| Form | Liquid |
|---|---|
| Host Species | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Purification | Purified by antigen affinity column. |
| Endotoxin Level | Please contact with the lab for this information. |
| Applications | ELISA, IHC, WB |
| Species Reactivity | Human, Mouse |
| Target | MET18 homolog, MMS19, MMS19 nucleotide excision repair protein homolog, MMS19-like protein, MMS19L, hMMS19 |
| Immunogen | E. coli - derived recombinant Human MMS19 (Cys924-Ser1030). |
| Storage Buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. |
| Product Usage Information | ELISA:1:5000-1:20000;IHC:1:50-1:500;WB:1:500-1:2000 |
| Accession Number | Q96T76 |
| Background | MMS19 nucleotide excision repair protein homolog is a ~113 kDa protein. Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER), homologous recombination-mediated double-strand break DNA repair, DNA replication and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur (Fe-S) cluster assembly into ERCC2/XPD. Together with CIAO2, facilitates the transfer of Fe-S clusters to the motor protein KIF4A, which ensures proper localization of KIF4A to mitotic machinery components to promote the progression of mitosis. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery. 1. Ben-Shimon, L. et al. (2018) Journal of cell science 131. PMID: 29848660 2. Gari, K. et al. (2012) Science (New York, N.Y.) 337, 243-5. PMID: 22678361 3. Stehling, O. et al. (2012) Science (New York, N.Y.) 337, 195-9. PMID: 22678362 4. Seki, M. et al. (2013) The Journal of biological chemistry 288, 16680-16689. PMID: 23585563 5. Weon, JL. et al. (2018) Molecular cell 69, 113-125.e6. PMID: 29225034 6. Ito, S. et al. (2010) Molecular cell 39, 632-40. PMID: 20797633 7. Wu, X. et al. (2001) The Journal of biological chemistry 276, 23962-8. PMID: 11279242 |
| Note | For research use only |
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