Anti-C8G polyclonal antibody (DPABH-13092)


Host Species
Antibody Isotype
Species Reactivity
Synthetic peptide within Human C8G aa 56-105 (N terminal). The exact sequence is proprietary. (NP_000597).Sequence: VGSACRFLQEQGHRAEATTLHVAPQGTAMAVSTFRKLDGICWQVRQLYGD Database link: P07360


Application Notes
WB: 1 μg/ml.
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.


Alternative Names
C8G; complement component 8, gamma polypeptide; complement component C8 gamma chain; C8C; MGC142186
Entrez Gene ID
UniProt ID

Product Background

Amoebiasis; Complement and Coagulation Cascades; Complement and coagulation cascades; Complement cascade; Immune System;


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Hepatotoxicity and mechanism study of chrysophanol-8-O-glucoside in vitro


Authors: Lin, Longfei; Yuan, Fang; Liu, Yuling; Zhong, Ming; Xie, Tanggui; Ni, Jian; Li, Hui

To better understand the hepatotoxicity of anthraquinone glycosides, the hepatotoxicity of six anthraquinone glycosides was evaluated. The results show that chrysophanol-8-O-glucoside(C8G) has strong hepatotoxicity and can lead to increased LDH leakage and ROS, decreased GSH and MMP in L-02 hepatocytes. The results of C8G hepatotoxicity proteomics shows that, a total of 773 differentially expressed proteins were screened and analyzed using GO analysis and Pathway enrichment analysis. Our results show that C8G can lead to abnormal oxidative phosphorylation by inhibiting the function of mitochondrial complexes, resulting in decreased mitochondrial membrane potential (MMP), increased reactive oxygen species (ROS), and eventually resulting in mitochondrial damage and apoptosis. Western blot results verified the accuracy of quantitative proteomic results, and also evaluated the expression of Bax, caspase-3, -8, -9, Bcl-2, Cyt C in the mitochondria and cytosolic. The mitochondrial respiratory chain complexes activity assay result also confirmed that C8G could inhibit the activity of all mitochondrial complexes. The results of this study indicate that the hepatotoxicity mechanism of C8G is related to mitochondrial dysfunction, especially the mitochondrial complex function.

Side chain assisted nanotubular self-assembly of cyclic peptides at the air-water interface


Authors: Kwak, Byeongdo; Shin, Kwanwoo; Seok, Sangjun; Kim, Doseok; Ahmad, Farhan; Geckeler, Kurt E.; Seeck, Oliver H.; Seo, Young-Soo; Satija, Sushil K.; Kubik, Stefan

Langmuir monolayers of two artificial cyclic peptides with an alternating sequence of L-glutamic acid and 3-aminobenzoic acid subunits, a cyclohexapeptide (C6G) and a cyclooctapeptide (C8G), were investigated using a variety of techniques, including pi-A isotherms, in situ surface sum-frequency generation (SFG) and Brewster angle microscopy. The monolayers were also transferred onto a solid substrate by the Langmuir-Blodgett technique and characterized by grazing incident X-ray diffraction (GIXD), atomic force microscopy (AFM), and transmission electron microscopy (TEM). The investigations indicated that C6G forms 2D crystallite structures at the air-water interface, whereas no such structures were observed for C8G. Being amphiphilic, both peptides attain a horizontal orientation on the water surface after spreading. Surface compression causes the molecules to flip to a perpendicular state, thus minimizing the molecular area. The measurements also indicate that, in the perpendicular state, self-assembly of C6G leads to a tubular arrangement of the peptide rings. According to GIXD and TEM data, pairs of tubes arrange in a well defined and oriented order producing 2D crystals. Surface vibrational spectroscopic methods (sum-frequency generation and polarization modulation IR reflection-absorption) combined with molecular modeling gave insight into the arrangement of individual C6G molecules in the tubes. Overall, our results indicated that the tubular assembly of C6G is most likely due to intermolecular H-bonding between the CO group in the glutamic acid side chains and peptide NH group of a neighboring peptide ring.

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