FST Mouse

Follistatin Mouse Recombinant
Cat. No.
BT23528
Source
Escherichia Coli.
Synonyms
Follistatin, FST, FS, Activin-binding protein, AL033346.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY.They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Follistatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids and having a total molecular mass of 31.6kDa.
The FST is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Follistatin, a single-chain gonadal protein, plays a crucial role in regulating follicle-stimulating hormone (FSH) release. It exists in two isoforms, FST317 and FST344, differing in amino acid count due to alternative splicing of precursor mRNA. Studies have revealed a potential link between follistatin and polycystic ovary syndrome (PCOS). Functioning as an activin antagonist, follistatin directly interacts with activin, effectively inhibiting the production and secretion of pituitary FSH.
Description
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.
Physical Appearance
White lyophilized powder, sterile filtered.
Formulation
Mouse Follistatin undergoes lyophilization in a buffer solution of 10mM Na₂PO₄ and 50mM NaCl, at a pH of 7.5.
Solubility
For reconstitution, it is recommended to dissolve the lyophilized Follistatin in sterile 18MΩ-cm H2O at a concentration not less than 100µg/ml. Further dilutions can be made using other aqueous solutions.
Stability
Lyophilized Follistatin remains stable at room temperature for up to 3 weeks. However, for extended storage, it is recommended to store desiccated below -18°C. Upon reconstitution, FST should be stored at 4°C for 2-7 days. For long-term storage, adding a carrier protein like 0.1% HSA or BSA is advisable. Avoid freeze-thaw cycles.
Purity
Purity exceeds 90.0% as assessed by SDS-PAGE.
Biological Activity
The ED₅₀, representing the dose required for 50% neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, falls within the range of 0.13-0.19µg/ml.
Synonyms
Follistatin, FST, FS, Activin-binding protein, AL033346.
Source
Escherichia Coli.
Amino Acid Sequence
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.

Product Science Overview

Structure and Function

Follistatin is a glycoprotein that exists in multiple isoforms, primarily Follistatin-288 (FS-288) and Follistatin-315 (FS-315), which differ in their ability to bind heparin and cell surface proteoglycans. The recombinant mouse Follistatin used in research is often derived from the Spodoptera frugiperda (Sf 21) cell line using baculovirus expression systems .

The primary function of Follistatin is to bind and neutralize members of the TGF-β superfamily, particularly activins. By inhibiting activins, Follistatin regulates various physiological processes, including muscle growth, inflammation, and reproductive functions .

Biological Significance
  1. Muscle Growth: Follistatin has gained significant attention for its role in muscle development. It inhibits myostatin, a negative regulator of muscle growth, thereby promoting muscle hypertrophy. This property makes Follistatin a potential therapeutic target for muscle-wasting diseases.

  2. Reproductive Health: Follistatin is involved in the regulation of reproductive hormones. By inhibiting activins, it modulates the secretion of follicle-stimulating hormone (FSH), which is essential for reproductive health.

  3. Inflammation and Wound Healing: Follistatin also plays a role in modulating inflammatory responses and promoting wound healing. Its ability to bind and neutralize activins helps in controlling inflammation and tissue repair processes.

Applications in Research

Recombinant mouse Follistatin is widely used in research to study its various biological functions and potential therapeutic applications. It is utilized in experiments involving muscle growth, reproductive health, and inflammatory responses. The recombinant protein is typically produced in a carrier-free form to avoid interference from other proteins, ensuring accurate and reliable results in experimental settings .

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