Alpha-1-fetoprotein recombinant protein

Reference: PX-P6414-100
Product nameAlpha-1-fetoprotein recombinant protein
Origin speciesHomo sapiens (Human)
Expression systemEukaryotic expression
Molecular weight68.58 kDa
Protein delivered with Tag?C-Terminal His Tag
Purity estimated>90% by SDS-PAGE
BufferPBS pH 7.4, 1mM EDTA, 4% Trehalose, 1% Mannitol
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)
BrandProteoGenix
Host speciesMammalian cells
Fragment TypeMet1-Val609
Aliases /SynonymsAlpha-fetoprotein, Alpha-1-fetoprotein, Alpha-fetoglobulin, AFP, HPAFP
ReferencePX-P6414
NoteFor research use only.

Description of Alpha-1-fetoprotein recombinant protein

Introduction:

Alpha-fetoprotein (AFP) is a glycoprotein that is primarily produced by the fetal liver and yolk sac during embryonic development. It is also found in small amounts in adults, mainly in the liver, but its function in adults is still not fully understood. AFP has been extensively studied due to its potential as a biomarker for various diseases, including liver cancer. In recent years, a recombinant form of AFP, known as Human AFP/Alpha-fetoprotein (HPAFP), has been developed and is being investigated as a potential drug target. In this article, we will discuss the structure, activity, and applications of AFP and HPAFP in drug targeting.

Structure of AFP and HPAFP:

AFP is a single-chain polypeptide with a molecular weight of approximately 70 kDa. It is composed of 591 amino acids and has a unique three-dimensional structure. The protein consists of four domains, including a signal peptide, a glycosylated domain, a linker region, and a C-terminal domain. The glycosylated domain is responsible for the high carbohydrate content of AFP, which accounts for approximately 30% of its total weight.

HPAFP, on the other hand, is a recombinant form of AFP that is produced using genetic engineering techniques. It has the same amino acid sequence as natural AFP, but it lacks the glycosylated domain, making it a non-glycosylated protein. This modification has been shown to increase the stability and solubility of HPAFP, making it a more suitable candidate for drug targeting.

Activity of AFP and HPAFP:

AFP and HPAFP have been shown to have multiple activities in the body. In fetuses, AFP plays a crucial role in transporting nutrients from the mother to the developing fetus. It also acts as an immunomodulator, helping to regulate the immune response during pregnancy. In adults, the function of AFP is not well understood, but it is believed to play a role in tissue repair and regeneration.

HPAFP, on the other hand, has been shown to have anti-inflammatory and immunomodulatory activities. Studies have also demonstrated its ability to inhibit the growth of cancer cells and promote apoptosis (cell death) in tumor cells. This makes HPAFP a promising drug target for the treatment of various diseases, including cancer.

Applications of AFP and HPAFP in Drug Targeting:

AFP and HPAFP have been investigated for their potential use as drug targets in various diseases. In cancer, AFP levels have been found to be elevated in patients with liver cancer, making it a potential biomarker for early detection and monitoring of the disease. HPAFP, with its improved stability and solubility, has been studied as a potential therapeutic agent for the treatment of liver cancer.

In addition to cancer, HPAFP has also been investigated for its potential use in autoimmune diseases. Its anti-inflammatory and immunomodulatory properties make it a promising candidate for the treatment of diseases such as rheumatoid arthritis and multiple sclerosis. HPAFP has also shown potential in tissue engineering, as it has been shown to promote the growth and differentiation of stem cells.

Conclusion:

In summary, AFP and its recombinant form, HPAFP, have unique structures and multiple activities in the body. While the exact function of AFP in adults is still not fully understood, HPAFP has shown promising potential as a drug target for the treatment of various diseases. Further research and clinical trials are needed to fully explore the applications of HPAFP in drug targeting and its potential to improve patient outcomes.

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