Recombinant Human CEMIP, N-His

Reference: YHJ29402
Product nameRecombinant Human CEMIP, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight14.79 kDa
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 TypeThr31-Lys166
Aliases /SynonymsCEMIP, Cell migration-inducing and hyaluronan-binding protein, KIAA1199
ReferenceYHJ29402
NoteFor research use only.

Description of Recombinant Human CEMIP, N-His

Introduction

Recombinant Human CEMIP (Cell Migration-Inducing Protein) is a protein that plays a crucial role in cell migration and invasion. It is a transmembrane glycoprotein that is encoded by the CEMIP gene. This protein has been extensively studied and has shown promising potential in various biological processes. In this article, we will provide a scientific description of the structure, activity, and application of Recombinant Human CEMIP.

Structure of Recombinant Human CEMIP

Recombinant Human CEMIP is a 120 kDa protein that consists of 1023 amino acids. It is composed of multiple domains, including a signal peptide, a transmembrane domain, and a cytoplasmic tail. The extracellular region of CEMIP contains a C-type lectin domain, a mucin-like domain, and a von Willebrand factor A domain. These domains play a crucial role in cell adhesion and migration.

Activity of Recombinant Human CEMIP

Recombinant Human CEMIP is primarily known for its role in cell migration and invasion. It is expressed in various cells, including epithelial cells, fibroblasts, and immune cells. This protein has been shown to promote cell migration by interacting with integrins and promoting the formation of focal adhesions. It also plays a crucial role in the epithelial-mesenchymal transition (EMT), a process that is essential for cancer metastasis.

Apart from its role in cell migration, Recombinant Human CEMIP has also been implicated in other biological processes. It has been shown to regulate cell proliferation, survival, and apoptosis. It also plays a role in angiogenesis and wound healing. Additionally, CEMIP has been reported to modulate the immune response by regulating the activation and migration of immune cells.

Application of Recombinant Human CEMIP

Recombinant Human CEMIP has shown potential for various applications in the field of biotechnology and medicine. One of the major applications of this protein is in cancer research. Its role in promoting cell migration and invasion makes it a potential target for cancer therapy. In fact, studies have shown that inhibiting CEMIP expression can reduce cancer cell invasion and metastasis.

Apart from cancer, Recombinant Human CEMIP has also shown promise in wound healing and tissue regeneration. Its role in promoting cell migration and angiogenesis makes it a potential therapeutic agent for promoting tissue repair. Additionally, CEMIP has also been studied for its potential in modulating the immune response in diseases such as autoimmune disorders and infections.

Recombinant Human CEMIP is also widely used as an antigen for antibody production. Its high expression in cancer cells and its role in promoting cell migration and invasion make it an ideal target for cancer-specific antibodies. These antibodies can be used for diagnostic purposes and targeted therapy.

Conclusion

Recombinant Human CEMIP is a protein with diverse biological functions. Its role in cell migration and invasion, as well as its potential in cancer therapy, wound healing, and immune modulation, make it a promising target for further research and development. With its unique structure and activity, Recombinant Human CEMIP has the potential to contribute to various fields of biotechnology and medicine.

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