REV1 Human

REV1 Polymerase Human Recombinant

Cat. No.

BT3356

Source

Escherichia Coli.

Synonyms

REV1 Polymerase (DNA Directed), REV1L, Alpha Integrin-Binding Protein 80, Rev1-Like Terminal Deoxycytidyl Transferase, AIBP80, REV1 (Yeast Homolog)- Like, REV1 Homolog (S. Cerevisiae) , REV1-Like (Yeast) , DNA Repair Protein REV1, REV1 Homolog, REV1- Like, EC 2.7.7.-.

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

REV1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (51-256) and having a molecular mass of 25.2kDa.
REV1 is fused to a 21 amino acid His-tag at N-terminus.

Product Specs

Introduction

REV1 Polymerase, also known as REV1, plays a crucial role in DNA repair mechanisms. Its BRCT domain facilitates protein-protein interactions, essential for its function. This deoxycytidyl transferase participates in bypassing abasic lesions during DNA replication by incorporating a nucleotide opposite the damaged site. Moreover, REV1 is vital for normal mutation rates induced by physical and chemical agents. Functionally, it catalyzes the transfer of a dCMP residue from dCTP to the 3' end of a DNA primer in a template-dependent manner. Studies suggest that the human Rev1-like protein acts as a scaffold, recruiting DNA polymerases involved in translesion synthesis (TLS) to repair damaged DNA.

Description

Recombinant human REV1, expressed in E. coli, is available as a single, non-glycosylated polypeptide chain. This protein consists of 227 amino acids (residues 51-256) and has a molecular weight of 25.2 kDa. For purification and detection purposes, a 21 amino acid His-tag is fused to the N-terminus of the REV1 protein.

Physical Appearance

The product is a sterile, colorless solution.

Formulation

The REV1 solution is provided at a concentration of 1 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.4 M Urea, and 10% glycerol.

Stability

For short-term storage (2-4 weeks), the REV1 solution can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To ensure long-term stability, adding a carrier protein such as 0.1% HSA or BSA is advisable. Multiple freeze-thaw cycles should be avoided to maintain protein integrity.

Purity

The purity of the REV1 protein is greater than 85%, as determined by SDS-PAGE analysis.

Synonyms

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGVAIYVNGY TDPSAEELRK LMMLHGGQYH VYYSRSKTTH IIATNLPNAK IKELKGEKVI RPEWIVESIK AGRLLSYIPY QLYTKQSSVQ KGLSFNPVCR PEDPLPGPSN IAKQLNNRVN HIVKKIETEN EVKVNGMNSW NEEDENNDFS FVDLEQTSPG RKQNGIPHPR GSTAIFNGHT PSSNGALKTQ DCLVPMVNSV ASRLSPA.

Product Science Overview

Introduction

REV1 Polymerase is a member of the Y-family DNA polymerases, which are specialized enzymes involved in translesion DNA synthesis (TLS). This process allows the DNA replication machinery to bypass lesions or damages on the DNA template, ensuring the continuation of DNA replication and maintaining genomic stability. The human recombinant form of REV1 Polymerase is produced through recombinant DNA technology, enabling detailed studies of its structure and function.

Structure and Function

REV1 Polymerase is characterized by its unique ability to incorporate deoxycytidine monophosphate (dCMP) opposite damaged bases in the DNA template. This activity is crucial for bypassing various types of DNA damage, including abasic sites and adducts caused by environmental mutagens. The enzyme’s structure includes a BRCT domain, which is involved in protein-protein interactions, and a catalytic domain responsible for its polymerase activity.

Role in DNA Damage Tolerance

REV1 plays a pivotal role in the DNA damage tolerance pathway. It acts as a scaffold protein, recruiting other TLS polymerases to the site of DNA damage. This recruitment is essential for the bypass of lesions that would otherwise stall the replication fork. REV1’s ability to interact with multiple proteins involved in DNA repair highlights its importance in maintaining genomic integrity.

Clinical Significance

The expression and activity of REV1 have been linked to various cancers. Studies have shown that alterations in the REV1 gene can impact patient prognosis and the sensitivity of cancer cells to anti-tumor drugs. For instance, high expression of REV1 is associated with better prognosis in lung and breast cancers, while low expression is linked to better outcomes in colorectal and ovarian cancers. Additionally, REV1’s role in promoting radioresistance in lung cancer has been identified, making it a potential target for enhancing the efficacy of radiotherapy.

Recombinant Production

The human recombinant form of REV1 Polymerase is produced using recombinant DNA technology. This involves cloning the REV1 gene into an expression vector, which is then introduced into a host cell, such as E. coli or yeast. The host cells express the REV1 protein, which can be purified and used for various biochemical and structural studies. Recombinant REV1 is invaluable for research into its mechanisms of action and potential therapeutic applications.

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REV1 Human

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