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  • 产品名称：Glutaredoxin1(GRX1)(AA1-106)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
Glutaredoxin1(GRX1)(AA1-106)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 12.7 kDa. The protein migrates as 12.7 kDa under reducing (R) condition (SDS-PAGE).
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Background Glutaredoxin-1 (GRX1) is also known as Thioltransferase-1 (TTase-1), GLRX, GRX, GLRX1, which belongs to the glutaredoxin family. GRX1 / GLRX contains one glutaredoxin domain, which exists in either a reduced or an oxidized form. GRX1 / GLRX has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase and functions as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by the enzymeribonucleotide reductase.
Molecular Weight 12.7 kDa
NCBI Accession NP_001112362
UniProt P35754
Research Area Oxidative Stress
Pathways Cell RedoxHomeostasis
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 150 mM NaCl, pH 7.5 with 1 mM DTT
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Glutaredoxin 1 (GRX1) (AA 1-106) (Active) protein (His tag) (ABIN2181166) Human Glutaredoxin 1, His Tag on SDS-PAGE under reducing (R) condition. The gel was s...
Background publications Yang, Jao, Nanduri, Starke, Mieyal, Qin: "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity." in: Biochemistry, Vol. 37, Issue 49, pp. 17145-56, 1999 (PubMed).