Recombinant Proteins
Product List
SERPINA8 Human
Serpin Peptidase Inhibitor, Clade A Member 8 Human Recombinant
The Human SERPINA8 is purified by proprietary chromatographic techniques.
SERPINA9 Mouse
Serpin Peptidase Inhibitor, Clade A Mouse Recombinant
SERPINA9 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
SERPINB2 Human
Serpin Peptidase Inhibitor, Clade B Member 2 Human Recombinant
SERPINB2 Human, His
Serpin Peptidase Inhibitor, Clade B Member 2 Human Recombinant, His Tag
SERPINB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SERPINB3 Human
Serpin Peptidase Inhibitor, Clade B Member 3 Human Recombinant
SERPINB4 Human
Serpin Peptidase Inhibitor, Clade B Member 4 Human Recombinant
SERPINB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SERPINB5 Human
Serpin Peptidase Inhibitor, Clade B Member 5 Human Recombinant
The SERPINB5 Human is purified by proprietary chromatographic techniques.
SERPINB5 Human, His
Serpin Peptidase Inhibitor, Clade B Member 5 Human Recombinant, His tag
SERPINB5 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 395 amino acids (1-375 a.a.) and having a molecular mass of 44.2 kDa.
The SERPINB5 is purified by proprietary chromatographic techniques.
SERPINB8 Human
Serpin Peptidase Inhibitor, Clade B Member 8 Human Recombinant
SERPINB8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SERPINC1 Human, Sf9
Serpin Peptidase Inhibitor, Clade C Member 1 Human Recombinant, Sf9
SERPINC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (33-464a.a.) and having a molecular mass of 50.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). SERPINC is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Introduction
Serpins, or serine protease inhibitors, are a superfamily of proteins that inhibit proteases by undergoing a significant conformational change. Initially identified for their role in inhibiting chymotrypsin-like serine proteases, serpins are now known to be present in all kingdoms of life . They are classified into clades based on their phylogenetic relationships, with human serpins divided into nine clades (A-I) .
Serpins exhibit a wide range of biological properties. They are relatively large proteins, typically consisting of 330-500 amino acids . In humans, 37 serpins have been identified, with 30 functioning as protease inhibitors . Serpins are found in various tissues throughout the body, both extracellularly and intracellularly . They play roles in processes such as inflammation, immune function, tumorigenesis, blood clotting, dementia, and cancer metastasis .
The primary function of serpins is to inhibit proteases, thereby regulating proteolytic cascades. This regulation is crucial for processes such as coagulation, fibrinolysis, inflammation, and angiogenesis . Serpins also play significant roles in immune responses and pathogen recognition, helping to maintain immune homeostasis . Some serpins have non-inhibitory functions, such as hormone transport and molecular chaperoning .
Serpins inhibit their target proteases through a unique mechanism involving a large conformational change. This change disrupts the active site of the protease, rendering it inactive . Serpins can inhibit multiple proteases, but only in their active state . This mechanism contrasts with the more common competitive inhibition, where inhibitors bind to and block access to the protease active site . The conformational change mechanism, while effective, makes serpins vulnerable to mutations that can lead to misfolding and the formation of inactive polymers .
The expression and activity of serpins are tightly regulated at multiple levels. Transcriptional regulation involves various factors that control the expression of serpin genes . Post-translational modifications, such as glycosylation and phosphorylation, also play crucial roles in modulating serpin activity . Additionally, serpins can be regulated by other proteins and molecules that influence their stability and function .
Serpins have significant applications in biomedical research, diagnostics, and therapeutics. They are used as models to study protein folding and conformational diseases . In diagnostics, serpins serve as biomarkers for various diseases, including emphysema and liver cirrhosis . Therapeutically, serpins are being developed to treat conditions caused by serpin deficiencies, such as antithrombin and alpha-1 antitrypsin deficiencies . Recombinant serpins and serpin-derived peptides are also being explored for their potential to modulate immune responses and treat inflammatory diseases .
Throughout the life cycle, serpins play critical roles in development, aging, and disease. During development, serpins regulate processes such as tissue remodeling and cell migration . In adulthood, they maintain homeostasis by controlling protease activity in various physiological processes . As organisms age, changes in serpin expression and function can contribute to age-related diseases, such as dementia and cancer . Genetic mutations in serpins can lead to serpinopathies, which are associated with severe pathologies like emphysema and liver cirrhosis .
