Recombinant Proteins
Product List
SPINK7 Human
Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant
SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SPINT2 Human
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant
SPINT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SPINT2 Human, Sf9
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9
Introduction
Serine peptidase inhibitors, commonly known as serpins, are a superfamily of proteins that inhibit serine proteases. These inhibitors are found across all kingdoms of life, including animals, plants, bacteria, and archaea . Serpins are classified based on their structure and function, with the majority inhibiting serine proteases, while some inhibit other protease classes such as cysteine proteases . They are named using the format SERPINXy, where X represents the clade and y the number within that clade .
Serpins exhibit a wide range of biological properties. They are relatively large molecules, typically consisting of 330-500 amino acids . Serpins are expressed in various tissues and have diverse expression patterns. For instance, humans have 36 serpin-like genes, while other organisms like Drosophila and Arabidopsis thaliana have 13 and 29, respectively . These proteins are central in controlling proteolytic cascades, including coagulation pathways .
The primary biological functions of serpins include regulating proteolytic processes such as coagulation, fibrinolysis, inflammation, and immune responses . They play a crucial role in pathogen recognition and immune responses by inhibiting proteases that pathogens use to invade host tissues . Additionally, serpins are involved in various physiological processes, including cell adhesion, apoptosis, and tumor suppression .
Serpins act as irreversible, suicide inhibitors by trapping an intermediate of the protease’s catalytic mechanism . This unique mechanism involves a significant conformational change that disrupts the protease’s active site . Some serpins also inhibit other protease classes, such as cysteine proteases, and are termed "cross-class inhibitors" . They interact with various binding partners and initiate downstream signaling cascades that regulate cellular processes .
The expression and activity of serpins are tightly regulated through multiple mechanisms. Transcriptional regulation involves controlling the mRNA levels of serpin genes, while post-translational modifications such as glycosylation and phosphorylation modulate their activity . Additionally, serpins are often released in inactive forms or zymogens, which are activated through proteolytic cleavage . This ensures precise control over their inhibitory functions.
Serpins have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. They are used as drug targets for various diseases, including cancer, cardiovascular disorders, and inflammatory diseases . Serpins are also employed in diagnostic assays to detect protease activity and in therapeutic interventions to modulate protease functions . Their ability to regulate proteolytic processes makes them valuable in developing treatments for conditions involving excessive protease activity.
Throughout the life cycle, serpins play essential roles from development to aging and disease. During development, they regulate processes such as cell differentiation and tissue remodeling . In adulthood, serpins maintain homeostasis by controlling proteolytic activities involved in immune responses, coagulation, and tissue repair . In aging and disease, dysregulation of serpin activity can lead to conditions such as emphysema, thrombosis, and cancer . Understanding the role of serpins in these processes is crucial for developing therapeutic strategies to mitigate their impact on health.
