Specifications
| SPECIES: | Human |
|---|---|
| SOURCE SPECIES: | HEK293 cells |
| SEQUENCE: | Thr 22 - Thr 457 |
| FUSION TAG: | Tag free |
| TESTED APPLICATIONS: | WB |
| APPLICATIONS: | This recombinant protein can be used for WB. For research use only. |
Properties
| PURITY: | >98% as determined by SDS-PAGE. |
|---|---|
| PREDICTED MOLECULAR WEIGHT: | 49 kDa |
| PHYSICAL STATE: | Lyopholized |
| BUFFER: | PBS, pH7.4 |
| STORAGE CONDITIONS: | Lyophilized Protein should be stored at -20˚C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20˚C or -70˚C. Avoid repeated freeze-thaw cycles. |
Additional Info
| ALTERNATE NAMES: | BACE1, ASP2, BACE, FLJ90568, HSPC104, KIAA1149, Memapsin-2 |
|---|---|
| ACCESSION NO.: | NP_036236.1 |
Background
| Beta-secretase 1 (BACE1) is also known as beta-site APP cleaving enzyme 1 (beta-site amyloid precursor protein cleaving enzyme 1), memapsin-2 (membrane-associated aspartic protease 2), and aspartyl protease 2 (ASP2), β-Secretase , and is a member of the peptidase A1 protein family, BACE1 is a type I integral membrane glycoprotein and aspartic protease that is found mainly in the Golgi. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths in peripheral nerve cells. The transmembrane protein contains two active site aspartate residues in its extracellular protein domain and may function as a dimer. This protease is responsible for the proteolytic processing of the amyloid precursor protein (APP). Generation of the 40 or 42 amino acid-long amyloid-β peptides that aggregate in the brain of Alzheimer's patients requires two sequential cleavages of the APP. Extracellular cleavage of APP by BACE creates a soluble extracellular fragment and a cell membrane-bound fragment referred to as C99. The elevation of BACE1 levels can be induced by amyloid plaques surrounding neurons at early stages of pathology before neuron death occurs, and may drive a positive-feedback loop in AD. |
ebiomall.com
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你可以试着读一下看看。
提供亲和纯化相关资料:http://wenku.baidu.com/view/ef8f3831f8c75fbfc67db276
如有帮助,请采纳,谢谢~
▷ 重组蛋白生产平台
▪ HEK293细胞瞬转
▪ CHO细胞
▪ 昆虫细胞/杆状病毒
▪ 酵母细胞
▪ 大肠杆菌发酵
大家好,想请教大家一个关于HPLC方法学的问题。
目前我们做的一个蛋白药,没有标准品,液相建立一个方法只想用于纯度鉴定,不去定量,这个方法所得到的图谱就一个主蛋白峰,面积归一化法相当于100%,现在就这个方法的方法学验证提出下面几点疑问:
1.因为我只做纯度鉴定,这个方法的方法学应该做系统适用性、专属性、检测限、耐用性和精密度这些,还是按照定量的全套加上定量限、线性、范围、准确度这些?
2.纯度鉴定中,我觉得应该对杂质进行定量,但是我们的这个方法只有一个主蛋白峰,几乎没有杂质峰,这样的话这个方法学我应该以什么为标准证明纯度呢?需将样品进行适当的氧化、酸、碱破坏吗?然后证明破坏后主峰能和产生的杂质分开?
3.对应生物蛋白药的杂质,应该属于无法获得的,如果通过强破坏,这个杂质也是不好鉴定的,是不是我只需要知道主峰能和强破坏的降解物分开,就可以说方法建立成功?还是生物药没有必要做这个强破坏,简单的走一下系统适用性、专属性、检测限、耐用性和精密度这样的流程就行?
说的有点乱,主要是自己对这个生物药的HPLC纯度鉴定的方法学,实在是疑惑重重,希望有经验的大侠能帮忙解答下。非常感谢!

