The Complement System, An Innate Immunity Station

The Complement System occupies a unique position among early cellular sensors, acting directly on the surface of triggering cells or substances to coordinate downstream cellular humoral immune responses. This makes this system a critical part of the immune cascade, contributing to both innate immune responses, including:

Local inflammation for removal and killing of pathogens
Signaling and influencing of T and B-cell biology

As a global regulator of immunity and tissue homeostasis, the Complement System has become an interesting, yet complex pharmacological target, contributing a network that contributes to pathogenesis in various inflammatory and neurodegenerative diseases, as well as, cancers.

Overall, the Complement-targeted therapies has been a very active field in recent years. Potent complement inhibitors are now available and increasingly used in approved and off-label indications that demonstrate the therapeutic potential of complement control.

Complement activation is implicated in numerous diseases

Complement activation is implicated in numerous diseases

https://doi.org/10.1016/j.molimm.2019.07.030

 Anti-complement drugs currently in clinical development

Anti-complement drugs currently in clinical development

https://doi.org/10.1016/j.molimm.2019.07.030

A better understanding of the complement's structure, function, and biological role will support our complement-based understanding to contribute to treating inflammation, neurodegenerative diseases, and cancers. Complement-targeted drugs that intervene at the signaling cascade level can help to better tailor therapeutic strategies and allow such strategies to be applied to a wider range of indications. To assist with research h into the Complement system, ACROBiosystems has developed a series of recombinant complement proteins expressed by HEK293 Cells, including C2, C3, C5, C5a and complement factor D (CFD).

Product Features

Comprehensive catalog of Complement products are available

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Native conformation, various species, free protocols available

High biological activity verified by ELISA and cell-based assay

Product List

Complement C5
Complement C5a
Complement C3
Complement C3a
Complement C2
Complement C1S
Complement Factor B
Complement Factor D

Verification Data

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

The purity of Human Complement C5a, Fc Tag (Cat. No. C5A-H525a) is more than 90% and the molecular weight of this protein is around 80-90 kDa verified by SEC-MALS.

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

The purity of Cynomolgus Complement C3, His Tag (Cat. No. CO3-C52H5) is more than 95% and the molecular weight of this protein is around 168-205 kDa verified by SEC-MALS.

High bioactivity verified by antibody binding

High bioactivity verified by antibody binding

Immobilized Human Complement C5, His Tag (Cat. No. CO5-H52Ha) at 2 μg/mL (100 μL/well) can bind Eculizumab Biosimilar with a linear range of 0.1-4 ng/mL (Routinely tested).

High bioactivity verified by antibody binding

Immobilized Human Complement C5a, His Tag (Cat. No. C5A-H51H9) at 5 μg/mL (100 μL/well) can bind Monoclonal Anti-Human C5a Human Antibody, Human IgG1 with a linear range of 0.1-4 ng/ml (QC tested).

High bioactivity verified by cell-based assay

High bioactivity verified by cell-based assay

Human Complement C5a, Tag Free (Cat. No. C5A-H5116) induce N-acetyl-β-D-glucosaminidase release from differentiated U937 cells. The ED50 for this effect is 0.215-0.323 μg/mL (Routinely tested).

Reference

  • 1. King B C, Blom A M. Intracellular complement: Evidence, definitions, controversies, and solutions[J]. Immunological Reviews, 2023, 313(1): 104-119.

  • 2. Zelek W M, Xie L, Morgan B P, et al. Compendium of current complement therapeutics[J]. Molecular immunology, 2019, 114: 341-352.

  • 3. Lubbers R, Van Essen M F, Van Kooten C, et al. Production of complement components by cells of the immune system[J]. Clinical & Experimental Immunology, 2017, 188(2): 183-194.

  • 4. Ricklin D, Lambris J D. New milestones ahead in complement-targeted therapy[C]//Seminars in immunology. Academic Press, 2016, 28(3): 208-222.

FAQ

Q

Which complement proteins should I select for studying different activation pathways?

C1s and C2 are relevant to the classical pathway, while Complement Factor B and Factor D are key components of the alternative pathway. C3 is the central convergence point, whereas C5 and C5a participate in terminal pathway activation and inflammatory signaling. Target selection should reflect the pathway stage being investigated.
Q

What are the experimental differences among C3, C3a, C5, and C5a?

C3 and C5 are precursor proteins used in antibody-binding, cleavage-mechanism, and complement-inhibitor studies. C3a and C5a are cleavage-derived inflammatory mediators suitable for receptor-binding, inflammatory-signaling, and cell-based assays. C5a is particularly potent in chemotaxis and immune-cell activation.
Q

Which complement protein format should I choose for ELISA, SPR, or cell-based assays?

His-tagged proteins support routine capture and binding assays. Biotinylated proteins containing an Avitag™ enable controlled immobilization for SPR, BLI, and ELISA. Tag-free proteins are preferred for cell-based assays focused on native activity, while Fc-fused proteins can provide added stability for selected assay formats.
Q

Why should both binding and cell-based activity be evaluated for complement proteins?

Binding assays confirm interactions with antibodies or receptors, while cell-based assays determine whether the protein produces the expected biological response. For example, ACRO Human C5 binds Eculizumab Biosimilar, and tag-free Human C5a induces N-acetyl-β-D-glucosaminidase release from differentiated U937 cells.
Q

How should I choose among human, mouse, and cynomolgus complement proteins?

Human proteins are suitable for immunization, therapeutic antibody screening, and human-target studies. Mouse proteins support studies linked to mouse disease models, while cynomolgus proteins can be used for preclinical cross-species binding evaluation. Comparing homologous proteins across species helps assess candidate cross-reactivity during drug development.
  • Introduction
  • Product Features
  • Product List
  • Verification Data
  • Reference
  • FAQ