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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human HMGB4, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 19.62 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
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 | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Asn25-Arg167 |
Aliases /Synonyms | HMGB4, High mobility group protein B4 |
Reference | ARO-P13221 |
Note | For research use only. |
Recombinant human HMGB4 is a protein that plays a crucial role in various biological processes, including DNA repair, transcription regulation, and immune response. This protein is a member of the high mobility group B (HMGB) family, which is known for its ability to bind to DNA and regulate gene expression. In this article, we will discuss the structure, activity, and application of recombinant human HMGB4.
The HMGB family consists of four members, HMGB1-4, which share a high degree of sequence similarity. Recombinant human HMGB4 is a 25 kDa protein composed of 215 amino acids. It contains two HMG-box domains, which are known for their DNA-binding activity. These domains are connected by a flexible linker region, which allows for the protein to bend and adapt to different DNA structures. Additionally, HMGB4 has a C-terminal acidic tail, which is involved in protein-protein interactions.
The crystal structure of recombinant human HMGB4 has been determined, revealing the mechanism of its DNA-binding activity. The HMG-box domains adopt a distorted L-shaped structure, with the DNA-binding residues located in the concave surface. This allows for the protein to bind to DNA in a non-sequence-specific manner, making it a versatile player in various cellular processes.
Recombinant human HMGB4 is involved in many cellular processes, including DNA repair, transcription regulation, and immune response. Its ability to bind to DNA and regulate gene expression makes it a key player in these processes.
One of the main functions of HMGB4 is its role in DNA repair. It has been shown to interact with other DNA repair proteins, such as XRCC1, and contribute to the repair of damaged DNA. Additionally, HMGB4 has been found to play a role in transcription regulation by binding to specific DNA sequences and influencing the activity of transcription factors.
Furthermore, recombinant human HMGB4 has been shown to have immunomodulatory effects. It can act as an antigen, stimulating the production of antibodies and activating immune cells. This makes it a potential target for therapeutic interventions in autoimmune diseases and cancer.
The versatility of recombinant human HMGB4 makes it a valuable tool in various research areas. Its ability to bind to DNA and regulate gene expression has made it a target for studying DNA repair and transcription regulation. Additionally, its immunomodulatory effects have made it a potential target for developing therapies for autoimmune diseases and cancer.
Recombinant human HMGB4 is also used in the production of diagnostic tools, such as ELISA kits, for the detection of antibodies against this protein. This allows for the detection of autoimmune diseases and the monitoring of immune response in cancer patients.
Moreover, recombinant human HMGB4 has potential applications in biotechnology, particularly in the development of new drugs. Its ability to interact with other proteins and influence cellular processes makes it a promising target for drug development.
In summary, recombinant human HMGB4 is a versatile protein with important roles in DNA repair, transcription regulation, and immune response. Its structure, activity, and application make it a valuable tool for research and potential target for therapeutic interventions. Further studies on this protein will provide a better understanding of its functions and potential applications in various fields.
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