Cytokines
Product List
FST Human
Follistatin Human Recombinant
The FST is purified by proprietary chromatographic techniques.
FST Human, His
Follistatin Human Recombinant, His Tag
FST Human, Sf9
Follistatin Human Recombinant, Sf9
FST is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
FST Mouse
Follistatin Mouse Recombinant
The FST is purified by proprietary chromatographic techniques.
FSTL1 Human
Follistatin Like 1 Human Recombinant
FSTL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
FSTL1 Human, HEK
Follistatin Like 1 Human Recombinant, HEK
FSTL1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-308) containing 296 amino acids including a 8 a.a C-terminal His tag. The total molecular mass is 33.8kDa (calculated).
HEK293 cells.
Introduction
Follistatin, also known as activin-binding protein, is a secreted glycoprotein encoded by the FST gene in humans . It belongs to the TGF-β superfamily and is characterized by its ability to bind and neutralize activins, myostatin, and bone morphogenetic proteins (BMPs) . Follistatin exists in multiple isoforms, including FS-288, FS-300, and FS-315, which are generated through alternative splicing and post-translational modifications .
Follistatin is expressed in nearly all tissues of higher animals, with the highest concentrations found in the ovaries and skin . It plays a crucial role in various biological processes, including embryonic development, muscle growth, and tissue repair . The expression patterns of follistatin are tissue-specific, with notable expression in the liver, endometrium, and various other tissues .
Follistatin’s primary function is to bind and neutralize activins, thereby inhibiting their biological activity . This inhibition is essential for regulating processes such as follicle-stimulating hormone (FSH) secretion, muscle growth, and inflammation . Additionally, follistatin plays a role in immune responses and pathogen recognition by modulating the activity of TGF-β family members .
Follistatin exerts its effects by binding to activins, myostatin, and BMPs, preventing them from interacting with their receptors . This binding is highly specific and nearly irreversible, effectively neutralizing the target proteins . Follistatin’s interaction with these molecules triggers downstream signaling cascades that regulate various cellular processes, including cell proliferation, differentiation, and apoptosis .
The expression and activity of follistatin are tightly regulated at multiple levels. Transcriptional regulation involves various transcription factors and signaling pathways that modulate FST gene expression . Post-translational modifications, such as proteolytic cleavage and glycosylation, further influence follistatin’s stability and activity . Additionally, the glucagon-to-insulin ratio has been shown to regulate circulating follistatin levels .
Follistatin has significant applications in biomedical research, particularly in the fields of muscle growth and regenerative medicine . It is being explored as a therapeutic strategy for conditions such as muscle wasting, fibrosis, and certain cancers . Follistatin’s ability to modulate TGF-β family members makes it a valuable tool for developing diagnostic and therapeutic approaches .
Throughout the life cycle, follistatin plays a critical role in various stages of development, from embryogenesis to aging . During embryonic development, it is involved in processes such as neural plate formation and folliculogenesis . In adulthood, follistatin continues to regulate muscle growth, tissue repair, and immune responses . Its dysregulation has been associated with aging-related conditions and diseases, highlighting its importance in maintaining physiological homeostasis .
