FSTL1 Human

Follistatin Like 1 Human Recombinant

Recombinant human FSTL1, produced in E. coli, is a single polypeptide chain comprising 309 amino acids (residues 21-308) with a molecular weight of 34.9 kDa. It features a 21 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23621
Source
E.coli.
Appearance
A sterile, colorless solution.

FSTL1 Human, HEK

Follistatin Like 1 Human Recombinant, HEK

Recombinant Human FSTL1, produced in HEK293 cells, is a single, glycosylated polypeptide chain encompassing amino acids 21-308 (a.a 21-308). It comprises 296 amino acids, including an 8 amino acid C-terminal His tag, and has a calculated molecular mass of 33.8kDa.
Shipped with Ice Packs
Cat. No.
BT23675
Source

HEK293 cells.

Appearance
White lyophilized powder (filtered).

FST Human

Follistatin Human Recombinant

Recombinant Human Follistatin, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 288 amino acids. It has a molecular weight of 31.5kDa. The purification of FST is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23290
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FST Human, His

Follistatin Human Recombinant, His Tag

FST His Protein is a 36.0 kDa protein. It consists of 325 amino acids, including the 315 amino acid sequence of FST His and a 10 amino acid N-terminal His-tag.
Shipped with Ice Packs
Cat. No.
BT23366
Source
E. coli.

FST Human, Sf9

Follistatin Human Recombinant, Sf9

This product contains human Follistatin (FST) protein produced in Sf9 insect cells. It is a single, glycosylated polypeptide chain with a molecular weight of 32.5kDa. The protein sequence includes a 7 amino acid His tag at the C-terminus. The product is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23447
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless liquid solution that is sterile.

FST Mouse

Follistatin Mouse Recombinant

Recombinant Mouse Follistatin, produced in E.Coli, is a single, non-glycosylated polypeptide chain comprising 289 amino acids. With a molecular weight of 31.6kDa, it undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23528
Source
Escherichia Coli.
Appearance
White lyophilized powder, sterile filtered.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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 .

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