Product Overview Complement C1 Peptide Inhibitor-PIC1 is a highly potent C1 inhibitor which can inhibit ~90% complement activity in a hemolytic assay at Conc. 0.77mM. This inhibitor specifically inhibits the classical and lectin pathways of complement by binding to C1q, it also can bound to the lectin pathway initiator molecule MBL as well as the ficolins H, M and L.
Complement C1q, a 460 kDa hexameric glycoprotein, is the first recognition subcomponent of the complement classical pathway. This protein is made up of 18 polypeptide chains, consisting of 9 non-covalently linked subunits having 6 of A, B, and C chains (Fig.1). These chains contain three different domains which are a short N-terminal region (3-9 residues), a collagen region having 81 residues, and a C-terminal globular (gC1q) domain of about 185 residues. C1q is able to bind many antibodies and ligands, including IgG, IgM, CRP, phosphatidylserine (PS), HIV-1, HTLV-1, as well as some receptors such as integrin α2β1 and calreticulin-CD91.
C1q has a variety of complement and non-complement functions. Firstly, C1q can bind a range of ligands derived from self, non-self, and altered self and modulate the functions of immune and non-immune cells including dendritic cells and microglia. Moreover, C1q is associated with the clearance of apoptotic cells and subsequent B cell tolerance. Previous research has demonstrated that C1q plays a crucial role in pregnancy where its deficiency and dysregulation can have adverse effects, resulting in missed abortion, preeclampsia, or spontaneous loss, and infections. In addition, C1q is generated in the central nervous system and has a protective role against pathogens and possible inflammatory functions while interacting with aggregated proteins leading to neurodegenerative diseases.
Fig.1 Structure of C1q.1
C1q Functional Service
Creative Biolabs offers an extensive collection of products focused on C1q, encompassing anti-C1q antibodies, ELISA kits, C1q proteins, C1q blocking peptides, and reporter vectors containing C1q clones. These meticulously engineered reagents are crucial in elucidating the interactions between C1q proteins and various molecules thereby significantly advancing research efforts to develop therapeutic strategies for numerous diseases.
Fig.2 Schematic diagram of C1q and C3d binding assays.2
Heart transplantation (HTx) outcomes face challenges due to antibody-mediated rejection (AMR), which undermines cardiac graft longevity despite advancements in immunosuppressive treatment. Researchers emphasize the detrimental role of anti-donor-specific antibodies (DSAs), particularly against donor human leukocyte antigen (HLA), in heart graft failure, causing hemodynamic issues and potential recipient mortality. The classical complement pathway is activated when alloantibodies bind HLA antigens on graft cells, recruiting C1q, a critical component in forming the membrane attack complex. The C1q binding single antigen beads (SABs) assay identifies HLA antibodies binding to C1q, utilizing heat-inactivated serum incubated with recombinant C1q and PE-conjugated anti-C1q antibodies. These assays offer a novel supplementary approach for guiding immunotherapy decisions.
Creative Biolabs delivers an extensive suite of C1q-related functional services, encompassing thorough interaction analyses and a variety of specialized assessments. These expertly customized services are designed to support researchers in pushing the boundaries of their scientific inquiries and clinical endeavors.
References
Ain, Danyaal, et al. "The role of complement in the tumor microenvironment." Faculty Reviews 10 (2021). Distributed under Open Access license CC BY 4.0, without modification.
Watanabe, Takuya, and Norihide Fukushima. "Novel Diagnostic and Therapeutic Approach to Antibody-Mediated Rejections in Heart Transplantation." Immunosuppression. IntechOpen, 2020.
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Datasheet
Fig.1 Structure of C1q.1
Fig.2 Schematic diagram of C1q and C3d binding assays.2
