Recombinant Human SEM1 Protein, N-His-SUMO & C-Strep

Description of Recombinant Human SEM1 Protein, N-His-SUMO & C-Strep

Introduction

Recombinant Human SEM1 Protein, also known as Semenogelin-1, is a protein that is primarily found in the seminal fluid of males. It is encoded by the SEMG1 gene and is a member of the semenogelin family of proteins. Recombinant Human SEM1 Protein is commonly used in scientific research due to its unique structure and various activities.

Structure of Recombinant Human SEM1 Protein

Recombinant Human SEM1 Protein is a glycoprotein that consists of 416 amino acids and has a molecular weight of approximately 45 kDa. It is composed of three distinct domains: a central region, a proline-rich N-terminal domain, and a C-terminal domain. The central region contains a high percentage of hydrophobic amino acids, while the N-terminal domain is rich in proline residues. The C-terminal domain contains multiple cysteine residues, which allow for the formation of disulfide bonds.

The structure of Recombinant Human SEM1 Protein is highly conserved among different species, with a 97% sequence identity between humans and chimpanzees. This indicates the importance of this protein in reproductive function.

Activity of Recombinant Human SEM1 Protein

Recombinant Human SEM1 Protein has been found to have multiple activities, including antimicrobial, immunomodulatory, and protease inhibitory activities.

One of the main activities of Recombinant Human SEM1 Protein is its antimicrobial activity. It has been shown to inhibit the growth of various bacteria, including Escherichia coli, Staphylococcus aureus, and Streptococcus pyogenes. This activity is thought to be due to the high percentage of hydrophobic amino acids in the central region of the protein, which allows it to interact with and disrupt the cell membranes of these bacteria.

In addition to its antimicrobial activity, Recombinant Human SEM1 Protein also has immunomodulatory properties. It has been shown to stimulate the production of cytokines, which are important signaling molecules involved in the immune response. This activity may play a role in the protection of the male reproductive system from infections.

Recombinant Human SEM1 Protein also has protease inhibitory activity, specifically against serine proteases. This activity is due to the presence of multiple cysteine residues in the C-terminal domain, which form disulfide bonds with the active site of these proteases, inhibiting their activity. This activity may be important in maintaining the integrity of the seminal fluid and protecting the sperm from damage.

Application of Recombinant Human SEM1 Protein

Due to its unique structure and multiple activities, Recombinant Human SEM1 Protein has a variety of applications in scientific research.

One of the main applications of Recombinant Human SEM1 Protein is in the study of male reproductive function. It is commonly used as an antigen in immunoassays to measure levels of this protein in seminal fluid. Changes in the levels of Recombinant Human SEM1 Protein have been associated with various reproductive disorders, making it a valuable biomarker for diagnosis and monitoring of these conditions.

Recombinant Human SEM1 Protein is also used in the development of antimicrobial agents. Its antimicrobial activity has been found to be effective against a wide range of bacteria, making it a potential candidate for the development of new antibiotics.

Furthermore, Recombinant Human SEM1 Protein has been studied for its potential use in male contraceptive methods. Its ability to inhibit sperm motility and interact with the female reproductive tract has shown promise in the development of non-hormonal male contraceptives.

Conclusion

In conclusion, Recombinant Human SEM1 Protein is a unique and multifunctional protein that plays an important role in male reproductive function. Its structure, activities, and various applications make it a valuable tool in