Recombinant Proteins

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SERPINA3

Alpha-1 AntiChymotrypsin Human Recombinant

This product consists of recombinant human SERPINA3, containing a 20 amino acid His tag fused at its N-terminus. It is produced in E.Coli and exists as a single, non-glycosylated polypeptide chain with a molecular weight of 47.6 kDa. The protein encompasses 421 amino acids, spanning from residue 24 to 423. Purification of SERPINA3 is achieved using proprietary chromatographic techniques, resulting in a highly pure product.
Shipped with Ice Packs
Cat. No.
BT22806
Source
Escherichia Coli.
Appearance
Clear and colorless solution, sterilized by filtration.

SERPINA3 Human

Alpha-1 AntiChymotrypsin Human

Human Alpha-1 AntiChymotrypsin is a protein with a molecular mass of 68 kDa, produced from normal human serum.
Shipped with Ice Packs
Cat. No.
BT22902
Source
Human Serum.
Appearance
Sterile Filtered White lyophilized powder.

SERPINA7 Human

Serpin Peptidase Inhibitor, Clade A Member 7 Human

This is a purified protein, called SERPINA7, that is naturally found in human blood. It is approximately 55 kilodaltons in size.

Shipped with Ice Packs
Cat. No.
BT23596
Source

Human serum.

Appearance

It appears as a white powder that has been freeze-dried and sterilized through filtration.

SERPINA8 Human

Serpin Peptidase Inhibitor, Clade A Member 8 Human Recombinant

Recombinant Human SERPINA8 is produced in HEK cells. It is a single-chain polypeptide containing 462 amino acids (a.a 34-485), with a C-terminal 2 a.a linker and an 8 a.a Flag tag. This protein is glycosylated and has a calculated molecular mass of 51.0 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23670
Source
HEK 293.
Appearance
White lyophilized powder.

SERPINA9 Mouse

Serpin Peptidase Inhibitor, Clade A Mouse Recombinant

Recombinant Mouse SERPINA9, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 401 amino acids (26-418 a.a) with a molecular mass of 45.2kDa (appears at approximately 50-70kDa on SDS-PAGE). It has an 8 amino acid His-tag at its C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23766
Source
Sf9, Baculovirus cells.
Appearance
A sterile, colorless solution.

SERPINB2 Human

Serpin Peptidase Inhibitor, Clade B Member 2 Human Recombinant

Recombinant human SERPINB2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 415 amino acids. It has a molecular weight of 46.6 kDa.
The purification of SERPINB2 is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23872
Source
Escherichia Coli.
Appearance
The product appears as a sterile, filtered, white lyophilized (freeze-dried) powder.

SERPINB5 Human

Serpin Peptidase Inhibitor, Clade B Member 5 Human Recombinant

Recombinant human SERPINB5, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 375 amino acids. It has a molecular weight of 42.2 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24313
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SERPINB5 Human, His

Serpin Peptidase Inhibitor, Clade B Member 5 Human Recombinant, His tag

Recombinant human SERPINB5, with a 20-amino acid His tag at the N-terminus, is produced in E. coli. This single, non-glycosylated polypeptide chain consists of 395 amino acids (residues 1-375) and has a molecular weight of 44.2 kDa. Purification of SERPINB5 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24399
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SERPINB8 Human

Serpin Peptidase Inhibitor, Clade B Member 8 Human Recombinant

Recombinant Human SERPINB8, produced in E. coli, is a single polypeptide chain without any glycosylation modifications. It consists of 397 amino acids (specifically, amino acids 1 to 374) and has a molecular weight of 45.2 kDa. For purification and detection purposes, a 23 amino acid His-tag is attached to the N-terminus of the protein. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24464
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

SERPINC1 Human, Sf9

Serpin Peptidase Inhibitor, Clade C Member 1 Human Recombinant, Sf9

Recombinant human SERPINC1, expressed in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. This protein consists of 441 amino acids (residues 33-464), has a molecular weight of 50.1 kDa, and appears as a band at approximately 50-70 kDa on SDS-PAGE. It is tagged at the C-terminus with a 9-amino acid His tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24547
Source

Sf9, Baculovirus cells.

Appearance
Sterile, colorless solution.
Definition and Classification

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) .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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 .

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