Recombinant Human ITIH2, N-His

Reference: YHD35601
Product nameRecombinant Human ITIH2, N-His
Uniprot IDP19823
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
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)
Aliases /SynonymsSHAP, ITI heavy chain H2, Serum-derived hyaluronan-associated protein, ITI-HC2, Inter-alpha-trypsin inhibitor complex component II, Inter-alpha-inhibitor heavy chain 2, ITIH2, Inter-alpha-trypsin inhibitor heavy chain H2, IGHEP2
ReferenceYHD35601
NoteFor research use only

Description of Recombinant Human ITIH2, N-His

Introduction

Recombinant Human ITIH2, N-His is a highly promising drug target that has gained significant attention in recent years due to its potential therapeutic applications. This protein is a member of the inter-alpha-trypsin inhibitor (ITI) family and is involved in various physiological processes such as inflammation, coagulation, and wound healing. In this article, we will discuss the structure, activity, and potential applications of Recombinant Human ITIH2, N-His.

Structure of Recombinant Human ITIH2, N-His

Recombinant Human ITIH2, N-His is a 120 kDa glycoprotein that consists of 940 amino acids. It is composed of a heavy chain (H1) and a light chain (L1), which are connected by a disulfide bond. The H1 chain contains a von Willebrand factor type A (vWFA) domain, a chondroitin sulfate attachment site, and a C-terminal cystatin-like domain. The L1 chain, on the other hand, contains a Kunitz-type protease inhibitor domain and a C-terminal low-density lipoprotein receptor class A (LDLRA) domain.

Activity of this protein

Recombinant Human ITIH2, N-His has been shown to have multiple activities, including anti-inflammatory, anticoagulant, and wound healing properties. The vWFA domain of the H1 chain is responsible for the protein’s anti-inflammatory activity by inhibiting the binding of leukocytes to the endothelium. This prevents the recruitment of inflammatory cells to the site of injury, reducing inflammation.

The Kunitz-type protease inhibitor domain of the L1 chain has anticoagulant activity by inhibiting the activity of serine proteases involved in the coagulation cascade. This prevents the formation of blood clots, which is crucial in wound healing and preventing thrombotic disorders.

The C-terminal cystatin-like domain of the H1 chain has been shown to have wound healing properties by promoting cell migration and proliferation. This domain interacts with the extracellular matrix and promotes the formation of new blood vessels, aiding in tissue repair and regeneration.

Applications of Recombinant Human ITIH2, N-His

Recombinant Human ITIH2, N-His has shown potential in various therapeutic applications, including inflammatory diseases, coagulation disorders, and wound healing. Its anti-inflammatory activity makes it a promising drug target for conditions such as rheumatoid arthritis, asthma, and inflammatory bowel disease.

The anticoagulant activity of Recombinant Human ITIH2, N-His can be utilized in the treatment of thrombotic disorders, such as deep vein thrombosis and pulmonary embolism. It can also be used in surgical procedures to prevent blood clots and promote wound healing.

The wound healing properties of Recombinant Human ITIH2, N-His make it a potential treatment for chronic wounds, such as diabetic ulcers and pressure sores. It can also be used in tissue engineering to promote the regeneration of damaged tissues and organs.

Conclusion

In summary, Recombinant Human ITIH2, N-His is a promising drug target with multiple activities and potential therapeutic applications. Its structure, consisting of a vWFA domain, Kunitz-type protease inhibitor domain, and cystatin-like domain, allows it to have anti-inflammatory, anticoagulant, and wound healing properties. Further research and development of this protein could lead to new treatments for various diseases and conditions.

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