The presence of Cysteine 26 in Wheat germ (Triticum aestivum) calmodulin (CaM) makes it unique vis-a-vis mammalian calmodulin. In contrast to mammalian CaMs, which lack cysteine, this preparation is ideal for applications requiring both calmodulin activation and residue specific tagging. The single SH moiety at Cys26 can be labeled using a variety of sulfhydryl (SH) reactive protein-modification reagents such as fluorescent maleimide derivatives. The presence of a single C-terminal tyrosine residue at the138 position (Tyr138) as against two tyrosines in mammalian calmodulin makes Tyr138 suitable as a mono-specific tag. Using Cys26 and Tyr138 allows wheat germ CaM to be independently derivatized at both N- and C-terminal regions within the molecule for structural, proteomic biomarker discovery and protein-protein interaction studies. Wheat germ CaM also has no tryptophan resulting in a distinctive absorbance spectrum when compared to mammalian CaM sequences. Calmodulin (CaM) is a ubiquitous, calcium-binding protein that binds and regulates a multitude of protein targets, many of which are involved in the Alzheimer"s and the Parkinson"s pathways^1,4. CaM has a molecular weight of about 17kDa, containing 148 amino acids, and pI of 3.9. CaM is characterized by two domains, connected by an alpha-helix chain. Each domain has the capacity to bind two calcium ions. Binding Ca²⁺ ions causes a conformational change in CaM, making it available for interaction with target proteins. Hence, CaM functions as an intracellular calcium ion bridge to mediate cellular reactions and responds appropriately to calcium ion concentration. In Alzheimer"s disease (AD), irregular calcium homeostasis seems to trigger CaM and its binding proteins, to enhance plaque formation and neurofibrillary degeneration, which results in cell death¹. The increased cytosolic levels of Ca²⁺ in AD neurons promotes CaM binding and regulation of available Ca²⁺/CaM-dependent CaM-binding proteins, associated with amyloid beta (Ab) formation. In addition, the increased level of Ca²⁺ triggers Calmodulin to activate calcium/CaM-dependent kinase II and precede neurofibrillary tangle formation^2,4. In Parkinson"s disease (PD), Calmodulin has been found to interact, in a calcium dependent manner, with Alpha-Synuclein, which is associated with the progression of PD. CaM was identified as one of the synuclein-interacting proteins that regulate synuclein conformation³. 用产品只提供给进一步的科研使用，不可应用于治疗等其他方面。 rPeptide是设在雅典，美国佐治亚州的一家生物技术公司，是一种在阿尔茨海默氏症和帕金森氏病的研究提供研究产品（重组多肽和蛋白质，抗体，试剂）市场的*。rPeptide还提供定制服务的范围从分子生物学，蛋白表达和纯化，13C和15N的多肽和蛋白质的统一标识。 rPeptide有一个专有的平台载体技术，使可溶性肽/蛋白在大肠杆菌中（如淀，β-淀粉样蛋白，瘦素，亲胰岛素）历史上的困难肽/蛋白表达。 商品名称    商品货号    商品品牌 Beta-Amyloid (1-40), Mouse, Rat    A-1007-1    rPeptide Beta-Amyloid (1-40), Starter Kit    A-1150-1    rPeptide Beta-Amyloid (1-40), Starter Kit    A-1150-2    rPeptide Beta-Amyloid (1-40), Ultra Pure, HCl    A-1156-1    rPeptide Beta-Amyloid (1-40), Ultra Pure, HCl    A-1156-2    rPeptide Beta-Amyloid (1-40), Ultra Pure, HFIP    A-1153-1    rPeptide Beta-Amyloid (1-40), Ultra Pure, HFIP    A-1153-2    rPeptide Beta-Amyloid (1-40), Ultra Pure, NaOH    A-1155-1    rPeptide Beta-Amyloid (1-40), Ultra Pure, NaOH    A-1155-2    rPeptide Beta-Amyloid (1-40), Ultra Pure, TFA    A-1001-1    rPeptide Beta-Amyloid (1-40), Ultra Pure, TFA    A-1001-2    rPeptide Beta-Amyloid (1-40, D23N)    A-1013-1    rPeptide Beta-Amyloid (1-40, D23N)    A-1013-2    rPeptide Beta-Amyloid (1-40, F4W)    A-1011-1    rPeptide Beta-Amyloid (1-40, F4W)    A-1011-2    rPeptide