Product List

MME Human

Membrane Metalloendopeptidase Human Recombinant

MME Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 a.a.) and having a molecular mass of 80.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
MME is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21236
Source

Sf9, Insect cells.

Appearance
Sterile Filtered clear solution.

Aminopeptidase

Aminopeptidase Aeromonas Recombinant

The 29 kDa Aeromonas Aminopeptidase is produced by genetic engineering and can be used for physical & structural investigations, sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at –X- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins.
Shipped with Ice Packs
Cat. No.
BT21283
Source
Aeromonas Proteolytica.
Appearance
Sterile filtered liquid formulation.

ANPEP Mouse

Alanyl Aminopeptidase Membrane Mouse Recombinant

ANPEP Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing  943 amino acids (33-966 a.a.) and having a molecular mass of  107.5 kDa. ANPEPis expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21367
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

ASPRV1 Human

Aspartic Peptidase, Retroviral-Like 1 Human Recombinant

ASPRV1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (191-326) and having a molecular mass of 17.2kDa.
ASPRV1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21438
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

Carboxypeptidase B Rat

Carboxypeptidase-B Rat Recombinant

Recombinant Rat Carboxypeptidase-B is expressed in E.Coli having a Mw of 31kDa is purified by standard chromatography techniques.
Recombinant Rat Carboxypeptidase-B is free from foreign enzymes such as carboxypeptidase A & chymotrypsin. Recombinant Carboxypeptidase-B is free from protease inhibitors such as PMSF and EDTA.

Shipped with Ice Packs
Cat. No.
BT21530
Source
Escherichia Coli.
Appearance
Sterile Filtered lyophilized powder.

CASP2 Human

Caspase 2 Apoptosis-Related Cysteine Peptidase Human Recombinant

CASP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (348-452) and having a molecular mass of 14.1kDa.
CASP2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21624
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

CASP3 Human

Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant

CASP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 103 amino acids (176-277) and having a molecular mass of 12kDa.
CASP3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21703
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

CASP3 Human, Sf9

Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant, Sf9

CASP3 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (29-277 a.a.) and having a molecular mass of 29.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions).
CASP3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21793
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

CLPP Human

ClpP Caseinolytic Peptidase Human Recombinant

CLPP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (57-277 a.a.) and having a molecular mass of 24.2kDa.
CLPP is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21855
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CNDP1 Human

CNDP Dipeptidase 1 Human Recombinant

CNDP1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507a.a.) and having a molecular mass of 54.9kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21929
Source
Sf9, Insect cells.
Appearance
Sterile filtered colorless solution.

Introduction

Definition and Classification

Peptidases, also known as proteases or proteinases, are enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes by breaking down proteins into smaller peptides or amino acids. Peptidases are classified based on their catalytic mechanisms and substrate specificities into several major groups:

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

Key Biological Properties: Peptidases exhibit high specificity for their substrates, ensuring precise cleavage of peptide bonds. They are involved in protein turnover, processing, and degradation. Expression Patterns: Peptidases are expressed in various tissues and cells, with specific peptidases being more abundant in certain tissues. Tissue Distribution: For example, digestive peptidases like trypsin and chymotrypsin are predominantly found in the pancreas, while lysosomal peptidases like cathepsins are abundant in lysosomes of various cell types.

Biological Functions

Primary Biological Functions: Peptidases are essential for protein digestion, cellular protein turnover, and the activation of precursor proteins. Role in Immune Responses: They play a critical role in antigen processing and presentation, aiding the immune system in recognizing and responding to pathogens. Pathogen Recognition: Certain peptidases are involved in the degradation of pathogen-derived proteins, facilitating the immune response.

Modes of Action

Mechanisms with Other Molecules and Cells: Peptidases interact with various substrates, inhibitors, and cofactors to regulate their activity. Binding Partners: They often form complexes with other proteins or molecules to enhance or inhibit their function. Downstream Signaling Cascades: Peptidase activity can trigger downstream signaling pathways, influencing cellular responses such as apoptosis, proliferation, and differentiation.

Regulatory Mechanisms

Expression and Activity Control: Peptidase expression is tightly regulated at the transcriptional level by various transcription factors and signaling pathways. Transcriptional Regulation: Specific genes encoding peptidases are activated or repressed in response to cellular signals. Post-Translational Modifications: Peptidases undergo modifications such as phosphorylation, glycosylation, and ubiquitination, which can alter their activity, stability, and localization.

Applications

Biomedical Research: Peptidases are studied for their roles in diseases such as cancer, neurodegenerative disorders, and infectious diseases. Diagnostic Tools: Peptidase activity assays are used in diagnostics to detect abnormalities in enzyme function. Therapeutic Strategies: Inhibitors of specific peptidases are developed as drugs to treat conditions like hypertension, cancer, and viral infections.

Role in the Life Cycle

Development to Aging and Disease: Peptidases are involved in various stages of the life cycle, from embryonic development to aging. They play roles in tissue remodeling, cell differentiation, and apoptosis. Dysregulation of peptidase activity is associated with aging and various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.

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