Analytical Data
-
基因名
F11
- Application
-
别名
F11；HATL4；Transmembrane protease serine 11F
-
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
P03951
-
表达区间
19-625aa
-
氨基酸序列
ECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV
-
分子量
69.4 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
The F11 protein, also known as coagulation factor XI, plays a critical role in the intrinsic pathway of blood coagulation, contributing to hemostasis and thrombus formation. Research into F11 and its related pathways has garnered significant attention in the context of thromboembolic disorders, such as deep vein thrombosis and pulmonary embolism, as well as during surgical procedures where bleeding risks must be managed. Studies have revealed that patients with deficiencies in F11 experience reduced clotting tendencies, which presents a paradox since their levels of other coagulation factors are generally normal. This has prompted investigations into the potential of F11-targeted therapies, particularly in anticoagulation strategies that aim to minimize the risk of thrombosis without significantly increasing bleeding risks. The exploration of F11's structure and function has also led to novel understanding of its role in immune response and inflammation, further expanding its significance beyond hemostasis. Recent advancements in recombinant DNA technology have enabled the production of recombinant F11 proteins, facilitating experiments to delineate its functional mechanisms and interaction with other components of the coagulation cascade. Consequently, ongoing research into F11 not only aims to refine therapeutic interventions for clotting disorders but also enhances our understanding of cardiovascular biology and pathology.
