FAP Human

Fibroblast Activation Protein Alpha Human Recombinant

FAP Human, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 744 amino acids (26-760aa). It has a molecular mass of 86.1 kDa. This protein is fused to a 6 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22603
Source

Sf9, Baculovirus cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.

GLU-C S.aureus

Glutamyl endopeptidase Staphylococcal Recombinant

This product consists of recombinant Staphylococcal GLU-C, produced in E. coli. It is a single, non-glycosylated polypeptide chain with a molecular weight of 28.9 kDa, comprising 267 amino acids.
Shipped with Ice Packs
Cat. No.
BT22692
Source
Escherichia Coli.
Appearance
The product is a sterile, lyophilized powder.

IMMP2L Human

IMP2 Inner Mitochondrial Membrane Peptidase-Like Human Recombinant

IMMP2L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (38-175aa) and having a molecular mass of 18.0kDa. IMMP2L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22777
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

METAP1 Human

Methionyl Aminopeptidase 1 Human Recombinant

This product consists of the recombinant human METAP1 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 409 amino acids (amino acids 1 to 386) with a molecular weight of 45.7 kDa. For purification and detection purposes, a 23 amino acid His-tag is fused to the N-terminus of the protein. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23245
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

METAP1D Human

Methionyl Aminopeptidase 1D Human Recombinant

Recombinant human METAP1D, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 37.4 kDa. It consists of 339 amino acids (residues 20-335) and includes a 23-amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23331
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

MME Human, Active

Membrane Metalloendopeptidase Human Recombinant, Active

This product consists of the human form of the MME protein, produced in Sf9 insect cells using a baculovirus expression system. This protein is a single chain with glycosylation, containing 708 amino acids (specifically, amino acids 52 to 750 of the full protein sequence) and has a molecular weight of 80.9 kDa. For purification and detection purposes, a six-histidine tag is present at the C-terminus. The protein has been purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT23444
Source
Sf9, Baculovirus cells.
Appearance
A clear solution without any color that has been sterilized by filtration.

NAPSA Human

Napsin A Aspartic Peptidase Human Recombinant

Recombinant human NAPSA, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 380 amino acids (residues 64-420) with a molecular weight of 40.9 kDa. It features a 23-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23513
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

PEPD Human

Peptidase D Human Recombinant

Recombinant human PEPD, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 516 amino acids (1-493a.a.), including a 23 amino acid His-tag attached to the N-terminus, and has a molecular weight of 56.9kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23940
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PGPEP1 Human

Pyroglutamyl-Peptidase I Human Recombinant

Recombinant human PGPEP1, expressed in E.coli, is a single, non-glycosylated polypeptide chain comprising 232 amino acids (1-209). It has a molecular weight of 25.5kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24019
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.

PI16 Human

Peptidase Inhibitor 16 Human Recombinant

This recombinant human PI16 protein is produced in HEK293 cells. An 11-amino acid Flag tag is fused to the C-terminus of the protein. The resulting PI16 Flag-tagged fusion protein has a molecular weight of 45.7 kDa and consists of 426 amino acid residues. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24088
Source
HEK293 (Human Embryonic Kidney cell line).
Appearance
White, lyophilized powder after filtration.
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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