Analytical Data
-
基因名
Serpina9
- Application
-
别名
SERPINA9;GCET1;SERPINA11;Serpin A9
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q86WD7
-
表达区间
24-417aa
-
氨基酸序列
ANAPSAYPRPSSTKSTPASQVYSLNTDFAFRLYRRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQGLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNFPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVLPSKGKMRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLETILPKMGIQNVFDKNADFSGIAKRDSLQVSKATHKAVLDVSEEGTEATAATTTKFIVRSKDGPSYFTVSFNRTFLMMITNKATDGILFLGKVENPTKS
-
分子量
49.1 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Serpina9, also known as serpin family A member 9, is a serine protease inhibitor that plays a crucial role in regulating various physiological processes, especially in the immune system and apoptosis. Recent studies have suggested that Serpina9 is involved in the modulation of inflammatory responses and cellular homeostasis, highlighting its potential implications in cancer and autoimmune diseases. The ability of Serpina9 to inhibit specific serine proteases makes it a key player in controlling proteolytic cascades that, when dysregulated, can contribute to pathological conditions. Despite its importance, research on Serpina9 has been relatively limited compared to other serpins, prompting investigations into its molecular structure, functional mechanisms, and therapeutic potentials. The development of recombinant Serpina9 proteins has enabled researchers to explore its biochemical properties in greater detail, paving the way for future studies that may reveal its applicability in medical interventions. Understanding the structure-function relationship of Serpina9 through recombinant techniques can offer insights into its role in disease modulation and could ultimately lead to novel therapeutic strategies that target its inhibitory functions.
