Mouse Anti-C9 Recombinant Antibody (887025) (CBMAB-C2760-LY)

Name: Mouse Anti-C9 Recombinant Antibody (887025)
SKU: CBMAB-C2760-LY
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

887025

Application

Immunogen

HEK293 human embryonic kidney cell line transfected with human Complement Component C9 Met1-Lys559.

Host Species

Mouse

Specificity

Human

Antibody Isotype

IgG1

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
WB	1 µg/ml

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

Format

Lyophilized

Buffer

PBS, Trehalose

Preservative

None

Purity

> 95% Purity determined by SDS-PAGE.

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

complement C9

Entrez Gene ID

Human	735
Pig	100037951
Baboon	101010222
Horse	100034183

UniProt ID

Human	P02748
Pig	F1SMJ6
Baboon	A0A096N4A4
Horse	P48770

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

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Isotype control

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

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