Recombinant Human AZIN2, N-His

Reference: YHJ99301
Product nameRecombinant Human AZIN2, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight40.06 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeMet1-Glu348
Aliases /SynonymsODC-p, AZIN2, Antizyme inhibitor 2, KIAA1945, ADC, ARGDC, Ornithine decarboxylase-like protein, ODC-like protein, ornithine decarboxylase paralog, ODCP, AzI2, Arginine decarboxylase
ReferenceYHJ99301
NoteFor research use only.

Description of Recombinant Human AZIN2, N-His

Introduction

Recombinant Human AZIN2 is a highly specialized protein that plays a crucial role in various cellular processes. It is a recombinant protein, meaning it is produced through genetic engineering techniques in a laboratory setting. This protein has gained significant attention in the scientific community due to its unique structure and diverse range of activities. In this article, we will delve into the structure, activity, and application of Recombinant Human AZIN2.

Structure of Recombinant Human AZIN2

Recombinant Human AZIN2 is a 373 amino acid protein with a molecular weight of approximately 42 kDa. It is composed of several functional domains, including an N-terminal domain, a central polyamine oxidase domain, and a C-terminal domain. The N-terminal domain is responsible for protein-protein interactions, while the central domain is responsible for the enzymatic activity of the protein. The C-terminal domain, on the other hand, is involved in the regulation of the protein’s activity.

The crystal structure of Recombinant Human AZIN2 has been determined, revealing a unique trimeric structure. Each monomer of the trimer consists of a central polyamine oxidase domain surrounded by two N-terminal domains. This trimeric structure is essential for the protein’s enzymatic activity, as it allows for the binding of multiple substrates and co-factors simultaneously.

Activity of Recombinant Human AZIN2

Recombinant Human AZIN2 is an enzyme that catalyzes the oxidation of polyamines, which are essential molecules involved in various cellular processes. The enzyme utilizes oxygen and produces hydrogen peroxide as a byproduct. This activity is crucial for maintaining optimal levels of polyamines in the cell, as an imbalance can lead to various diseases, including cancer and neurodegenerative disorders.

In addition to its role in polyamine metabolism, Recombinant Human AZIN2 has also been shown to regulate cell proliferation and apoptosis. It accomplishes this by interacting with various proteins involved in these processes, such as p53 and E2F1. This activity of Recombinant Human AZIN2 makes it a potential target for therapeutic interventions in cancer and other diseases characterized by abnormal cell growth.

Application of Recombinant Human AZIN2

The unique structure and diverse range of activities of Recombinant Human AZIN2 make it a valuable tool in various research fields. One of the primary applications of this protein is in the study of polyamine metabolism and its role in diseases. Recombinant Human AZIN2 can be used to investigate the effects of polyamine levels on cellular processes and to identify potential therapeutic targets.

Additionally, Recombinant Human AZIN2 has been utilized in drug discovery and development. As an enzyme involved in cancer cell proliferation, it can serve as a target for the development of novel anti-cancer drugs. Furthermore, the crystal structure of Recombinant Human AZIN2 can aid in the design of specific inhibitors that can selectively target this protein.

In conclusion, Recombinant Human AZIN2 is a highly specialized protein with a unique structure and diverse range of activities. Its role in polyamine metabolism and regulation of cellular processes makes it a valuable tool in various research fields and a potential target for therapeutic interventions. The continued study of this protein will undoubtedly lead to a better understanding of its functions and potential applications in disease treatment.

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