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Mouse S100A6 Protein

2A9,5B10,Cacy,CALCYCLIN,PRA

Catalog Number P50229-MNAE
Organism Species Mouse
Host E. coli
Synonyms 2A9,5B10,Cacy,CALCYCLIN,PRA
Molecular Weight The recombinant mouse S100A6 consisting of 89 amino acids and has a calculated molecular mass of 10 kDa as estimated in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 98 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mouse S100A6 (NP_035443.1) (Met 1-Lys 89) was expressed.
Bio-activity
Research Area Immunology |Signal Transduction |Neurotransmitter Receptors, Transporters, and Ion Channels |Calcium-binding Proteins and Related Molecules
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. S100A6 (S100 calcium binding protein A6) is a member of the S100 family of proteins, and functions in prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of S100A6 have been implicated in melanoma.
Reference
  • Schäfer, B.W. et al., 1996, Trends Biochem. Sci. 21 (4): 134-140.
  • Donato,R. et al., 2003, Microsc. Res. Tech. 60 (6): 540-551.
  • Nowotny, M. et al., 2003, J. Biol. Chem. 278 (29): 26923-26928.
  • Nonaka D, et al., 2008, J. Cutan. Pathol. 35 (11): 1014-1019.
  • Marenholz, I. et al., 2004, Biochem. Biophys. Res. Commun. 322 (4): 1111-22.