Recombinant Human PTPRM, N-His

Reference: YHD80401
Product nameRecombinant Human PTPRM, N-His
Uniprot IDP28827
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 /SynonymsProtein-tyrosine phosphatase mu, R-PTP-mu, PTPRL1, PTPRM, Receptor-type tyrosine-protein phosphatase mu
ReferenceYHD80401
NoteFor research use only

Description of Recombinant Human PTPRM, N-His

Introduction

Recombinant Human PTPRM, N-His is a protein that has been genetically engineered to mimic the structure and function of the human protein tyrosine phosphatase receptor M (PTPRM). This protein is a crucial drug target in various diseases and has been extensively studied for its potential therapeutic applications. In this article, we will delve into the structure, activity, and potential applications of Recombinant Human PTPRM, N-His.

Structure of Recombinant Human PTPRM, N-His

Recombinant Human PTPRM, N-His is a 134 kDa protein that consists of 1185 amino acids. It is composed of a single catalytic domain, a transmembrane domain, and a cytoplasmic domain. The catalytic domain is responsible for the dephosphorylation activity of the protein, while the transmembrane and cytoplasmic domains are involved in signaling and cell adhesion processes.

The crystal structure of Recombinant Human PTPRM, N-His has been determined, revealing a similar overall fold to other members of the protein tyrosine phosphatase family. The catalytic domain contains a conserved active site, consisting of a cysteine residue and two arginine residues, that is essential for the dephosphorylation activity of the protein.

Activity of this protein

Recombinant Human PTPRM, N-His is a receptor-type protein tyrosine phosphatase, which means it is located on the cell membrane and plays a crucial role in cell signaling. It is involved in the regulation of various cellular processes, such as cell growth, differentiation, and migration. The main activity of Recombinant Human PTPRM, N-His is the dephosphorylation of tyrosine residues on target proteins, which leads to the modulation of downstream signaling pathways.

Studies have shown that Recombinant Human PTPRM, N-His has a high substrate specificity, with a preference for dephosphorylating proteins involved in cell adhesion and migration. This makes it a promising drug target for diseases where these processes are dysregulated, such as cancer and autoimmune disorders.

Applications of Recombinant Human PTPRM, N-His

Recombinant Human PTPRM, N-His has been extensively studied for its potential therapeutic applications. One of the most promising areas of research is in cancer treatment. Studies have shown that Recombinant Human PTPRM, N-His is downregulated in various types of cancer, and its expression is associated with better patient outcomes. This suggests that restoring the activity of Recombinant Human PTPRM, N-His could be a potential strategy for cancer therapy.

In addition to cancer, Recombinant Human PTPRM, N-His has also been investigated for its role in autoimmune diseases. It has been found that the protein is involved in regulating immune cell function and can potentially modulate the immune response in diseases such as multiple sclerosis and rheumatoid arthritis.

Furthermore, Recombinant Human PTPRM, N-His has also been studied for its potential in tissue repair and regeneration. It has been shown to promote the migration and proliferation of cells involved in wound healing, making it a promising candidate for tissue engineering and regenerative medicine.

Conclusion

In summary, Recombinant Human PTPRM, N-His is a genetically engineered protein that mimics the structure and function of the human protein tyrosine phosphatase receptor M. It plays a crucial role in cell signaling and has been extensively studied for its potential therapeutic applications in cancer, autoimmune diseases, and tissue repair. Further research on this protein could lead to the development of novel treatments for these diseases.

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