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Mouse Anti-C9 Recombinant Antibody (CBFYC-0678) (CBMAB-C0732-FY)

This product is mouse antibody that recognizes C9. The antibody CBFYC-0678 can be used for immunoassay techniques such as: ELISA, WB, IHC, IF.
See all C9 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYC-0678
Antibody Isotype
IgG1, k
Application
ELISA, WB, IHC, IF

Basic Information

Immunogen
Complement factor C9
Specificity
Human
Antibody Isotype
IgG1, k
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
complement C9
Introduction
This gene encodes the final component of the complement system. It participates in the formation of the Membrane Attack Complex (MAC)
Entrez Gene ID
735
UniProt ID
P02748
Alternative Names
C9D; ARMD15
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:9634479, PubMed:9212048, PubMed:26841934).
C9 is the pore-forming subunit of the MAC (PubMed:4055801, PubMed:26841934, PubMed:30111885).
Biological Process
Cell killing Source: UniProtKB
Complement activation Source: Reactome
Complement activation, alternative pathway Source: UniProtKB-KW
Complement activation, classical pathway Source: UniProtKB-KW
Cytolysis Source: UniProtKB-KW
Protein homooligomerization Source: UniProtKB
Regulation of complement activation Source: Reactome
Cellular Location
Secreted; Target cell membrane. Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore.
Involvement in disease
Complement component 9 deficiency (C9D): A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Some patients may develop dermatomyositis.
Macular degeneration, age-related, 15 (ARMD15): A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
PTM
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).

Li, L., Shen, Y., Xu, X., Yang, W., & Li, J. (2021). Tracing and exploring the evolutionary origin and systematic function of fish complement C9. Molecular Genetics and Genomics, 296(3), 665-676.

David, M., Moodley, J., & Naicker, T. (2021). The function of adipsin and C9 protein in the complement system in HIV-associated preeclampsia. Archives of gynecology and obstetrics, 1-7.

Chantaraamporn, J., Champattanachai, V., Khongmanee, A., Verathamjamras, C., Prasongsook, N., Mingkwan, K., ... & Svasti, J. (2020). Glycoproteomic Analysis Reveals Aberrant Expression of Complement C9 and Fibronectin in the Plasma of Patients with Colorectal Cancer. Proteomes, 8(3), 26.

Hua, X. T., Fan, K., Zhang, Z., Li, X., Xia, Y., Liu, P. F., & Liu, Y. (2020). Characterization and expression analysis of the C8α and C9 terminal complement components from pufferfish (Takifugu rubripes). Developmental & Comparative Immunology, 106, 103634.

Fu, Y. W., Zhu, C. K., Zhang, Q. Z., & Hou, T. L. (2019). Molecular characterization, expression analysis, and ontogeny of complement component C9 in southern catfish (Silurus meridionalis). Fish & shellfish immunology, 86, 449-458.

Hollborn, M., Ackmann, C., Kuhrt, H., Doktor, F., Kohen, L., Wiedemann, P., & Bringmann, A. (2018). Osmotic and hypoxic induction of the complement factor C9 in cultured human retinal pigment epithelial cells: regulation of VEGF and NLRP3 expression. Molecular vision, 24, 518.

Kremlitzka, M., Geerlings, M. J., De Jong, S., Bakker, B., Nilsson, S. C., Fauser, S., ... & Blom, A. M. (2018). Functional analyses of rare genetic variants in complement component C9 identified in patients with age-related macular degeneration. Human molecular genetics, 27(15), 2678-2688.

Franc, V., Yang, Y., & Heck, A. J. (2017). Proteoform profile mapping of the human serum complement component C9 revealing unexpected new features of N-, O-, and C-glycosylation. Analytical chemistry, 89(6), 3483-3491.

Taylor, R. P., Lindorfer, M. A., Cook, E. M., Beurskens, F. J., Schuurman, J., Parren, P. W., ... & Morgan, B. P. (2017). Hexamerization-enhanced CD20 antibody mediates complement-dependent cytotoxicity in serum genetically deficient in C9. Clinical Immunology, 181, 24-28.

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For research use only. Not intended for any clinical use.

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