Mouse S100A1 Protein (His Tag)

AI266795,S100,S100a

100ug (NPP3462) Please inquiry

Catalog Number	P50266-M07E
Organism Species	Mouse
Host	E. coli
Synonyms	AI266795,S100,S100a
Molecular Weight	The recombinant mouse S100A1 consisting of 109 amino acids and has a calculated molecular mass of 12.5 kDa. rmS100A1 migrates as an approximately 14 kDa band in SDS-PAGE under reducing conditions.
predicted N	Met
SDS-PAGE
Purity	> 95 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the mouse S100A1 (P56565) (Gly 2-Ser 94) was expressed, with a polyhistide tag at the N-terminus.
Bio-activity	Measured by its ability to bind human AGER in a functional ELISA.
Research Area	Neuroscience \|Cell Type Marker in Neurodevelopment \|Neuronal Cell Markers \|Synapse & Synaptic Proteins \|Calcium Signaling \|Calcium Binding Protein \|
Formulation	Lyophilized from sterile PBS, pH 7.5 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	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.This protein has been shown to function in the processes including stimulation of Ca²⁺-induced Ca²⁺ release, inhibition of microtubule assembly, and inhibition of PKC-mediated phosphorylation.. Phosphoglucomutase is a target protein whose activity is antagonistically regulated by S100A1, and recently, S100A1 is also identified as a potent molecular chaperone and a new member of the Hsp70/Hsp90 multichaperone complex. S100A1 displays a tissue-specific expression pattern with highest levels in myocardium and is considered to be an important regulator of cardiac contractility. Accordingly, reduced expression or mutations of S100A1 gene have been implicated in cardiomyopathies.
Reference	Remppis, A .et al., 1996, Biochim. Biophs. Acta. 1313: 253-257. Most, P. et al., 2001, Proc. Natl. Acad. Sci. U.S.A. 98: 13889-13894 Okada, M. et al., 2004, J. Biol. Chem. 279: 4221-4233. Schafer, W.E. et al., 1995, Genomics. 25: 638-643. Landar, A. et al., 1996, Cell. Calcium. 20: 279-285.