Prokaryotic expression systems offer advantages such as high expression levels, simple operation, short production cycles, suitability for large-scale high-density cultivation, and low costs. However, for full-length antibodies and glycoprotein-based biopharmaceuticals, factors such as polypeptide chain folding, disulfide bond formation, and the presence or type of glycosylation often significantly influence the synthesis, secretion, biological activity, in vivo stability, and immunogenicity of the expressed products.

Compared to other eukaryotic expression systems, proteins produced from target genes in mammalian cells closely resemble native proteins in terms of structure and glycosylation patterns, and they are capable of correctly assembling into multi-subunit proteins.

· No endogenous endotoxin production;

· Capable of secretory expression;

· Possesses various post-translational processing capabilities, such as complex N-linked glycosylation and accurate O-linked glycosylation;

· Proteins expressed in mammalian cells most closely resemble native proteins in terms of molecular structure, physicochemical properties, and biological function.

· High cost-effectiveness;

· Short lead time: delivery in as little as 35 working days;

· High yield, reaching up to 100 mg/L.

Risk-free custom service: no charge unless successful.

Note: This risk-free custom protein service applies only to proteins of 800 amino acids or fewer. If you require the expression of a protein exceeding 800 amino acids, we will charge on a step-by-step basis.