PRTN3 Human

Proteinase-3 Human

PRTN3 is a protein naturally present in the human body with a molecular weight of 25kDa. It is extracted from human white blood cells for research purposes.
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Cat. No.
BT26563
Source
Native.

Urease

Urease Recombinant

This engineered Urease enzyme is derived from a microorganism and exhibits altered substrate affinity for urea compared to its wild-type counterpart. The genetic design of this enzyme originates from the wild-type gene found in the microorganism. Structurally, it shares similarities with well-characterized microbial ureases. For a deeper understanding, refer to published studies such as JBC 262, 5963-67 (1987). This urease comprises multiple subunits, forming a slightly intricate protein structure (α2β4γ4) in contrast to plant ureases. Notably, this genetically modified mutant urease (rUrease) displays a distinctive shift towards a higher Km for urea, making it well-suited for kinetic urea assays with an extended measurable range. The enzyme is composed of three distinct subunits (60.3 kDa α subunit, 11.7 kDa β subunit, and 11.1 kDa γ subunit) that assemble to form the fully active enzyme.
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Cat. No.
BT27828
Source
Escherichia Coli.
Appearance
Lyophilized powder, sterile.

Urokinase

Urokinase Human Recombinant

Recombinant Human Urokinase, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 419 amino acids (21-431). It has a molecular mass of 47.4kDa, although it may appear between 40-57kDa on SDS-PAGE. This Urokinase variant is fused with an 8 amino acid His-Tag at the C-terminus and undergoes purification using proprietary chromatographic techniques.
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Cat. No.
BT27919
Source
Sf9, Baculovirus cells.
Appearance
A clear solution that has been sterilized through filtration.
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Cat. No.
BT2029458
Source
E.Coli
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Cat. No.
BT2029515
Source
E.Coli

Recombinant Human Fructose-2,6-bisphosphatase TIGAR protein (TIGAR) (Active)

This recombinant human fructose-2,6-bisphosphatase TIGAR protein is produced in E. coli using an expression vector containing a C-terminal TAT-tag. Following expression, the protein is purified from the cell lysate and exhibits a purity exceeding 96%, as determined by both SDS-PAGE and HPLC analysis. The activity of the recombinant TIGAR protein is validated by its ability to protect U2OS cells from hydrogen peroxide-induced apoptosis. Pretreatment with purified rHuTIGAR-TAT protein for 4 hours demonstrates its efficacy in preserving cell viability within a concentration range of 0.1-5.0 µg/mL. The endotoxin level is less than 1.0 EU/µg, as determined by the LAL method.

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Cat. No.
BT2029617
Source
E.coli
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Cat. No.
BT2029647
Source
E.Coli
Shipped with Ice Packs
Cat. No.
BT2029715
Source
E.coli
Definition and Classification

Enzymes are biological catalysts that accelerate chemical reactions in living organisms. “Other enzymes” refer to those that do not fall into the major categories like oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. These enzymes often have unique functions and structures, making them essential for various biochemical processes.

Biological Properties

Key Biological Properties: Other enzymes exhibit diverse catalytic activities, substrate specificities, and structural features. They often have unique active sites and cofactor requirements.

Expression Patterns: The expression of these enzymes can be highly specific to certain cell types or tissues, and it can be regulated by various physiological conditions.

Tissue Distribution: These enzymes are distributed across different tissues, including the liver, brain, heart, and immune cells, reflecting their specialized roles in various biological processes.

Biological Functions

Primary Biological Functions: Other enzymes play crucial roles in metabolic pathways, signal transduction, DNA repair, and protein degradation. They are involved in synthesizing and breaking down biomolecules, maintaining cellular homeostasis.

Role in Immune Responses: Some of these enzymes are key players in the immune system, participating in pathogen recognition, antigen processing, and the activation of immune cells.

Pathogen Recognition: Enzymes like lysozymes and proteases help recognize and degrade pathogenic components, contributing to the body’s defense mechanisms.

Modes of Action

Mechanisms with Other Molecules and Cells: Other enzymes interact with substrates, cofactors, and other proteins to catalyze reactions. These interactions often involve specific binding sites and conformational changes.

Binding Partners: These enzymes may bind to various molecules, including nucleotides, lipids, and other proteins, to exert their catalytic functions.

Downstream Signaling Cascades: Enzymes can initiate or modulate signaling pathways, leading to cellular responses such as gene expression, cell proliferation, and apoptosis.

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of other enzymes are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications.

Transcriptional Regulation: Gene expression of these enzymes can be controlled by transcription factors, epigenetic modifications, and signaling pathways.

Post-Translational Modifications: Enzymes can undergo modifications such as phosphorylation, ubiquitination, and glycosylation, which can alter their activity, stability, and localization.

Applications

Biomedical Research: Other enzymes are valuable tools in research for studying biochemical pathways, disease mechanisms, and drug development.

Diagnostic Tools: Enzymes are used in diagnostic assays to detect biomarkers of diseases, such as enzyme-linked immunosorbent assays (ELISAs).

Therapeutic Strategies: Enzyme replacement therapies and enzyme inhibitors are used to treat various diseases, including metabolic disorders and cancers.

Role in the Life Cycle

Development: Enzymes are essential for embryonic development, cell differentiation, and organogenesis.

Aging: Enzyme activity can decline with age, contributing to the aging process and age-related diseases.

Disease: Dysregulation of enzyme activity is associated with various diseases, including genetic disorders, neurodegenerative diseases, and cancers.

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