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  • 产品名称：S100CalciumBindingProteinA1(S100A1)(AA1-94)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
S100CalciumBindingProteinA1(S100A1)(AA1-94)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 11.4 kDa. The protein migrates as 11 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 Protein S100-A1 / S100A1 is a Ca2+binding protein of the EF-hand type that belongs to the S100 protein family. S100 proteins consisting of at least 19 members exist as dimers in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell-cycle progression and cell differentiation. S100-A1 can weakly bind calcium but bind zinc very tightly-distinct s with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-s.
Molecular Weight 11.4 kDa
UniProt P23297
Pathways Regulation of Muscle Cell Differentiation, Toll-Like Receptors Cascades
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 8.0
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 S100 Calcium Binding Protein A1 (S100A1) (AA 1-94) (Active) protein (His tag) (ABIN2181709) Human S100A1, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained o...
Background publications Yamaguchi, Umeda, Shimamoto, Tsuchiya, Tokumitsu, Tokuda, Kobayashi: "S100 proteins modulate protein phosphatase 5 function: a link between CA2+ signal transduction and protein dephosphorylation." in: The Journal of biological chemistry, Vol. 287, Issue 17, pp. 13787-98, 2012 (PubMed).

Wang, Zhang, Fernig, Spiller, Martin-Fernandez, Zhang, Ding, Rao, Rudland, Barraclough: "Heterodimeric interaction and interfaces of S100A1 and S100P." in: The Biochemical journal, Vol. 382, Issue Pt 1, pp. 375-83, 2004 (PubMed).

Engelkamp, Schäfer, Erne, Heizmann: "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart." in: Biochemistry, Vol. 31, Issue 42, pp. 10258-64, 1992 (PubMed).