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Brand: ProteoGenix

Recombinant Human SEMG1 Protein, N-GST & C-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
32.80 kDa

329.00

100ug + 329 loyalty points
Thr68–Leu107
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Recombinant Human SEMG1 Protein, N-GST & C-His

Recombinant Human SEMG1 Protein, N-GST & C-His

Product name Recombinant Human SEMG1 Protein, N-GST & C-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 32.80 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
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 ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Thr68-Leu107
Aliases /Synonyms Semenogelin-1, Semenogelin I, SGI, SEMG1, Cancer/testis antigen 103, SEMG
Reference ARO-P11288
Note For research use only.
Molecular Constructor
Thr68–Leu107

Introduction

Recombinant Human SEMG1 Protein, also known as Semenogelin-1, is a protein that is found in human semen and is involved in the process of sperm coagulation. It is a member of the semenogelin family of proteins and is encoded by the SEMG1 gene. Recombinant Human SEMG1 Protein is produced through genetic engineering techniques and has a wide range of applications in both research and medical fields.

Structure of Recombinant Human SEMG1 Protein

Recombinant Human SEMG1 Protein is a glycoprotein that is composed of 359 amino acids and has a molecular weight of approximately 39 kDa. It is made up of two main domains, the N-terminal domain and the C-terminal domain. The N-terminal domain is responsible for the coagulation activity of the protein, while the C-terminal domain is involved in the interaction with other proteins and carbohydrates.

The N-terminal domain of Recombinant Human SEMG1 Protein contains a high proportion of cysteine residues, which are important for the formation of disulfide bonds and the stability of the protein structure. The C-terminal domain, on the other hand, contains a large number of serine and threonine residues, which are potential sites for post-translational modifications such as glycosylation.

Activity of Recombinant Human SEMG1 Protein

Recombinant Human SEMG1 Protein is primarily known for its role in sperm coagulation, which is an essential step in the process of fertilization. During ejaculation, semenogelin-1 is secreted by the seminal vesicles and forms a gel-like substance that helps to trap and immobilize sperm. This allows for a more efficient delivery of sperm to the female reproductive tract and increases the chances of successful fertilization.

In addition to its function in sperm coagulation, Recombinant Human SEMG1 Protein has also been found to have antibacterial properties. It has been shown to inhibit the growth of certain bacteria, including Escherichia coli and Staphylococcus aureus, by disrupting their cell membranes. This makes it a potential candidate for the development of new antimicrobial agents.

Application of Recombinant Human SEMG1 Protein

Recombinant Human SEMG1 Protein has a wide range of applications in both research and medical fields. In research, it is commonly used as an antigen to study the immune response to sperm and its role in fertility. It can also be used as a tool to study the structure and function of other proteins involved in sperm coagulation.

In the medical field, Recombinant Human SEMG1 Protein has potential applications in the treatment of male infertility. As it is a key player in sperm coagulation, it may be used to develop new methods of contraception or fertility treatments. It may also have potential therapeutic uses in the treatment of bacterial infections, as mentioned earlier.

Conclusion

In summary, Recombinant Human SEMG1 Protein is a glycoprotein that plays a crucial role in sperm coagulation and has potential applications in both research and medical fields. Its unique structure and diverse functions make it a valuable tool for studying fertility and developing new treatments. With further research, this protein may hold even more promise for the future of reproductive health and antimicrobial therapy.

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