GKGSFRFSYSKNETYQLFLSYSSKKEKMFLHVKGEIHLGRFVMRNRDVVLTTTFVDDIKA LPTTYEKGEYFAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELKDIKRCLGYHL DVSLAFSEISVGAEFNKDDCVKRGEGRAVNITSENLIDDVVSLIRGGTRKYAFELKEKLL RGTVIDVTDFVNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLERAIEDYINEF SVRKCHTCQNGGTVILMDGKCLCACPFKFEGIACEISKQKISEGLPALEFPNEK
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Partial
Tag Info
N-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage Condition
Store at -20°C, for extended storage, conserve at -20°C or -80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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. C9 is the pore-forming subunit of the MAC.
Gene References into Functions
The data supports the assumption that C9 gene expression may stimulate the expression of inflammatory (NLRP3) and angiogenic growth factors (VEGF) in retinal pigment epithelial cells.PMID:30090015
Serum-expressed apolipoprotein B-100 protein, C9 Complement, and gelsolin can be used for differential diagnosis of Barrertts esophagus and adenocarcinoma of esophagus.PMID:26404905
Data indicate that complement C9 binds to the ATPase domain of mortalin.PMID:24719326
Liver biopsy specimens from chronically hepatitis C virus-infected patients exhibited a lower level of C9 mRNA expression than liver biopsy specimens from unrelated disease or healthy control human liver RNA.PMID:23487461
the haploinsufficiency of C9, a terminal complement complex component, engenders reduced intraocular secretion of VEGF and decreased risk for CNV development.PMID:22190594
C9 and fucosylated form could serve as a useful marker for SQLC.PMID:21840429
It was concluded that variations in the complement component 9 gene are unlikely to influence clearance of chronic hepatitis B virus infection and hepatocellular carcinoma occurrence.PMID:21380615
Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9.PMID:21507937
These results suggested that the lack of membrane attack complex because of an Arg95Stop mutation of the complement component 9 gene predisposed patients to pathognomonic glomerulonephritis.PMID:21057849
provided evidence for the recognition of membrane-bound C9 on complement-lysed ghosts by an antibody specific for the helix-turn-helix fold.PMID:20153530
Data show that mortalin supports cancer cell resistance to complement-dependent cytotoxicity and suggest consideration of mortalin as a novel target for cancer adjuvant immunotherapy.PMID:19739077
The human complement C9 gene: structural analysis of the 5' gene region and genetic polymorphism studies.PMID:11881818
C9 binding is dependent on the N-terminal modules (thrombospondin type 1 and low-density lipoprotein receptor class A) of C8 alpha together with the C8 alpha membrane attack complex/perforin domain.PMID:12463754
Founder effect was demonstrated for the R95X mutation of the C9 gene in JapanesePMID:12596049
results indicate that the principal binding site for C9 lies within the MACPF domain of C8alphaPMID:16618117
analysis of the CD59-C9 binding interactionPMID:16844690