C1q-Based Inhibition of Hemolysis Protocol

Creative Biolabs is a recognized expert in the field of complement research. We are committed to the development of the life sciences, contributing leading analytical science and state-of-the-art analytical techniques for tailor-made solutions. More than 20 years of market experience and proven analytical methods ensure the highest quality of our complement-related assays. Here, we briefly summarize the C1q-based inhibition of hemolysis protocol for our customers all over the world.

Inhibition of C1q-Dependent Hemolysis

Flow chart of C1q-based inhibition of hemolysis protocol. (Creative Biolabs)

Fig.1 Flow chart of C1q-based inhibition of hemolysis protocol. (Creative Biolabs)

Published Data

 TsCRTΔ inhibits the initiation of the classical complement pathway through binding to C1q. Fig.2 TsCRTΔ impedes the classical complement pathway initiation via C1q binding.1

Earlier research identified that Trichinella spiralis, a tissue-dwelling helminth, secretes calreticulin (TsCRT) which binds to C1q, inhibiting the classical complement pathway. In this study, researchers employed X-ray crystallography to elucidate the structure of a truncated version, TsCRTΔ—the first helminth-derived CRT structure. To assess if TsCRTΔ retained the complement modulation ability of its full-length counterpart, researchers conducted biochemical and hemolysis assays. Electron microscopy verified the integrity of C1q, revealing its tulip-like structure with six heterotrimers each containing collagen-like and globular regions. Binding assays demonstrated that TsCRTΔ has a stronger C1q affinity than TsCRT, effectively inhibiting complement activation by binding C1q and preventing membrane attack complex formation.

Various complement products are available at Creative Biolabs, such as natural complement proteins, highly specific antibodies as well as complement inhibitors. After decades of development and expansion, Creative Biolabs has gradually gained a high reputation in the complement field. With the highly specialized technical capabilities and expertise of complement, we are fully prepared and capable to provide complement testing services in the rapidly developing complement field, such as complement activity testing and genetic testing.

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Reference

  1. Jia, Zhihui, et al. "Crystal structure of Trichinella spiralis calreticulin and the structural basis of its complement evasion mechanism involving C1q." Frontiers in Immunology 15 (2024): 1404752. Distributed under Open Access license CC BY 4.0, without modification.
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