Recombinant Human C9 protein is a Human Full Length protein, in the 22 to 559 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
Complement component C9, C9
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human C9 protein (AB114199)
ab114199 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
C9 participates in defending against pathogens. It joins other complement components like C5b C6 C7 and C8 to form the MAC complex which facilitates cell lysis by forming pores in the membrane of target cells. This action directly results in microbial cell destruction serving a critical immune function. C9 is not only part of the MAC complex but also holds significance due to its unique function as the last step in the formation of the pore influencing the efficacy of pathogen elimination.
Pathways
C9 functions primarily within the complement cascade which includes the classical and alternative pathways. Its role is in the terminal pathway segment that ultimately leads to the formation of the MAC and follows the activation of C5 which cleaves to produce C5b. This connection extends to proteins like C3 which is upstream in the cascade and significantly impacts the cascade's activation highlighting C9's function as an integral terminal component in these pathways.
Specifications
Form
Liquid
General info
Function
Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells (PubMed : 26841934, PubMed : 9212048, PubMed : 9634479). C9 is the pore-forming subunit of the MAC (PubMed : 26841934, PubMed : 30111885, PubMed : 4055801).
Sequence similarities
Belongs to the complement C6/C7/C8/C9 family.
Post-translational modifications
Thrombin cleaves factor C9 to produce C9a and C9b.. Phosphorylation sites are present in the extracellular medium.. Initially, positions and connectivity of disulfide bonds were based on peptide sequencing done for the human protein (PubMed:8603752). The crystal structures for the human and mouse proteins corrected the positions and connectivities of the disulfide bonds (PubMed:30111885). The distance between Cys-57 and Cys-94 in the monomeric mouse protein precludes formation of a disulfide bond, contrary to what is seen in the structure of the human polymeric form of the protein (Probable).
Target data
Product promise
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