CDGSH Iron Sulfur Domain 1 (CISD1) protein (His tag)

Details zu Produkt Nr. ABIN1098400, Anbieter: Anmelden zum Anzeigen
Proteinname
  • si:dkey-18n13.4
  • zgc:63561
  • ZCD1
  • zcd1
  • cisd1a
  • mitoneet
  • cisd1
  • cisd1b
  • C10orf70
  • mitoNEET
  • AU043990
  • AW743335
  • D10Ertd214e
  • Zcd1
  • MitoNEET
  • RGD1309529
  • CDGSH iron sulfur domain 1
  • CDGSH iron sulfur domain 1 L homeolog
  • CDGSH iron-sulfur domain-containing protein 1
  • CDGSH iron sulfur domain 1 S homeolog
  • cisd1
  • CISD1
  • cisd1.L
  • LOC450472
  • cisd1.S
  • Cisd1
Spezies
Human
5
1
1
1
Quelle
Escherichia coli (E. coli)
3
2
2
1
Protein-Typ
Recombinant
Aufreinigungstag / Konjugat
His tag
Applikation
SDS-PAGE (SDS)
Optionen
Hersteller
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Reinigung purified by chromatography
Reinheit > 90 % by SDS - PAGE
Proteinname
Hintergrund CISD1 is a protein with a CDGSH iron-sulfur domain and has been shown to bind a redox-active [2Fe-2S] cluster. The protein has been localized to the outer membrane of mitochondria and is thought to play a role in regulation of oxidation. Recombinant human CISD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Molekulargewicht 11.4 kDa (100aa) confirmed by MALDI-TOF
NCBI Accession NP_060934
Kommentare

Synonyms: CDGSH iron-sulfur domain-containing protein 1, C10orf70, MDS029, mitoNEET, ZCD1

Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Konzentration 0.5 mg/ml (determined by Bradford assay)
Buffer 20 mM Tris-HCl buffer (pH 8.0) containing 0.15 M NaCl, 10% glycerol, 1 MM DTT
Lagerung 4 °C
Informationen zur Lagerung Avoid repeated freezing and thawing cycles.
Bilder des Herstellers
 image for CDGSH Iron Sulfur Domain 1 (CISD1) protein (His tag) (ABIN1098400) CDGSH Iron Sulfur Domain 1 (CISD1) protein (His tag)
Allgemeine Veröffentlichungen Conlan, Paddock, Homer, Axelrod, Cohen, Abresch, Zuris, Nechushtai, Jennings: "Mutation of the His ligand in mitoNEET stabilizes the 2Fe-2S cluster despite conformational heterogeneity in the ligand environment." in: Acta crystallographica. Section D, Biological crystallography, Vol. 67, Issue Pt 6, pp. 516-23, 2011 (PubMed).

Zuris, Harir, Conlan, Shvartsman, Michaeli, Tamir, Paddock, Onuchic, Mittler, Cabantchik, Jennings, Nechushtai: "Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, Issue 32, pp. 13047-52, 2011 (PubMed).

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