RRM2 Human

Ribonucleotide Reductase M2 Human Recombinant

Cat. No.

BT20437

Source

Escherichia Coli.

Synonyms

EC 1.17.4.1, RR2M, RR2, Ribonucleotide Reductase M2, R2, RRM2.

Appearance

Sterile filtered colorless solution.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

RRM2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-389 a.a.) and having a molecular mass of 47 kDa. The RRM2 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

RRM2 is an enzyme that catalyzes the conversion of ribonucleotides to deoxyribonucleotides, a crucial step in DNA synthesis. The enzyme's activity is tightly regulated throughout the cell cycle, ensuring the availability of DNA building blocks when needed. RRM2's role in DNA synthesis makes it essential for cell division and proliferation. Additionally, RRM2 has been found to inhibit Wnt signaling, a pathway involved in cell fate determination and development.

Description

Recombinant Human RRM2 is a purified protein produced in E. coli. This 47 kDa protein consists of a single, non-glycosylated polypeptide chain of 409 amino acids (amino acids 1-389) and includes a 20 amino acid His-Tag at the N-terminus. The protein is purified using proprietary chromatographic techniques to ensure high purity.

Physical Appearance

Clear, colorless solution that has been sterilized by filtration.

Formulation

The RRM2 protein is supplied as a 1 mg/ml solution in a buffer containing 20mM Tris-HCl (pH 8), 0.1M NaCl, and 10% glycerol.

Stability

For short-term storage (up to 4 weeks), the protein can be stored at 4°C. For long-term storage, it is recommended to store the protein frozen at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. Repeated freezing and thawing of the protein should be avoided.

Purity

The purity of the RRM2 protein is greater than 85%, as determined by SDS-PAGE analysis.

Synonyms

EC 1.17.4.1, RR2M, RR2, Ribonucleotide Reductase M2, R2, RRM2.

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MLSLRVPLAP ITDPQQLQLS PLKGLSLVDK ENTPPALSGT RVLASKTARR IFQEPTEPKT KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS FWTAEEVDLS KDIQHWESLK PEERYFISHV LAFFAASDGI VNENLVERFS QEVQITEARC FYGFQIAMEN IHSEMYSLLI DTYIKDPKER EFLFNAIETM PCVKKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF ASIFWLKKRG LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRIE QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM ENISLEGKTN FFEKRVGEYQ RMGVMSSPTE NSFTLDADF.

Product Science Overview

Introduction

Ribonucleotide Reductase M2 (RRM2) is a critical enzyme involved in the synthesis of deoxyribonucleotides from ribonucleotides, which are essential precursors for DNA synthesis and repair. This enzyme plays a pivotal role in maintaining the balance of the deoxyribonucleotide pool within cells, ensuring proper DNA replication and cell division.

Structure and Function

RRM2 is one of the two non-identical subunits of ribonucleotide reductase, the other being RRM1. The RRM2 subunit is regulated in a cell-cycle-dependent manner, with its expression peaking during the S phase of the cell cycle. This regulation ensures that deoxyribonucleotide production is synchronized with DNA replication demands.

The enzyme catalyzes the reduction of ribonucleotides to deoxyribonucleotides through a complex mechanism involving radical generation and transfer. The active site of RRM2 contains a diiron-oxygen cluster, which is essential for the generation of a tyrosyl radical necessary for the reduction process.

Biological Significance

RRM2 is crucial for DNA synthesis and repair, making it indispensable for cell proliferation and survival. Its activity is tightly regulated to prevent imbalances in the deoxyribonucleotide pool, which can lead to genomic instability and contribute to carcinogenesis.

Expression Patterns and Tissue Distribution

RRM2 is ubiquitously expressed in proliferating cells, with higher expression levels observed in tissues with high proliferative rates, such as the bone marrow, thymus, and gastrointestinal tract. Its expression is also upregulated in various cancers, where it is often associated with poor prognosis.

Regulatory Mechanisms

The expression of RRM2 is regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications. Transcriptional regulation is mediated by cell cycle-dependent transcription factors, while post-transcriptional regulation involves microRNAs that target RRM2 mRNA for degradation. Post-translational modifications, such as phosphorylation, can also modulate the activity and stability of the RRM2 protein.

Clinical Implications

Given its essential role in DNA synthesis and repair, RRM2 is a potential target for cancer therapy. Inhibitors of ribonucleotide reductase, such as hydroxyurea, have been used to treat certain cancers by disrupting DNA synthesis in rapidly proliferating tumor cells. Additionally, the overexpression of RRM2 in cancers makes it a valuable biomarker for prognosis and a potential target for therapeutic intervention.

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RRM2 Human

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