Recombinant Proteins
Product List
SERPINA1
Alpha 1 Antitrypsin Human
SERPINA1 Human
Alpha 1 Antitrypsin Human Recombinant
The SERPINA1 protein is purified by proprietary chromatographic techniques.
SERPINA1 Human, Active
Alpha-1 Antitrypsin, Active Human Recombinant
The SERPINA1 protein is purified by proprietary chromatographic techniques.
SERPINA3
Alpha-1 AntiChymotrypsin Human Recombinant
The SERPINA3 is purified by proprietary chromatographic techniques.
SERPINA3 Human
Alpha-1 AntiChymotrypsin Human
SERPINA4 Human
Kallistatin Human Recombinant
SERPINA5 Human
Serpin Peptidase Inhibitor Clade A Member 5 Human Recombinant
The SERPINA5 is purified by proprietary chromatographic techniques.
SERPINA5 Human, Active
Serpin Peptidase Inhibitor, Clade A Member 5 Human Recombinant, Active
SERPINA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (20-406 a.a) and having a molecular mass of 45.9kDa.
SERPINA5 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SERPINA6 Human
Serpin Peptidase Inhibitor, Clade A Member 6 Human Recombinant
SERPINA6 Human Recombinant is a single, glycosylated polypeptide chain containing 389 amino acids (23-405a.a) and having a molecular mass of 43.5kDa (calculated). SERPINA6 is fused to a 6 a.a His tag at C-terminal.
HEK293 cells.
SERPINA7 Human
Serpin Peptidase Inhibitor, Clade A Member 7 Human
Human Serpin Peptidase Inhibitor, Clade A Member 7 Protein produced in Human plasma having a molecular mass of approximately 55kD.
Human serum.
Sterile Filtered White lyophilized (freeze-dried) powder.
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 .
