DTD1 Human

D-Tyrosyl-tRNA Deacylase 1 Human Recombinant

Recombinant human DTD1, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 232 amino acids (1-209 a.a.) with a molecular weight of 25.9 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23664
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

DTD2 Human

D-Tyrosyl-tRNA Deacylase 2 Human Recombinant

DTD2 Human Recombinant, produced in E.coli, is a single, non-glycosylated polypeptide chain comprising 191 amino acids (residues 1-168). With a molecular weight of 21.0 kDa, it features a 23 amino acid His-tag at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT23750
Source
Escherichia Coli.
Appearance
Clear solution, sterile filtered.

Ecotin E.Coli

Ecotin E.Coli Recombinant

Produced in E. coli, our Ecotin is a non-glycosylated polypeptide chain consisting of 163 amino acids (21-162a.a.) with a molecular weight of 18.3 kDa. It features a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23826
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

G3BP2 Human

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

Recombinant human G3BP2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 473 amino acids (residues 1-449) with a molecular weight of 53.3 kDa. This protein includes a 24 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24274
Source
Escherichia Coli.
Appearance
Clear, sterile, and filtered solution.

GALM Human

Galactose Mutarotase Human Recombinant

Recombinant human GALM, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 362 amino acids (residues 1-342) with a molecular weight of 39.9 kDa. It includes a 20-amino acid His-tag at the N-terminus to facilitate purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24357
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GLSA1 E.Coli

Glutaminase 1 E.Coli Recombinant

Recombinant E. coli GLSA1, expressed in E. coli and fused with a 20 amino acid His tag at the N-terminus, is a single, non-glycosylated polypeptide chain. It consists of 330 amino acids (1-310 a.a.) and has a molecular weight of 35.0 kDa. GLSA1 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24457
Source
Escherichia Coli.
Appearance
Sterile, colorless, and filtered solution.

GUSB Human

Glucuronidase Beta Human Recombinant

This product consists of recombinant human GUSB produced in Sf9 insect cells using a baculovirus expression system. The protein is a single, glycosylated polypeptide chain with 635 amino acids (residues 23-651). It has a molecular weight of 73.4 kDa, but on SDS-PAGE, it appears between 70-100 kDa due to glycosylation. The protein has a 6-amino acid His-tag at the C-terminus to facilitate purification, which is done through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT24537
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HTRA2 Human

HTRA2 Human Recombinant

Recombinant human HtrA2, encompassing amino acids 134-458 and containing a C-terminal His-tag, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain with a molecular weight of 36 kDa. Purification of HtrA2 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25020
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

HYAL1 Human

Hyaluronidase Human Recombinant

Recombinant human HYAL1, expressed in HEK cells, is a single-chain polypeptide with glycosylation. It consists of 420 amino acids (22-435 a.a) and has a molecular weight of 46.9 kDa. The HYAL1 protein includes a 6-amino acid His-tag at the C-terminus and is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT25237
Source

HEK293 Cells.

Appearance
Clear, colorless solution that has been sterilized by filtration.

PGC Human

Progastricsin-C Human Recombinant

Produced in Sf9 Baculovirus cells, PGC is a single, glycosylated polypeptide chain consisting of 380 amino acids (17-388 a.a.) with a molecular mass of 41.6kDa. On SDS-PAGE, its molecular size appears approximately between 40-57kDa. PGC is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26227
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered 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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