ACO1 Human

Aconitase-1 Human Recombinant

Produced in E. coli, ACO1 is a single, non-glycosylated polypeptide chain consisting of 912 amino acids (1-889a.a.) with a molecular weight of 100.8 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.
BT22018
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

ACY3 Human

AminoAcylase-3 Human Recombinant

Recombinant human ACY3, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 342 amino acids (with a sequence spanning from amino acid position 1 to 319). It has a molecular weight of 37.6 kDa. A 23 amino acid His-tag is fused to the N-terminus of the ACY3 protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22118
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

ALKBH2 Human

ALKB Alkylation Repair Homolog 2 Human Recombinant

Produced in E. coli, ALKBH2 is a single, non-glycosylated polypeptide chain composed of 281 amino acids (specifically, amino acids 1 to 261) with a molecular weight of 31.4 kDa. A 20 amino acid His-tag is fused to the N-terminus of ALKBH2. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22190
Source
Escherichia Coli.
Appearance
A clear solution, devoid of any color, that has been sterilized through filtration.

ALKBH3 Human

ALKB Alkylation Repair Homolog 3 Human Recombinant

Recombinant human ALKBH3, expressed in E. coli, is a monomeric protein with a His-tag fused at its N-terminus. This non-glycosylated polypeptide chain consists of 325 amino acids (residues 1-286), resulting in a molecular weight of 37.9 kDa. Purification of ALKBH3 is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22319
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for clarity.

ARG1 Human

Arginase-1 Human Recombinant

Recombinant human ARG1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 330 amino acids (specifically, amino acids 1 through 322 with an 8 amino acid His tag fused at the C-terminus). This protein has a molecular weight of 35.8 kDa and is purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT22390
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

BAT1 Human

HLA-B Associated Transcript 1 Human Recombinant

Recombinant BAT1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 448 amino acids (residues 1-428). With a molecular weight of 51.1 kDa, it features a 20 amino acid His Tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22834
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

BTD Human

Biotinidase Human Recombinant

Recombinant human BTD, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It comprises 510 amino acids (44-545a.a), with a molecular weight of 57.8 kDa. Note: On SDS-PAGE, the apparent molecular size may range from 50 to 70 kDa. The BTD protein is fused to an 8 amino acid His-tag at its C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22941
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CAT Human

Catalase Human Recombinant

Recombinant human CAT, expressed in E.coli, is a non-glycosylated polypeptide chain composed of 547 amino acids (1-527). With a molecular weight of 61.9 kDa, this monomeric protein is fused to a 20 amino acid His-tag at its N-terminus and purified through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23032
Source
Escherichia Coli.
Appearance
A clear, yellowish solution that has been sterilized by filtration.

Chitodextrinase

Chitodextrinase Clostridium Botulinum Recombinant

This product consists of recombinant Clostridium Botulinum Chitodextrinase, expressed in E. coli and fused with a 13 amino acid His tag at the N-terminus. It is a purified, non-glycosylated polypeptide chain with a molecular weight of 66.9kDa, comprising 590 amino acids. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23119
Source
Escherichia Coli.
Appearance
Sterile, white powder obtained by lyophilization (freeze-drying).

DCPS Human

Decapping Enzyme, Scavenger Human Recombinant

Recombinant human DCPS, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 357 amino acids (residues 1-337) with a molecular mass of 40.7 kDa. A 20 amino acid His-tag is fused to the N-terminus. The protein is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23601
Source
Escherichia Coli.
Appearance
Sterile filtered, clear 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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