Recombinant Proteins

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SPINK7 Human

Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant

Recombinant human SPINK7, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 89 amino acids (20-85) with a molecular weight of 9.6 kDa. A 23 amino acid His-tag is fused to the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22345
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

SPINT2 Human

Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant

Recombinantly produced in E. coli, SPINT2 Human Recombinant is a single, non-glycosylated polypeptide chain comprising 195 amino acids (28-197 a.a.) with a molecular weight of 21.8 kDa. This protein is expressed with a 25 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22412
Source
Escherichia Coli.
Appearance
Clear solution, sterile filtered.

SPINT2 Human, Sf9

Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9

SPINT2, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) with a molecular mass of 20 kDa. On SDS-PAGE, the molecular size will appear at approximately 18-28 kDa. SPINT2 is expressed with a 6 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22479
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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.

Applications

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.

Role in the Life Cycle

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.

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