TEV

Tobacco Etch Virus Protease Recombinant

Recombinant TEV Protease (rTEV), a site-specific protease derived from E. coli, facilitates the removal of affinity tags from fusion proteins. rTEV recognizes the seven-amino-acid sequence Glu-Asn-Leu-Tyr-Phe-Gln-Gly, cleaving between Gln and Gly. While the optimal cleavage temperature is 30°C, the enzyme remains active at temperatures as low as 4°C. rTEV is engineered with a His tag and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4737
Source
Escherichia Coli.
Appearance
Sterile liquid.

Welqut Protease

Welqut Protease Staphylococcus aureus Recombinant

The recombinant Welqut Protease is a single, non-glycosylated polypeptide chain with a molecular weight of 22kDa, composed of 204 amino acids. Its purification is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT4825
Source

Escherichia Coli.

Appearance
A colorless solution that has undergone sterile filtration.

Welqut Protease, His

Welqut Protease Staphylococcus aureus Recombinant, His Tag

Welqut Protease Recombinant is a single-chain polypeptide, devoid of any glycosylation. It comprises 210 amino acids, culminating in a molecular weight of 22kDa. A 6-amino acid His tag is fused to the C-terminus of the protease to facilitate purification, which is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT4924
Source

Escherichia Coli. 

Appearance

The product is a sterile, colorless solution that has been filtered for sterility.

LGMN Mouse

Legumain Mouse Recombinant

Produced in Sf9 Baculovirus cells, LGMN is a single, glycosylated polypeptide chain consisting of 426 amino acids (18-435a.a.) with a molecular weight of 48.6kDa. This protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT4010
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution that has been sterilized by filtration.

Protease

Recombinant Protease

Protease Recombinant is a fusion protein composed of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. Its primary function is to recognize and cleave a specific set of sequences containing the core amino acid sequence Leu-Phe-Gln/Gly-Pro, specifically targeting the bond between Gln and Gly residues. It's important to note that substrate recognition and cleavage might be influenced by the fusion protein's primary, secondary, and tertiary structures. The purification process of this recombinant protease involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4103
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PRSS22 Mouse

Protease Serine 22 Mouse Recombinant

Recombinant Mouse PRSS22, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It consists of 283 amino acids (33-307) with a molecular mass of 31.1 kDa. Note: On SDS-PAGE, the molecular size will appear between 28-40 kDa. The protein is fused to an 8 amino acid His-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4167
Source
Sf9, Baculovirus cells.
Appearance
Clear, sterile-filtered solution.

PRSS28 Mouse

Protease Serine 28 Mouse Recombinant

Recombinant Mouse PRSS28, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 256 amino acids (27-274a.a.) and has a molecular mass of 28.7 kDa. On SDS-PAGE, the apparent molecular size will be approximately 28-40 kDa. PRSS28 is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4235
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

PRSS3 Human

Protease Serine 3 Human Recombinant

Recombinant human PRSS3, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 247 amino acids (81-304) with a molecular mass of 26.0 kDa. This protein is fused to a 23 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4335
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

PRSS3 Human, HEK

Protease Serine 3 Human Recombinant, HEK

PRSS3 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 238 amino acids (16-247 a.a.) and having a molecular mass of 26kDa. PRSS3 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4416
Source

HEK293 Cells.

Appearance
Sterile, colorless, and filtered solution.

PRSS3 Human, sf9

Recombinant Human Protease Serine 3, sf9

PRSS3, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain with a molecular weight of 25.3 kDa (based on amino acid sequence; 81-304a.a.). On SDS-PAGE, it appears at a size of approximately 28-40 kDa. The recombinant protein is expressed with a 6-amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4505
Source
Sf9, Insect cells.
Appearance
The product is a sterile, colorless solution that has been filtered.
Definition and Classification

Proteases, also known as peptidases or proteinases, are enzymes that catalyze the hydrolysis of peptide bonds in proteins. They play a crucial role in various biological processes by breaking down proteins into smaller peptides or amino acids. Proteases are classified based on their catalytic mechanism into several categories:

  • Serine proteases: Utilize a serine residue in their active site.
  • Cysteine proteases: Employ a cysteine residue for catalysis.
  • Aspartic proteases: Use an aspartic acid residue.
  • Metalloproteases: Require a metal ion, usually zinc, for activity.
  • Threonine proteases: Utilize a threonine residue in their active site.
Biological Properties

Key Biological Properties:

  • Catalytic Activity: Proteases exhibit high specificity for their substrates, ensuring precise cleavage of peptide bonds.
  • Stability: They are stable under various physiological conditions, including different pH levels and temperatures.

Expression Patterns and Tissue Distribution:

  • Proteases are ubiquitously expressed in all living organisms, from bacteria to humans.
  • They are found in various tissues, including the digestive tract, blood, and immune cells.
  • Specific proteases are localized in particular cellular compartments, such as lysosomes, mitochondria, and the extracellular matrix.
Biological Functions

Primary Biological Functions:

  • Protein Digestion: Proteases break down dietary proteins into absorbable amino acids.
  • Cellular Regulation: They regulate cellular processes by activating or degrading key proteins.
  • Apoptosis: Proteases like caspases play a vital role in programmed cell death.

Role in Immune Responses and Pathogen Recognition:

  • Proteases are involved in the activation of immune cells and the processing of antigens for presentation to the immune system.
  • They help in the recognition and elimination of pathogens by degrading their proteins.
Modes of Action

Mechanisms with Other Molecules and Cells:

  • Proteases interact with substrates through their active sites, where they catalyze the cleavage of peptide bonds.
  • They can form complexes with inhibitors or activators that modulate their activity.

Binding Partners and Downstream Signaling Cascades:

  • Proteases often bind to specific inhibitors that regulate their activity, such as serpins for serine proteases.
  • They can initiate downstream signaling cascades by cleaving and activating other proteins, such as in the blood coagulation pathway.
Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity:

  • Transcriptional Regulation: Protease gene expression is controlled by transcription factors that respond to cellular signals.
  • Post-Translational Modifications: Proteases can be activated or inhibited by modifications such as phosphorylation, glycosylation, and ubiquitination.
Applications

Biomedical Research:

  • Proteases are used to study protein function and structure by selectively cleaving target proteins.

Diagnostic Tools:

  • Protease activity assays are employed in diagnostic tests for diseases such as cancer and infectious diseases.

Therapeutic Strategies:

  • Protease inhibitors are used as drugs to treat conditions like hypertension, HIV, and cancer.
Role in the Life Cycle

Role Throughout the Life Cycle:

  • Development: Proteases are essential for tissue remodeling and organ development.
  • Aging: Changes in protease activity are associated with aging and age-related diseases.
  • Disease: Dysregulation of protease activity is linked to various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases.
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