MME Human

Membrane Metalloendopeptidase Human Recombinant

This recombinant human MME protein is produced in Sf9 insect cells. It is a single, glycosylated polypeptide chain encompassing amino acids 52 to 750 of the MME protein sequence. This results in a protein with a molecular weight of 80.9 kDa. Note: On SDS-PAGE, the protein may appear between 70-100 kDa due to glycosylation. The recombinant protein is tagged with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT21236
Source

Sf9, Insect cells.

Appearance
A clear, sterile-filtered solution.

Aminopeptidase

Aminopeptidase Aeromonas Recombinant

The 29 kDa Aeromonas Aminopeptidase, produced via genetic engineering, is suitable for physical and structural investigations, sequence and amino-terminal determinations. This exopeptidase, which recognizes a specific stop sign at -X-Pro and requires a free α-amino group in the L-configuration, is suitable for removing 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.

ANPEP Mouse

Alanyl Aminopeptidase Membrane Mouse Recombinant

ANPEP Mouse, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain consisting of 943 amino acids (33-966 a.a.) with a molecular weight of 107.5 kDa. This recombinant protein is expressed with a 9 amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT21367
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ASPRV1 Human

Aspartic Peptidase, Retroviral-Like 1 Human Recombinant

Recombinant human ASPRV1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 159 amino acids (191-326). It has a molecular mass of 17.2 kDa. This ASPRV1 variant is fused to a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21438
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

Carboxypeptidase B Rat

Carboxypeptidase-B Rat Recombinant

Recombinant Rat Carboxypeptidase-B, with a molecular weight of 31 kDa, is produced in E. coli and purified using standard chromatographic methods. This recombinant enzyme is free from contaminants such as carboxypeptidase A, chymotrypsin, PMSF, and EDTA.
Shipped with Ice Packs
Cat. No.
BT21530
Source
Escherichia Coli.
Appearance
Sterile, lyophilized powder.

CASP2 Human

Caspase 2 Apoptosis-Related Cysteine Peptidase Human Recombinant

Recombinant human CASP2, expressed in E.coli, is available as a single, non-glycosylated polypeptide chain. It consists of 126 amino acids (residues 348-452) and has a molecular weight of 14.1 kDa. The protein is engineered with a 21 amino acid His-tag at the N-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21624
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

CASP3 Human

Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant

Recombinant human CASP3 protein was produced in E. coli. It is a single polypeptide chain that lacks glycosylation. This protein contains 103 amino acids (residues 176-277) and has a molecular weight of 12 kDa. CASP3 is purified using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21703
Source
Escherichia Coli.
Appearance
A clear and sterile solution.

CASP3 Human, Sf9

Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant, Sf9

This product consists of the human CASP3 protein produced using Sf9 insect cells infected with a baculovirus expression system. It is a single polypeptide chain that has undergone glycosylation, a common post-translational modification. The protein encompasses amino acids 29 to 277 of the CASP3 sequence, resulting in a protein of 256 amino acids. The molecular weight of the protein is 29.4 kDa. On SDS-PAGE analysis under reducing conditions, it migrates with an apparent molecular weight between 13.5 and 18 kDa. The protein has been engineered to include a 6-amino acid histidine tag at the C-terminus, facilitating its purification. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21793
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CLPP Human

ClpP Caseinolytic Peptidase Human Recombinant

Produced in E. coli, CLPP is a single, non-glycosylated polypeptide chain consisting of 222 amino acids (specifically, amino acids 57 to 277). Its molecular weight is 24.2 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21855
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

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 has a molecular mass of 54.9 kDa. On SDS-PAGE, the molecular size will appear at approximately 50-70 kDa.
This protein is expressed with an 8 amino acid His tag at the C-terminus and is purified by proprietary chromatographic techniques.

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