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Recombinant Human HMGB4, N-His

Reference: ARO-P13221
Size

100ug

Brand

Arovia

Product type

Recombinant Proteins

Product nameRecombinant Human HMGB4, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight19.62 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°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)
BrandArovia
Host speciesEscherichia coli (E.coli)
Fragment TypeAsn25-Arg167
Aliases /SynonymsHMGB4, High mobility group protein B4
ReferenceARO-P13221
NoteFor research use only.

Description of Recombinant Human HMGB4, N-His

Introduction

Recombinant Human HMGB4 is a protein that has been engineered in the laboratory using recombinant DNA technology. This technology involves inserting the gene for HMGB4 into a host cell, such as bacteria or yeast, and allowing the cell to produce large quantities of the protein. Recombinant Human HMGB4 has gained significant attention in the scientific community due to its unique structure, diverse activities, and potential applications.

Structure of Recombinant Human HMGB4

Recombinant Human HMGB4 is a member of the High Mobility Group Box (HMGB) protein family, which consists of four proteins (HMGB1-4) that share a similar structure and function. The HMGB proteins are characterized by two DNA-binding domains, known as HMG boxes, which are connected by a flexible linker region. HMGB4 is a small protein, consisting of 164 amino acids, and has a molecular weight of approximately 18 kDa.

Activity of Recombinant Human HMGB4

Recombinant Human HMGB4 has been shown to have multiple activities, including DNA binding, chromatin remodeling, and regulation of gene expression. The protein has a high affinity for DNA and can bind to both double-stranded and single-stranded DNA. This binding is mediated by the HMG boxes, which interact with the minor groove of the DNA helix. Additionally, HMGB4 has been found to play a role in regulating the structure and function of chromatin, which is the complex of DNA and proteins in the nucleus of a cell. This activity is important for the proper functioning of genes and can impact various cellular processes.

Application of Recombinant Human HMGB4

The unique structure and diverse activities of Recombinant Human HMGB4 make it a valuable tool in various scientific applications. One of the major applications of HMGB4 is in the field of gene regulation and expression. Due to its ability to bind to DNA and regulate chromatin structure, HMGB4 can potentially be used to modulate gene expression and understand the underlying mechanisms of gene regulation.

Additionally, Recombinant Human HMGB4 has been studied for its potential role in cancer. It has been found to be overexpressed in various types of cancer, and its expression has been linked to tumor growth and metastasis. Therefore, targeting HMGB4 with specific inhibitors or antibodies could potentially be a therapeutic strategy for cancer treatment.

Furthermore, HMGB4 has also been investigated for its role in inflammation and immune response. It has been shown to interact with various immune cells and cytokines, suggesting its involvement in the regulation of immune response. This makes HMGB4 a potential target for developing new therapies for inflammatory diseases.

Conclusion

In conclusion, Recombinant Human HMGB4 is a unique protein with a diverse range of activities and potential applications. Its structure, DNA-binding ability, and role in gene regulation make it a valuable tool for studying various biological processes. Furthermore, its potential involvement in cancer and inflammation highlights the importance of further research on this protein. With ongoing studies and advancements in recombinant protein technology, the full potential of Recombinant Human HMGB4 is yet to be discovered.

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