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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human HSPB7, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 20.92 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 | Met1-Ile170 |
Aliases /Synonyms | HSPB7, CVHSP, Cardiovascular heat shock protein, cvHsp, HspB7, Heat shock protein beta-7 |
Reference | ARO-P13036 |
Note | For research use only. |
Recombinant Human HSPB7, also known as heat shock protein beta-7, is a protein that plays an important role in cellular stress response and protection against various diseases. This protein is produced through recombinant DNA technology, making it a valuable tool in scientific research and potential therapeutic applications.
Recombinant Human HSPB7 is a small protein consisting of 209 amino acids with a molecular weight of approximately 22 kDa. It belongs to the family of small heat shock proteins (sHSPs) and is highly conserved across different species. The protein has a characteristic α-crystallin domain, which is responsible for its chaperone activity.
Recombinant Human HSPB7 is primarily involved in protecting cells from stress-induced damage. It acts as a molecular chaperone, which means it helps other proteins to fold correctly and prevents them from aggregating under stressful conditions. This chaperone activity is crucial for the proper functioning of cells, as misfolded proteins can lead to various diseases, including neurodegenerative disorders.
In addition to its chaperone activity, Recombinant Human HSPB7 has been shown to have anti-apoptotic properties, meaning it can prevent cells from undergoing programmed cell death. This activity is particularly important in protecting cells from damage caused by oxidative stress, which is a major contributor to various diseases, including cancer and cardiovascular diseases.
Recombinant Human HSPB7 has a wide range of potential applications in both scientific research and therapeutic interventions. Some of the key applications are listed below:
Recombinant Human HSPB7 can be produced in large quantities using recombinant DNA technology. This makes it a valuable tool for studying the structure and function of the protein, as well as its role in cellular stress response. Recombinant Human HSPB7 can also be used as a control protein in experiments involving other heat shock proteins.
There is growing evidence that levels of HSPB7 are altered in various diseases, including heart failure and neurodegenerative disorders. Recombinant Human HSPB7 can be used as a biomarker to detect these diseases at an early stage and monitor their progression. This can aid in timely diagnosis and treatment, improving patient outcomes.
Given its anti-apoptotic and chaperone activities, Recombinant Human HSPB7 has the potential to be developed as a therapeutic agent for various diseases. For example, it could be used to protect cells from damage during chemotherapy or as a treatment for neurodegenerative disorders. Further research is needed to explore these potential therapeutic applications.
Recombinant Human HSPB7 can also be used in vaccine development as an antigen. Antigens are substances that stimulate the body’s immune system to produce antibodies, which can then protect against specific diseases. By using Recombinant Human HSPB7 as an antigen, researchers can potentially develop vaccines against diseases that are associated with this protein, such as heart failure.
In summary, Recombinant Human HSPB7 is a valuable protein with various potential applications in scientific research and therapeutic interventions. Its structure, activity, and potential applications make it a promising target for further study and development. With continued research, this protein has the potential to improve our understanding of cellular stress response and provide new treatments for various diseases.
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