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Brand: ProteoGenix

Recombinant Human TREX1 Protein, N-His-SUMO

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
35.20 kDa

$392.00

100ug + 392 loyalty points
Met11–His222
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Recombinant Human TREX1 Protein, N-His-SUMO

Recombinant Human TREX1 Protein, N-His-SUMO

Product name Recombinant Human TREX1 Protein, N-His-SUMO
Origin species Human
Expression system Prokaryotic expression
Molecular weight 35.20 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°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)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Met11-His222
Aliases /Synonyms TREX1, Deoxyribonuclease III, DNase III, Three-prime repair exonuclease 1, 3'-5' exonuclease TREX1
Reference ARO-P11316
Note For research use only.
Molecular Constructor
Met11–His222

Introduction

Recombinant human TREX1 protein, also known as DNase III, is a 33 kDa protein that plays a crucial role in the regulation of the immune response and DNA metabolism. This protein is encoded by the TREX1 gene and is highly conserved among mammals, with 99% similarity between human and mouse sequences. Recombinant human TREX1 protein has been extensively studied and has shown promising potential in various applications, making it a valuable tool for scientific research.

Structure of Recombinant Human TREX1 Protein

The recombinant human TREX1 protein is composed of 293 amino acids and has a predicted molecular weight of 33 kDa. It belongs to the DNase III family and contains a conserved DNase domain, which is responsible for its enzymatic activity. The protein also has a nuclear localization signal and a C-terminal domain that is involved in protein-protein interactions. Recombinant human TREX1 protein is expressed in E. coli and purified using chromatography techniques, resulting in a highly pure and active protein.

Activity of Recombinant Human TREX1 Protein

Recombinant human TREX1 protein is a 3′-5′ exonuclease that plays a vital role in the degradation of single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). It has been shown to have a preference for DNA with a 3′-OH end, making it an essential enzyme in the regulation of DNA metabolism. This protein is also involved in the clearance of DNA from apoptotic cells, preventing the activation of the immune system and the development of autoimmune diseases. Additionally, recombinant human TREX1 protein has been shown to have antiviral activity, inhibiting the replication of viruses such as HIV and hepatitis B.

Application of Recombinant Human TREX1 Protein

Recombinant human TREX1 protein has various applications in scientific research, including its use as an antigen in the development of diagnostic assays and vaccines. Its ability to degrade DNA makes it a valuable tool in the detection of DNA damage and the study of DNA repair mechanisms. This protein has also been studied for its potential therapeutic use in autoimmune diseases, as its deficiency has been linked to the development of systemic lupus erythematosus (SLE) and Aicardi-Goutières syndrome (AGS).

In addition, recombinant human TREX1 protein has been used in the development of novel cancer therapies. It has been shown to have a crucial role in the regulation of the immune response against cancer cells, making it a potential target for immunotherapy. Furthermore, its antiviral activity has sparked interest in using this protein as a therapeutic agent against viral infections.

Conclusion

In summary, recombinant human TREX1 protein is a versatile and essential protein in scientific research. Its structure, activity, and applications make it a valuable tool in various fields, including immunology, DNA metabolism, and cancer research. With further studies and advancements in recombinant protein technology, the potential of this protein in both diagnostic and therapeutic applications is promising.

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