Stressmarq公司研發(fā)的β淀粉樣蛋白，該產(chǎn)品有3種規(guī)格，產(chǎn)品貨號(hào)為SPR-488，如需購(gòu)買Stressmarq公司產(chǎn)品，請(qǐng)聯(lián)系國(guó)內(nèi)一級(jí)代理商-欣博盛生物，本文是對(duì)該產(chǎn)品的詳細(xì)介紹。

	從左至右分別為Aβ單體 (SPR-485)，寡聚體 (SPR-488) 和原纖維 (SPR-487) 的電鏡圖。負(fù)染色透射電子顯微鏡圖像在 80 Kv 下在碳涂層的 400 目銅網(wǎng)格上使用磷鎢酸和乙酸雙氧鈾染色獲得。比例尺 = 100 nm。
	從左至右分別為Aβ單體 (SPR-485)，寡聚體 (SPR-488) 和原纖維 (SPR-487) 的原子力顯微鏡圖。將1.0 mg/mL樣品在 dH2O 中稀釋至 0.1 mg/mL 置于新鮮切割的云母上，清洗、干燥并以輕敲模式進(jìn)行原子力顯微鏡分析。左圖為 2.5 x 2.5 µm x-y，z 范圍為 10 nm。
	從左至右分別是Aβ單體 (SPR-485)，寡聚體 (SPR-488) 和原纖維 (SPR-487) 的WB，抗體是抗Aβ6E10抗體。三種Aβ蛋白 (160 pmol) 在 4-12% Bis-Tris SDS-PAGE 上跑膠后，在 0.02% v/v Tween-20 存在下轉(zhuǎn)移到硝酸纖維素上，并用 1:1000 小鼠 6E10 一抗做WB。在 TEM/AFM 下觀察到的寡聚體顯示出明顯的二聚體/三聚體條帶以及來自 ~37-75 kDa 的信號(hào)（中）。在 TEM/AFM 下觀察到的原纖維顯示出大于 100 kDa 的信號(hào)，并且在濃縮膠（右）中有明顯的信號(hào)。
	Aβ 1-42 寡聚體 (SPR-488) 和原纖維 (SPR-487) 對(duì)原代大鼠皮層神經(jīng)元顯示出劑量依賴性毒性，但單體 (SPR-485) 沒有毒性。大鼠原代皮層神經(jīng)元用不同濃度的 (A) 單體、(B) 寡聚體或 (C) 原纖維處理 14 天后的存活率，由 MAP2 陽性神經(jīng)元量化并表示為對(duì)照的百分比（空白對(duì)照設(shè)為100%）。原纖維和相應(yīng)的載體對(duì)照先在 Bioruptor 超聲破碎儀中進(jìn)行超聲處理。測(cè)試條件在與未處理的對(duì)照和載體對(duì)照相同的板中運(yùn)行，由不含Aβ 1-42 蛋白的緩沖液組成。數(shù)據(jù)表示為平均值 +/- s.e.m. (n = 6)。使用單向方差分析和 Dunnett 檢驗(yàn)對(duì)數(shù)據(jù)進(jìn)行全局分析； ** p<0.01 統(tǒng)計(jì)數(shù)據(jù)相比于對(duì)照； ## p<0.01, #### p<0.0001 統(tǒng)計(jì)數(shù)據(jù)相比于載體對(duì)照。 § 代表未經(jīng)處理的對(duì)照條件。

產(chǎn)品概述

產(chǎn)品名稱：β淀粉樣蛋白

產(chǎn)品描述：β淀粉樣蛋白 1-42 寡聚體

應(yīng)用范圍：WB, In vivo Assay, In vitro Assay

濃度：各批次不同，請(qǐng)?jiān)斠娬f明書

標(biāo)記物：無標(biāo)簽

性質(zhì)：合成的 (TFA 制備)

來源物種：人

表達(dá)系統(tǒng)：N/A

氨基酸序列：DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

純度：>95%

蛋白長(zhǎng)度：42 個(gè)氨基酸

產(chǎn)品特性

儲(chǔ)存緩沖液：Phosphate buffer (PB) pH 7.4 and 20 mM NaCl

儲(chǔ)存溫度：-80oC

運(yùn)輸溫度：干冰. 運(yùn)輸: 該產(chǎn)品會(huì)與其他同訂單產(chǎn)品分開發(fā)貨.

純化方式：N/A

Protein Size：4.5 kDa

引用該產(chǎn)品：Human Synthetic Amyloid Beta Oligomers (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-488)

分析證書：該蛋白已經(jīng)通過質(zhì)譜儀和HPLC檢測(cè)證明純度大于95%.

生物學(xué)特性

別名：Abeta Oligomers, Abeta peptide, Amyloid beta peptide oligomers, Beta amyloid peptide oligomers, amyloid beta precursor protein peptide oligomers, APP

研究領(lǐng)域：淀粉樣蛋白, 神經(jīng)生物學(xué), 神經(jīng)衰退疾病, 阿爾茨海默病

細(xì)胞定位：細(xì)胞膜

GeneID：351

Swiss Prot：P05067

科研背景：

Our Amyloid Beta 1-42 (Aβ42) Oligomers are generated from Amyloid Beta Peptide 1-42 pre-treated with 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) as previously published (1,2). Our Aβ42 oligomers present as globular oligomers when observed under TEM and AFM, and have a unique dimer/trimer and oligomer signal on a Western Blot with an anti-amyloid beta antibody. Our Aβ42 oligomers were also demonstrated to be toxic to primary rat cortical neurons in a dose-dependent manner. In the brain, amyloid beta peptide (Aβ) is generated by protease cleavage of amyloid precursor protein (APP), which aggregates into oligomers, protofibrils, fibrils and ultimately plaques in neurodegenerative diseases. The accumulation of Aβ plaques in the brain is considered a hallmark of Alzheimer’s disease (AD), and most of the drugs tested for AD in the past 20 years have targeted amyloid beta accumulation (3). Soluble Aβ oligomers isolated from the brains of AD patients or those generated in vitro potently impaired synapse structure and function (4). Aβ oligomers generated in vitro were toxic to PC12 cells (5) and SH-SY5Y cells (6). Aβ was demonstrated to interact with tauopathies to affect neurodegeneration in AD patients (7) and accumulations of Aβ were shown to be associated with lower survival rates in Parkinson’s disease patients with dementia (8).

參考資料：

1. Stine et al. 2003. JBC. 278(13):11612-22. doi: 10.1074/jbc.M210207200

2. Ahmed et al. 2010. Nature Structural & Molecular Biology. 17(5):561-7. doi: 10.1038/nsmb.1799

3. Panza et al. 2019. Nat Rev Neurol. 15:73-88 

4. Shankar et al. 2008. Nat Med. 14(8):837-842. doi: 10.1038/nm1782

5. Chromy et al. 2003. Biochemistry. 42:12749-12760. doi: 10.1021/bi030029q

6. Kayed et al. 2003. Science. 300(5618): 486-489. doi: 10.1126/science.1079469

7. Want et al. 2016. JAMA Neurol. 73(9):1070-7. doi: 10.1001/jamaneurol.2016.2078

8.,Kotzbauer et al. 2012. Arch Neurol. 69(10): 1326-1331. doi: 10.1001/archneurol.2012.1608

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