Lysozyme Human

Lysozyme Human Recombinant

Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT25527
Source

Oryza sativa (rice).

Appearance

Sterile Filtered lyophilized (freeze-dried) off white powder.

ME2 Human

Malic Enzyme 2 Human Recombinant

ME2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 573 amino acids and having a total molecular mass of 64.4kDa.
ME2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25600
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

MMLV RT

Moloney Murine Leukemia Virus Reverse Trancscriptase Recombinant

MMLV (Moloney Murine Leukemia Virus) Reverse Transcriptase is a DNA polymerase that synthesizes a complementary DNA strands from single-stranded RNA, DNA, or an RNA-DNA hybrid as a template. This recombinant enzyme was purified from E.coli, which carried a modified MMLV-RT gene. Compared to AMV Reverse Transcriptase, this enzyme has a much weaker 5' - 3' ribonuclease H activity, which allows the syntesis of longer cDNAs (>7kb).
Shipped with Ice Packs
Cat. No.
BT25684
Source
Recombinant E. coli strain.
Appearance
Sterile Filtered clear solution (200 U/µl).

NAE1 Human

NEDD8 Activating Enzyme E1 Subunit 1 Human Recombinant

NAE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 557 amino acids (1-534) and having a molecular mass of 62.7kDa.
NAE1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25768
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

NEU1 Human

Sialidase 1 Human Recombinant

NEU1 Human Recombinant produced in E. coli is a single polypeptide chain containing 393 amino acids (48-415) and having a molecular mass of 42.9 kDa.
NEU1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25881
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

NIT2 Human

Nitrilase Family Member 2 Human Recombinant

NIT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276a.a.) and having a molecular mass of 33kDa.
NIT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25972
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

OLA1 Human

Obg-Like ATPase 1 Human Recombinant

OLA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 47.3kDa.
OLA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26044
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PAPP A Human

Pregnancy-Associated Plasma Protein-1 Human Recombinant

PAPP-A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 191 amino acids fragment (81-271) corresponding to the PAPP-A “Jelly-Roll” domain fragment, having a total molecular mass of 25.75kDa and fused with an amino-terminal hexahistidine tag.

The PAPP-A is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT26160
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PGC Human

Progastricsin-C Human Recombinant

PGC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (17-388 a.a.) and having a molecular mass of 41.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). 
PGC is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26227
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

PGLS Human

6-Phosphogluconolactonase Human Recombinant

PGLS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-258a.a.) and having a molecular mass of 29.7kDa.
PGLS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26314
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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