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Brand: ProteoGenix

Recombinant Human DPF2 Protein, N-His-SUMO & C-Strep

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

$392.00

100ug + 392 loyalty points
Glu290–Ser391
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Recombinant Human DPF2 Protein, N-His-SUMO & C-Strep

Recombinant Human DPF2 Protein, N-His-SUMO & C-Strep

Product name Recombinant Human DPF2 Protein, N-His-SUMO & C-Strep
Origin species Human
Expression system Prokaryotic expression
Molecular weight 25.12 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 Glu290-Ser391
Aliases /Synonyms Protein requiem, BAF45D, Zinc finger protein ubi-d4, BRG1-associated factor 45D, REQ, DPF2, UBID4, Apoptosis response zinc finger protein, D4, zinc and double PHD fingers family 2
Reference ARO-P11707
Note For research use only.
Molecular Constructor
Glu290–Ser391

Recombinant Human DPF2 Protein: Structure, Activity, and Application

Introduction

Recombinant proteins are proteins that are produced through genetic engineering techniques, where a specific gene is inserted into a host organism, such as bacteria or yeast, to produce large quantities of the desired protein. Recombinant proteins have become essential tools in various fields of research, including biotechnology, medicine, and diagnostics.

Structure of Recombinant Human DPF2 Protein

The Recombinant Human DPF2 Protein is a 147 kDa protein that belongs to the D4, zinc finger-containing protein family. It is encoded by the DPF2 gene, located on chromosome 8 in humans. The protein consists of 1273 amino acids and contains two conserved domains: the C2H2-type zinc finger domain and the PHD-type zinc finger domain.

The C2H2-type zinc finger domain is responsible for DNA binding, while the PHD-type zinc finger domain is involved in protein-protein interactions. These two domains play a crucial role in the function of Recombinant Human DPF2 Protein.

Structure of Recombinant Human DPF2 Protein

Activity of Recombinant Human DPF2 Protein

Recombinant Human DPF2 Protein is a transcriptional co-activator that regulates gene expression by binding to specific DNA sequences and interacting with other proteins. It is a key component of the transcriptional machinery and is involved in various cellular processes, including cell proliferation, differentiation, and development.

Studies have shown that Recombinant Human DPF2 Protein plays a critical role in the regulation of gene expression in different tissues, such as the brain, heart, and skeletal muscle. It has also been linked to several diseases, including cancer and neurological disorders.

Application of Recombinant Human DPF2 Protein

Recombinant Human DPF2 Protein has various applications in both research and clinical settings. Its ability to regulate gene expression makes it a valuable tool in studying the molecular mechanisms of different diseases and identifying potential therapeutic targets.

In addition, Recombinant Human DPF2 Protein has been used in the production of monoclonal antibodies for the diagnosis and treatment of cancer. It has also been used in the development of gene therapy strategies for inherited diseases caused by mutations in the DPF2 gene.

Furthermore, Recombinant Human DPF2 Protein has been used in the production of vaccines as an antigen. Its high immunogenicity makes it an ideal candidate for eliciting an immune response and providing protection against specific diseases.

Conclusion

In summary, Recombinant Human DPF2 Protein is a crucial protein with diverse roles in gene regulation and cellular processes. Its structure, activity, and application make it a valuable tool in various fields of research and medicine. Further studies on this protein may lead to a better understanding of its function and potential therapeutic applications.

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