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Key Documents

M0630

Sigma-Aldrich

肌红蛋白 来源于马骨骼肌

95-100%, essentially salt-free, lyophilized powder

同義詞:

肌红蛋白 来源于马骨骼肌

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About This Item

CAS號碼:
EC號碼:
MDL號碼:
分類程式碼代碼:
12352202
NACRES:
NA.61

生物源

equine skeletal muscle

品質等級

化驗

95-100%

形狀

essentially salt-free, lyophilized powder

分子量

~17 kDa(lit.)

鐵含量

0.25-0.32%

技術

mass spectrometry (MS): suitable

溶解度

H2O: soluble 10 mg/mL

UniProt登錄號

儲存溫度

−20°C

基因資訊

horse ... MB(100054434)

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應用

马骨骼肌肌红蛋白被应用于一项对实验蛋白混合物进行质谱分析的研究中。

生化/生理作用

肌红蛋白对骨骼肌在接近最大氧气需求时的O2 的供应至关重要,并通过将PO2 维持在高于支持线粒体功能所需的水平来防止缺氧。
马骨骼肌肌红蛋白是一种单链血红素蛋白,含有153个氨基酸残基。它没有二硫键或游离-SH基团。肌红蛋白含8个大小不一的右旋螺旋区域,并由无序或随机线圈区域连接。

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


分析證明 (COA)

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Anthony W Maresso et al.
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Emily S Choy et al.
The Journal of experimental biology, 222(Pt 11) (2019-05-18)
Arctic marine ecosystems are currently undergoing rapid environmental changes. Over the past 20 years, individual growth rates of beluga whales (Delphinapterus leucas) have declined, which may be a response to climate change; however, the scarcity of physiological data makes it difficult
Ru Fang et al.
Journal of nanobiotechnology, 9, 19-19 (2011-05-19)
The synthesis of bioactive nanoparticles with precise molecular level control is a major challenge in bionanotechnology. Understanding the nature of the interactions between the active components and transport biomaterials is thus essential for the rational formulation of bio-nanocarriers. The current
Y H Guan et al.
Journal of chromatography. A, 1217(21), 3525-3530 (2010-04-20)
Separation of large bioactive molecules such as proteins, DNAs and RNAs using aqueous two-phase systems (ATPSs) and liquid-liquid partition-based counter-current chromatography (CCC) can avoid risks of sample loss and denaturation, and greatly reduce processing time. We have constructed toroidal columns
L Henry et al.
Structural dynamics (Melville, N.Y.), 7(5), 054702-054702 (2020-09-29)
The correct folding of proteins is of paramount importance for their function, and protein misfolding is believed to be the primary cause of a wide range of diseases. Protein folding has been investigated with time-averaged methods and time-resolved spectroscopy, but

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