Human C2 Recombinant Protein (C-Fc) (HY106021)

Name: Human C2 Recombinant Protein (C-Fc)
Brand: abinScience
SKU: HY106021
Price: 298 USD
Availability: InStock

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Overview

Catalog No.	HY106021
Description	Recombinant Human C2 Protein, C-Fc (HY106021) expressed in Mammalian Cells, spanning Met1-Leu752. Purity: >90% by SDS-PAGE. Highlights ●Fc Fusion — Enhanced stability with Protein A/G purification compatibility. ●Mammalian Expression — Proper folding and native glycosylation. ●High Purity — >90% purity verified by SDS-PAGE.
Expression system	Mammalian cells
Accession	P06681
Protein length	Met1-Leu752
Applications	ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
Species	Homo sapiens (Human)
Nature	Recombinant
Endotoxin level	Please contact with the lab for this information.
Purity	>90% as determined by SDS-PAGE.
Predicted molecular weight	109.67 kDa
Form	Lyophilized
Storage buffer	Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
Reconstitution	Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping	In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage	Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate Names	C2, C3/C5 convertase, Complement C2, Complement C2a, EC:3.4.21.43, Serine protease complement C2b
Background	Complement C2 is a ~83 kDa protein. Precursor of the catalytic component of the C3 and C5 convertase complexes, which are part of the complement pathway, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. Component C2 is part of the classical, lectin and GZMK complement systems. 1. Rawal, N. et al. (2003) The Journal of biological chemistry 278, 38476-83. PMID: 12878586 2. Milder, FJ. et al. (2006) Structure (London, England : 1993) 14, 1587-97. PMID: 17027507 3. Rawal, N. et al. (2008) The Journal of biological chemistry 283, 7853-63. PMID: 18204047 4. Donado, CA. et al. (2025) Nature 641, 211-221. PMID: 39914456 5. Lan, F. et al. (2025) Nature 638, 490-498. PMID: 39814882 6. Héja, D. et al. (2012) Proceedings of the National Academy of Sciences of the United States of America 109, 10498-503. PMID: 22691502
Note	For research use only