TPSAB1 Human

Tryptase Alpha/Beta 1 Human Recombinant

TPSAB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 270 amino acids (31-275) and having a molecular mass of 30.1 kDa.
TPSAB1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27676
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TPSAB1 Human, Sf9

Tryptase Alpha/Beta 1 Human Recombinant, Sf9

TPSAB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (31-275 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 251 amino acids and having a molecular mass of 28.2kDa.TPSAB1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques. 

Shipped with Ice Packs
Cat. No.
BT27757
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

Urease

Urease Recombinant

The mutant Urease from microorganism source, showing shifted substrate affinity to urea. It was designed wildtype coding gene from microorganism. 
The subunit structure is very similar to well known microbial urease.
Please refer to published literature such as JBC 262, 5963-67 (1987).
It is composed of multi-subunits and shows a bit complex protein structure (alpha 2 Beta 4 Gamma 4) as compared to plant urease
rUrease is genetically designed unique mutant having shifted high Km to urea, which is suited material to kinetic urea assay with wide measurable range.
The enzyme comprises of three different subunits to make complete fully active form, 60.3 kD a subunit, 11.7 kD b subunit and 11.1 kD g subunit respectively.
Shipped with Ice Packs
Cat. No.
BT27828
Source
Escherichia Coli.
Appearance
Sterile Lyophilized Powder.

Urokinase

Urokinase Human Recombinant

Urokinase Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 419 amino acids (21-431) and having a molecular mass of 47.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
Urokinase is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques. 
Shipped with Ice Packs
Cat. No.
BT27919
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.

FBL Human

Fibrillarin Human Recombinant

FBL Human Recombinant fused with 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 262 amino acids (83-321 a.a.) and having a molecular mass of 28.9kDa. The FBL is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24029
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

FUT3 Human

Fucosyltransferase 3 Human Recombinant

FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.
FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24109
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

G3BP1 Human

GTPase Activating Protein (SH3 domain) Binding Protein 1 Human Recombinant

G3BP1 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 474 amino acids (1-466 a.a.) and having a molecular mass of 53.2kDa.
The G3BP1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24197
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

G3BP2 Human

GTPase Activating Protein (SH3 domain) Binding Protein 2 Human Recombinant

G3BP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-449) and having a molecular mass of 53.3kDa.
G3BP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24274
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

GALM Human

Galactose Mutarotase Human Recombinant

GALM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-342 a.a.) and having a molecular mass of 39.9 kDa. The GALM is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. 

Shipped with Ice Packs
Cat. No.
BT24357
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GLSA1 E.Coli

Glutaminase 1 E.Coli Recombinant

GLSA1 E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310a.a.) and having a molecular mass of 35.0kDa.
The GLSA1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24457
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
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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