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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human ITIH4 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 28.86 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 | Gly32-Gly267 |
Aliases /Synonyms | Inter-alpha-trypsin inhibitor family heavy chain-related protein, Inter-alpha-trypsin inhibitor heavy chain H4, PK120, PK-120, Plasma kallikrein sensitive glycoprotein 120, Inter-alpha-inhibitor heavy chain 4, ITIHL1, ITIH4, IHRP, ITI-HC4, ITI heavy chain H4, Gp120 |
Reference | ARO-P11645 |
Note | For research use only. |
Recombinant Human ITIH4 Protein, also known as Inter-alpha-trypsin inhibitor heavy chain H4, is a protein that is encoded by the ITIH4 gene in humans. This protein is a member of the inter-alpha-trypsin inhibitor (ITI) family and is involved in various biological processes such as inflammation, coagulation, and wound healing. Recombinant Human ITIH4 Protein is produced through genetic engineering techniques, making it a valuable tool for research and therapeutic applications.
Recombinant Human ITIH4 Protein is a large glycoprotein consisting of 1206 amino acids with a molecular weight of approximately 130 kDa. It is composed of three distinct domains: a heavy chain, a light chain, and a chondroitin sulfate attachment region. The heavy chain is responsible for the protein’s structural stability and contains multiple glycosylation sites. The light chain is responsible for the protein’s interaction with other molecules, such as proteases and cytokines. The chondroitin sulfate attachment region is responsible for the attachment of chondroitin sulfate, a type of glycosaminoglycan, which plays a role in the protein’s anti-inflammatory activity.
Recombinant Human ITIH4 Protein has multiple activities that make it a crucial component in various physiological processes. One of its main functions is its role in the inflammatory response. It acts as an acute-phase protein, meaning its levels increase in response to inflammation, and it has been shown to inhibit the activity of pro-inflammatory molecules such as cytokines and chemokines. This anti-inflammatory activity makes it a potential therapeutic target for conditions such as arthritis and sepsis.
In addition to its anti-inflammatory activity, Recombinant Human ITIH4 Protein also plays a role in coagulation. It has been shown to interact with proteins involved in blood clotting, such as thrombin and factor XIa, and may play a role in regulating the coagulation process. This activity is particularly relevant in the context of wound healing, where the protein’s anti-inflammatory and pro-coagulant properties may work together to promote tissue repair.
Due to its various activities, Recombinant Human ITIH4 Protein has a wide range of applications in both research and therapeutic settings. In research, it is commonly used as an antigen in studies investigating the role of ITI family proteins in disease processes. It can also be used as a tool for studying the interactions between ITIH4 and other proteins, such as cytokines and proteases.
In the therapeutic setting, Recombinant Human ITIH4 Protein has potential applications in the treatment of inflammatory and coagulation disorders. Its anti-inflammatory activity makes it a promising candidate for the treatment of conditions such as rheumatoid arthritis and sepsis. Additionally, its role in coagulation may make it useful in promoting wound healing and preventing excessive bleeding in surgical procedures.
Recombinant Human ITIH4 Protein is a versatile protein with multiple activities that make it a valuable tool for scientific research and potential therapeutic applications. Its structural and functional properties make it a promising candidate for the treatment of inflammatory and coagulation disorders, and further studies on its interactions and mechanisms of action may reveal even more potential uses for this protein.
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