Calneuron 1 (CALN1) (AA 1-192) protein (His tag)

Details zu Produkt Nr. ABIN667256, Anbieter: Anmelden zum Anzeigen
Proteinname
  • CALN1
  • CABP8
  • 9630012C17Rik
  • Cabp8
  • calneuron 1
  • CALN1
  • caln1
  • Caln1
Proteineigenschaft
AA 1-192
4
3
2
1
1
1
1
Spezies
Human
10
2
Quelle
Escherichia coli (E. coli)
6
3
2
1
Protein-Typ
Recombinant
Aufreinigungstag / Konjugat
Dieses Calneuron 1 Protein ist gelabelt mit His tag.
Applikation
SDS-PAGE (SDS)
Optionen
Hersteller
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Hersteller Produkt- Nr.
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Produktmerkmale CALN1, 1-192aa, Human, His tag, E.coli
Reinheit > 90 % by SDS - PAGE
Hintergrund CALN1 is high similarity to the calcium-binding proteins of the calmodulin family. This protein contains two EF-hand domains and potential calcium-binding sites. Also, It negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. CALN1 play a role in the physiology of neurons and is potentially important in memory and learning. Recombinant human CALN1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Synonyms: Calcium-binding protein 8, CABP8, Calneuron-1, CaBP8, Calneuron I. NCBI no.: NP_001017440
Molekulargewicht 24.0 kDa (212aa) confirmed by MALDI-TOF
Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Konzentration 0.5mg/ml (determined by Bradford assay)
Buffer Liquid. 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol, 2mM DTT, 50mM NaCl, 0.1mM PMSF
Lagerung 4 °C
Bilder des Herstellers
SDS-PAGE (SDS) image for Calneuron 1 (CALN1) (AA 1-192) protein (His tag) (ABIN667256) Calneuron 1 (CALN1) (AA 1-192) protein (His tag)
Allgemeine Veröffentlichungen McCue, Burgoyne, Haynes: "Membrane targeting of the EF-hand containing calcium-sensing proteins CaBP7 and CaBP8." in: Biochemical and biophysical research communications, Vol. 380, Issue 4, pp. 825-31, 2009 (PubMed).

Wu, Lin, Liu, Jamrich, Shaffer: "Identification of a human brain-specific gene, calneuron 1, a new member of the calmodulin superfamily." in: Molecular genetics and metabolism, Vol. 72, Issue 4, pp. 343-50, 2001 (PubMed).