产品名称
钙调素 来源于牛睾丸, BioUltra, ≥98% (SDS-PAGE), lyophilized powder, essentially salt free
biological source
bovine testis
product line
BioUltra
assay
≥98% (SDS-PAGE)
form
lyophilized powder
mol wt
16.79 kDa
storage condition
(Keep container tightly closed in a dry and well-ventilated place)
technique(s)
ligand binding assay: suitable
impurities
salt, essentially free
UniProt accession no.
application(s)
cell analysis
storage temp.
−20°C
Quality Level
Gene Information
cow ... CALM3(520277)
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Application
从牛睾丸中提取的钙调素已用于:
- 作为PhosphoSens试验中反应混合物的组分,以测量Ca2+/钙调素依赖性蛋白激酶II(CaMKII)底物磷酸化
- 生成标准曲线,用于测定组织中的钙调素原位浓度
- 作为无线电配体结合中的配体,用于研究钙调蛋白亲和力
Biochem/physiol Actions
环核苷酸依赖性磷酸二酯酶活化所需的 Ca2+ 结合蛋白。它也是一氧化氮合成酶、钙调磷酸酶以及多种激酶的辅因子/活化剂,这些激酶包括 ATP 酶、肌球蛋白轻链激酶和 CAM 激酶 I、II、III。它通过环二磷酸腺苷核糖介导利阿诺定受体活化并且与细胞内 Ca2+ 的内稳态有关。
钙调素(CaM)在高等植物和动物Ca2+ 信号转导通路中起辅助作用。Ca2+结合是CaM激活所必需的。激活后,CaM结合并激活许多参与多种细胞过程的靶蛋白,包括调节植物代谢、植物激素信号、离子转运、蛋白质折叠、蛋白质磷酸化和去磷酸化、细胞运动、胞吐和细胞骨架组装。在神经元中,钙激活的CaM有助于调节谷氨酸受体,调节信号通路中的蛋白质,调节电压门控钙通道(VGCC)活性。
General description
研究领域:细胞信号传导
钙调蛋白(CaM)是一种Ca2+传感器蛋白,包含四个EF手形基序,可与四个Ca2+离子结合。它广泛存在于所有真核生物中。
钙调蛋白(CaM)是一种Ca2+传感器蛋白,包含四个EF手形基序,可与四个Ca2+离子结合。它广泛存在于所有真核生物中。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
监管及禁止进口产品
此项目有
Nane Griem-Krey et al.
Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 156, 113895-113895 (2022-10-25)
Ca2+/calmodulin-dependent protein kinase II alpha (CaMKIIα) is a potential target for acute neuroprotection due to its key role in physiological and pathological glutamate signaling. The hub domain organizes the CaMKII holoenzyme into large oligomers, and additional functional effects on holoenzyme
The diversity of calcium sensor proteins in the regulation of neuronal function
McCue HV, et al.
Cold Spring Harbor Perspectives in Biology, 2(8) (2010)
Arkadiusz Miazek et al.
Scientific reports, 11(1), 7312-7312 (2021-04-02)
The neuronal membrane-associated periodic spectrin skeleton (MPS) contributes to neuronal development, remodeling, and organization. Post-translational modifications impinge on spectrin, the major component of the MPS, but their role remains poorly understood. One modification targeting spectrin is cleavage by calpains, a
E J McConnell et al.
Circulation research, 86(2), 191-197 (2000-02-10)
Plasma membrane (Ca(2+)+Mg(2+))-ATPase and Ca(2+) transport activities, best characterized in human erythrocytes, are stimulated by calmodulin and thought to play a crucial role in the termination of cellular Ca(2+) signaling in all cells. In plasma membranes isolated from cultured porcine
comparative proteomics illustrates the molecular mechanism of potato (Solanum tuberosum L.) tuberization inhibited by exogenous gibberellins in vitro
Cheng L, et al.
Physiologia Plantarum, 163, 103-123 (2018)
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