Equipped with world-leading technology platforms and professional scientific staff, Creative Biolabs is confident in offering a full range of complement therapeutic products and services for our clients all over the world. Based on our established insect expression system, the recombinant proenzyme C1r can be easily expressed. It has been shown that the PCR fragment size expected for C1r is 2,118 bp. Here, we describe the recombinant proenzyme C1r production protocol to promote your research.
Recombinant Proenzyme C1r Production Protocol
Fig.1 Flow chart of recombinant proenzyme C1r production. (Creative Biolabs)
Published Data
Fig.2 Recombinant C1s proteins characterized by SDS-PAGE analysis.1
C1s is a modular serine protease essential for cleaving C4 and C2, substrates of the complement's first component. The catalytic γ-B region contains a serine protease domain (SP), an activation peptide (ap), and two complement control protein (CCP) modules. Employing a baculovirus expression system, we generated recombinant truncated fragments missing either the initial CCP module (CCP2-ap-SP) or both CCP modules (ap-SP). Additionally, an aglycosylated CCP2-ap-SPag fragment was expressed with tunicamycin. These fragments were isolated, chemically characterized, and functionally analyzed alongside intact C1s. Upon activation by C1r, they exhibited esterolytic activity and reacted with the C1 inhibitor similarly to intact C1s.
As a forward-looking research as well as a leading custom service provider in the field of complement therapy, Creative Biolabs has won a good reputation among our worldwide customers for accomplishing numerous challenging projects. Our service portfolio includes therapeutic antibodies, serine protease inhibitors, soluble complement regulators, complement component inhibitors, as well as anaphylatoxin receptor antagonists, and other small molecules.
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Please note that our protocols are only for your reference!
Reference
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Rossi, Véronique, et al. "Baculovirus-mediated expression of truncated modular fragments from the catalytic region of human complement serine protease C1s: evidence for the involvement of both complement control protein modules in the recognition of the C4 protein substrate." Journal of Biological Chemistry 273.2 (1998): 1232-1239. Distributed under Open Access license CC BY 4.0, without modification.
For Research Use Only.
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