Analytical Data
-
基因名
AFM
- Application
-
别名
AFM；ALB2；ALBA；Afamin
-
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
P43652
-
表达区间
1-599aa
-
氨基酸序列
MKLLKLTGFIFFLFFLTESLTLPTQPRDIENFNSTQKFIEDNIEYITIIA FAQYVQEATF EEMEKLVKDMVEYKDRCMADKTLPECSKLPNNVLQEKI CAMEGLPQKHNFSHCCSKVDAQ RRLCFFYNKKSDVGFLPPFPTLDPEE KCQAYESNRESLLNHFLYEVARRNPFVFAPTLLT VAVHFEEVAKSCCE EQNKVNCLQTRAIPVTQYLKAFSSYQKHVCGALLKFGTKVVHFIYI AI LSQKFPKIEFKELISLVEDVSSNYDGCCEGDVVQCIRDTSKVMNHICSKQ DSISSKIK ECCEKKIPERGQCIINSNKDDRPKDLSLREGKFTDSENVC QERDADPDTFFAKFTFEYSR RHPDLSIPELLRIVQIYKDLLRNCCNTE NPPGCYRYAEDKFNETTEKSLKMVQQECKHFQ NLGKDGLKYHYLIRLT KIAPQLSTEELVSLGEKMVTAFTTCCTLSEEFACVDNLADLVFG ELCG VNENRTINPAVDHCCKTNFAFRRPCFESLKADKTYVPPPFSQDLFTFHAD MCQSQN EELQRKTDRFLVNLVKLKHELTDEELQSLFTNFANVVDKCCK AESPEVCFNEESPKIGN
-
分子量
96 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
Atomic Force Microscopy (AFM) has emerged as a powerful tool in the study of recombinant proteins due to its ability to provide high-resolution, three-dimensional images of molecular structures at the nanoscale. Recombinant proteins, produced through recombinant DNA technology, are essential in various biomedical applications, including drug development, vaccine production, and enzyme engineering. The characterization of these proteins is vital for understanding their function, stability, and interactions. Traditional techniques, such as X-ray crystallography and NMR spectroscopy, although widely used, may not fully capture the dynamic nature of proteins in their native environments. AFM, on the other hand, allows for the visualization of protein conformations and interactions in real-time, under physiological conditions. This unique capability has opened new avenues for studying protein folding, aggregation, and binding events, providing insights that are critical for the design of more effective therapeutics. Recent advancements in AFM techniques, such as high-speed imaging and force spectroscopy, have further enhanced the resolution and applicability of this approach in protein research. As a result, researchers are increasingly turning to AFM to complement conventional methodologies, aiming to unravel the complexities of recombinant proteins and accelerate the development of innovative solutions in medicine and biotechnology.
