Recombinant Human CFD Protein, N-His (PX-P5643) expressed in E. coli, Purity: >90% as determined by SDS-PAGE..
Highlights
High Purity (>90% as determined by SDS-PAGE.) — Verified by SDS-PAGE for downstream accuracy.
E. coli Expression — Optimized for functional studies.
表达系统
E. coli
Accession号
P00746
蛋白长度
Met1-Ala253
应用
ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
种属
Homo sapiens (Human)
性质
Recombinant
内毒素水平
Please contact with the lab for this information.
纯度
>90% as determined by SDS-PAGE.
预测分子量
29.34 kDa
状态
Lyophilized
保存溶液
Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
重悬
Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
运输
In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
稳定性和存储
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Complement factor D (CFD) is a ~27 kDa protein. Serine protease that initiates the alternative pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. In contrast to other complement pathways (classical, lectin and GZMK) that are directly activated by pathogens or antigen-antibody complexes, the alternative complement pathway is initiated by the spontaneous hydrolysis of complement C3. The alternative complement pathway acts as an amplification loop that enhances complement activation by mediating the formation of C3 and C5 convertases. Activated CFD cleaves factor B (CFB) when the latter is complexed with complement C3b, activating the C3 convertase of the alternative pathway.
1. Forneris, F. et al. (2010) Science (New York, N.Y.) 330, 1816-20. PMID: 21205667
2. Katschke, KJ. et al. (2012) The Journal of biological chemistry 287, 12886-92. PMID: 22362762
