Recombinant Human GSDMD, N-His

Reference: YHF23901
Product nameRecombinant Human GSDMD, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight24.47 kDa
Protein delivered with Tag?N-Terminal His Tag
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)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypePro278-His484
Aliases /SynonymsGSDMD-CT, hGSDMD-NTD, Gasdermin domain-containing protein 1, Gasdermin-D, DFNA5L, GSDMD-NT, hGSDMD-CTD, GSDMDC1, GSDMD
ReferenceYHF23901
NoteFor research use only.

Description of Recombinant Human GSDMD, N-His

Introduction to Recombinant Human GSDMD

Recombinant Human GSDMD (Gasdermin D) is a protein that plays a crucial role in the process of cell death, known as pyroptosis. It is a member of the gasdermin family of proteins, which are involved in various cellular processes such as cell differentiation, proliferation, and death. GSDMD is a 53 kDa protein that is expressed in various tissues, including the skin, immune cells, and gastrointestinal tract.

Structure of Recombinant Human GSDMD

The recombinant form of GSDMD is produced through genetic engineering techniques, where the gene encoding for GSDMD is inserted into a suitable expression system. The resulting protein is then purified and characterized for its structure and function. Recombinant Human GSDMD has a similar structure to its native form, consisting of an N-terminal domain, a linker region, and a C-terminal domain.

The N-terminal domain of GSDMD is responsible for its interaction with other proteins and is crucial for its function. It contains a conserved sequence known as the gasdermin domain, which is essential for the formation of pores in the cell membrane. The linker region connects the N-terminal domain to the C-terminal domain and is involved in regulating the activity of GSDMD. The C-terminal domain is responsible for binding to lipids and forming pores in the cell membrane, leading to cell death.

Activity of Recombinant Human GSDMD

The main function of GSDMD is to induce pyroptosis, a form of programmed cell death that is triggered by infection or cellular stress. Upon activation, GSDMD forms pores in the cell membrane, causing the release of pro-inflammatory cytokines and danger signals, which attract immune cells to the site of infection or injury. This leads to the elimination of infected or damaged cells and helps in the control of infection and tissue repair.

In addition to its role in pyroptosis, GSDMD has also been implicated in other cellular processes, such as cell proliferation and differentiation. Studies have shown that GSDMD can interact with other proteins involved in these processes and modulate their activity. It has also been suggested that GSDMD may have a role in regulating the immune response and promoting tissue repair.

Applications of Recombinant Human GSDMD

The recombinant form of GSDMD has various applications in the field of research and medicine. It is commonly used as a tool in studying the process of pyroptosis and its role in disease. Recombinant Human GSDMD can be used to induce pyroptosis in cell culture models, allowing researchers to study the mechanism of cell death and its impact on various diseases.

Moreover, GSDMD has been identified as a potential therapeutic target for various diseases, including infectious diseases and cancer. Inhibition of GSDMD activity has been shown to reduce inflammation and tissue damage in animal models of sepsis and inflammatory bowel disease. In cancer, GSDMD has been found to be involved in the regulation of tumor growth and metastasis, making it a potential target for cancer therapy.

In conclusion, Recombinant Human GSDMD is a crucial protein involved in the process of pyroptosis and has various applications in research and medicine. Its structure and function make it an essential tool for studying cell death and its role in diseases, and it holds promise as a therapeutic target for various conditions. Further research on GSDMD and its interactions with other proteins may reveal new insights into its role in health and disease.

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