Insect cell expression systems have emerged as a powerful tool for the production of recombinant proteins, particularly for applications requiring complex post-translational modifications.

Mammalian protein expression systems are now widely used in the biopharmaceutical industry for producing complex recombinant proteins. These systems use mammalian cell lines like Chinese hamster ovary (CHO) cells and human embryonic kidney (HEK) 293 cells.

Frozen section IHC is a technique that involves quickly freezing tissue samples and then using a cryostat to prepare ultrathin sections. These sections are subsequently stained with specific antibodies to target antigens. Compared with traditional paraffin - embedded section IHC, frozen section IHC has the advantages of being rapid and efficient and preserving more antigen activity. It is especially suitable for clinical situations that require rapid diagnosis and for the study of fresh tissue samples.

Pichia pastoris, a methylotrophic yeast, has emerged as a highly efficient and widely used eukaryotic host for the production of recombinant proteins. This system combines the advantages of eukaryotic post-translational modifications with the rapid growth and scalability of yeast-based expression systems, making it particularly suitable for the production of complex proteins that require glycosylation and other modifications for proper folding and functionality.

Escherichia coli (E. coli) is one of the most widely used prokaryotic expression systems for the production of recombinant proteins. Its popularity stems from several key advantages, including ease of genetic manipulation, rapid growth rate, and cost-effectiveness. E. coli has been extensively studied and optimized for protein expression, making it a cornerstone in both research and industrial applications.

Protein expression is a critical biological process that involves the synthesis, folding, localization, and regulation of proteins in response to the functional demands of the body. It represents the dynamic output of the genome, where specific proteins are produced to meet cellular and physiological needs

Antibody labeling, or antibody conjugation, involves attaching specific tags to antibodies to facilitate detection and measurement in various immunoassays.Labeling tag include biotin, fluorescent dyes, enzymes, or proteins.

Our innovative process for manufacturing recombinant antibodies involves cloning antibody genes into high-yield expression vectors and introducing these vectors into suitable host systems.

Antibody labeling, or antibody conjugation, involves attaching specific tags to antibodies to facilitate detection and measurement in various immunoassays.Labeling tag include biotin, fluorescent dyes, enzymes, or proteins.

Antibodies, also known as immunoglobulins (Ig), are a class of highly specific glycoproteins produced by the immune system, particularly by B lymphocytes, in response to antigenic stimulation. They are the core effector molecules of adaptive humoral immunity and play an irreplaceable role in defending against pathogen infections, clearing abnormal cells, and maintaining homeostasis within the body.