CFD | Adipsin | PFD | DF | Complement factor D | C3 convertase activator | Properdin factor D | ADN | Complement Factor D (Adipsin) | D Component Of Complement (Adipsin) | EC 3.4.21.46 | AND | Complement Factor D Preproprotein | EC 3.4.21
规格或纯度
无动物源, 无载体, His标签, ≥95%(SDS-PAGE), expressed in HEK293; 见COA
生化机理
Complement Factor D is a serine protease that catalyzes the initial proteolytic step in the alternative pathway of complement. Expressed in adipose tissue at high levels, factor D is also known as adipsin. It is an exceptionally specific protease and the only known protein substrate is factor B in complex with C3. Factor D protease activity is regulated by reversible conformational changes, which differs from the majority of serine proteases whose regulation involves either activation by processing of the zymogens or inactivation by binding of the inhibitors. Compared to its physiologically important proteolytic activity, factor D has much lower activity toward synthetic peptide substrates. However, thioester substrates have been routinely used for assessing factor D activity.
Post-translational: CFD is activated by the removal of 5 residues at the N-terminus, named activation peptide, by the MASP-3 isoform of MASP1.
27.3 kDa, under reducing conditions; 26.7 kDa, under non-reducing conditions.
分子类型
蛋白质
产品线
生物产品
储存与运输
物理形态
粉末
储存缓冲液
Lyophilized from PBS, pH 7.4
浓度
expressed in HEK293; 见COA
复溶
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 0.5 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
-20℃保存 12个月;复溶后建议分装,避免反复冻融。
图片
Recombinant Human Complement Factor D Protein (rp181599) - SDS-PAGE
3 μg/lane of Recombinant Human Complement Factor D Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 27.3 kDa under reducing conditions and 26.7 kDa under non-reducing conditions.
In the absence of reducing agents, intramolecular disulfide bonds lock Complement Factor D into a compact conformation, leading to retarded migration and a dimer-like apparent molecular weight in SDS-PAGE (Uniport: P00746).