Recombinant Human NFKBIZ Protein, N-His

Introduction

Recombinant proteins are artificially produced proteins that are derived from genetic material and expressed in host cells. These proteins have become an essential tool in various fields of research and have revolutionized the biotechnology industry. One such protein is Recombinant Human NFKBIZ Protein, which has gained significant attention due to its unique structure, activity, and potential applications.

Structure of Recombinant Human NFKBIZ Protein

Recombinant Human NFKBIZ Protein is a member of the nuclear factor-kappa B (NF-κB) family of transcription factors. It is encoded by the NFKBIZ gene located on chromosome 3 in humans. The protein consists of 608 amino acids with a molecular weight of approximately 68 kDa. It contains an N-terminal Rel homology domain (RHD) and a C-terminal ankyrin repeat domain (ARD), which are essential for its transcriptional activity.

The RHD domain of Recombinant Human NFKBIZ Protein is responsible for DNA binding and dimerization with other NF-κB family members. It also contains two nuclear localization signals (NLS) that facilitate its translocation from the cytoplasm to the nucleus. The ARD domain, on the other hand, mediates protein-protein interactions and is involved in the recruitment of co-activators or co-repressors for transcriptional regulation.

Activity of Recombinant Human NFKBIZ Protein

Recombinant Human NFKBIZ Protein is a potent regulator of immune and inflammatory responses. It is activated by various stimuli, including pro-inflammatory cytokines, bacterial and viral infections, and cellular stress. Upon activation, it translocates to the nucleus and binds to specific DNA sequences, known as κB sites, to regulate the expression of target genes.

The transcriptional activity of Recombinant Human NFKBIZ Protein is dependent on its interaction with other proteins. It can form homodimers or heterodimers with other NF-κB family members, such as p65 and p50, to modulate gene expression. It can also interact with other transcription factors, such as AP-1 and STAT, to synergistically regulate gene expression.

Application of Recombinant Human NFKBIZ Protein

Recombinant Human NFKBIZ Protein has been implicated in various biological processes, including immune response, inflammation, cell proliferation, and survival. Its dysregulation has been associated with several diseases, such as cancer, autoimmune disorders, and infectious diseases. Therefore, it has become a potential therapeutic target for the development of novel treatments.

One of the main applications of Recombinant Human NFKBIZ Protein is in the study of NF-κB signaling pathways. Its recombinant form allows for the manipulation of its expression and activity, providing insights into its role in different cellular processes. It has also been used to screen for potential inhibitors or activators of NF-κB signaling, which can aid in the development of new therapeutics.

Furthermore, Recombinant Human NFKBIZ Protein has been used in various in vitro and in vivo studies to elucidate its role in different diseases. For instance, its overexpression has been shown to promote cell proliferation and survival in cancer cells, while its inhibition has been linked to decreased inflammation in autoimmune disorders.

Conclusion

Recombinant Human NFKBIZ Protein is a crucial member of the NF-κB family of transcription factors, with a unique structure and diverse functions. Its recombinant form has allowed for a better understanding of its role in different biological processes and diseases. Further research on this protein could lead to the development of new therapeutic strategies for various diseases.

ProteoGenix catalogue number ARO-P11694. For research use only.

Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 16.89 kDa; Fragment: Gln454-Leu586; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..

Available configurations: 50ug, 100ug, 1mg.

Download the manufacturer datasheet