GUSB Human

Glucuronidase Beta Human Recombinant

GUSB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 635 amino acids (23-651a.a) and having a molecular mass of 73.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GUSB is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24537
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

GYG1 Human

Glycogenin-1 Human Recombinant

GYG1 Human Recombinant fused with a 32 amino acid His-T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-333 a.a.) and having a molecular mass of 41.2kDa.
The GYG1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24637
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

HDDC2 Human

HD Domain Containing 2 Human Recombinant

HDDC2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a) and having a molecular mass of 25.8 kDa.
HDDC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24720
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

HEXA Human

Hexosaminidase A Human Recombinant

HEXA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 464 amino acids (89-529 a.a) and having a molecular mass of 52.9 kDa.
HEXA is fused to a 23 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT24804
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

HEXA Human, Sf9

Hexosaminidase A Human Recombinant, SF9

HEXA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 513 amino acids (23-529a.a.) and having a molecular mass of 59.2kDa. 
(Molecular size on SDS-PAGE will appear at approximately 50-70kDa). 
HEXA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24872
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

HTATIP2 Human

HIV-1 Tat Interactive Protein 2 Human Recombinant

HTATIP2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (1-242 a.a.) and having a molecular mass of 29.3 kDa. The HTATIP2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24945
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

HTRA2 Human

HTRA2 Human Recombinant

HtrA2 Human Recombinant amino acids 134-458 His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 36kDa.
The HtrA2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25020
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

HYAL1 Human

Hyaluronidase Human Recombinant

HYAL1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-435 a.a) containing a total of 420 amino acids, having a molecular mass of 46.9 kDa.
HYAL1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT25237
Source

HEK293 Cells.

Appearance
Sterile Filtered colorless solution.

IYD Human

Iodotyrosine Deiodinase Human Recombinant

IYD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (24-214 a.a) and having a molecular mass of 25.1kDa.
IYD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25322
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

Latexin Human

Latexin Human Recombinant

Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT25439
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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