AMH Human
Escherichia Coli.
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Greater than 95.0% as determined by SDS-PAGE.
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Description
AMH Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain (a.a 452-560) containing 118 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 12.8kDa (calculated).
Product Specs
Anti-Mullerian Hormone (AMH), a member of the TGF-beta family, is a glycoprotein produced by testicular Sertoli cells. It induces the regression of the Mullerian duct during fetal development. AMH also has roles in inhibiting the growth of tumors originating from Mullerian duct tissues, influencing Leydig cell development and function, and contributing to follicular development in adult females.
Recombinant human AMH, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of amino acids 452-560. This includes a 9 amino acid N-terminal His tag, resulting in a total calculated molecular mass of 12.8kDa.
The AMH undergoes filtration (0.4 µm) and lyophilization in a solution of 1mM HCl and 5% (w/v) trehalose.
To prepare a working stock solution, add deionized water to the lyophilized pellet, aiming for a concentration of approximately 0.5mg/ml. Allow complete dissolution. Note: This AMH product is not sterile. Before using in cell culture, filter it through an appropriate sterile filter.
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. While the reconstituted protein can be stored at 4°C for a limited period, it remains stable for at least one week at this temperature.
SDS-PAGE analysis indicates a purity greater than 95.0%.
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Escherichia Coli.
MKHHHHHHAS AGATAADGPC ALRELSVDLR AERSVLIPET YQANNCQGVC GWPQSDRNPR YGNHVVLLLK MQARGAALAR PPCCVPTAYA GKLLISLSEE RISAHHVPNM VATECGCR
Product Science Overview
AMH was first recognized in the mid-20th century by Alfred Jost, who discovered its role in the regression of the Mullerian ducts in male embryos . The hormone is produced by Sertoli cells in the testes of male fetuses and is responsible for inhibiting the development of female reproductive structures, thereby promoting male differentiation . In females, AMH is produced by granulosa cells in the ovaries and is involved in the regulation of folliculogenesis and ovarian reserve .
Human recombinant AMH is a laboratory-produced version of the naturally occurring hormone. It is created using recombinant DNA technology, which involves inserting the gene that encodes AMH into a host cell, such as bacteria or yeast, to produce the hormone in large quantities. This recombinant form is used in various research and clinical applications, including the calibration of immunoassays to measure AMH levels in human serum and plasma .
AMH levels are used as a biomarker for several clinical conditions. In women, AMH is a key indicator of ovarian reserve and is used in the assessment of fertility potential. It is also used in the diagnosis and management of polycystic ovary syndrome (PCOS) and premature ovarian failure . In men, AMH levels can be used to evaluate testicular function and diagnose disorders of sexual development .
Recent studies have explored the potential therapeutic applications of AMH. For instance, it has been investigated for its role in inhibiting the initiation of growth of human ovarian follicles, which could have implications for fertility preservation and treatment of ovarian disorders . Additionally, recombinant AMH is being studied for its potential use in treating certain types of cancer, such as ovarian and prostate cancer, due to its ability to inhibit cell proliferation .
