

Molecular Construction
N-term
RNF8 (G2-F485)
Accession # O76064
C-term
Synonyms
RNF8; E3 ubiquitin-protein ligase RNF8; hRNF8; RING finger protein 8; RING-type E3 ubiquitin transferase RNF8
Purity

Greater than 90% as determined by reducing SDS-PAGE.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Documentation
Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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The specific activity calculator equation

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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RNF8 Protein, Human
Cat. No.:
HY-P701564
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