FST Human

Follistatin Human Recombinant
Cat. No.
BT23290
Source
Escherichia Coli.
Synonyms

FST, FS

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.
The FST is purified by proprietary chromatographic techniques.

Product Specs

Introduction

Follistatin is a protein found in the gonads that specifically blocks the release of follicle-stimulating hormone. There are two forms of the FST gene, FST317 and FST344, which produce proteins with 317 and 344 amino acids, respectively. These different forms are created through alternative splicing of the precursor mRNA. A study examining 37 potential genes for their link to polycystic ovary syndrome (PCOS) or high levels of androgens in 150 families found evidence suggesting a connection between PCOS and follistatin. Follistatin acts against the effects of ACTV and specifically prevents the production and release of follicle-stimulating hormone (FSH) from the pituitary gland.

Description
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.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a solution of 1mg/ml concentration without any additional additives.
Solubility
It is advised to reconstitute the lyophilized Follistatin in sterile 18MΩ-cm H2O to a concentration not less than 100µg/ml. This solution can be further diluted into other aqueous solutions.
Stability
Lyophilized Follistatin, while stable at room temperature for 3 weeks, should ideally be stored in dry conditions below -18°C. Once reconstituted, FST should be stored at 4°C for 2-7 days. For long-term storage, it is recommended to store below -18°C. To ensure optimal stability during long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by:
(a) Reverse-Phase High Performance Liquid Chromatography (RP-HPLC) analysis.
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity

The biological activity is assessed by the ability to counteract the inhibitory effect of ACTV on mouse MPC-11 cells. In the presence of 7.5ng/ml ACTV A, the anticipated ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg.

Synonyms

FST, FS

Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

Product Science Overview

Structure and Function

Follistatin is a member of the transforming growth factor-beta (TGF-β) superfamily signaling modulators. It binds to and inhibits the function of several proteins, including activin, myostatin, growth differentiation factors, and bone morphogenetic proteins (BMP) . By inhibiting these proteins, follistatin regulates various biological processes such as muscle growth, inflammation, and tissue repair.

Recombinant Human Follistatin

Recombinant human follistatin is produced using advanced biotechnological methods. It is typically derived from Chinese Hamster Ovary (CHO) cell lines or Spodoptera frugiperda (Sf 21) cells using baculovirus expression systems . The recombinant form is designed to mimic the natural protein’s structure and function, making it useful for research and therapeutic applications.

Applications in Research and Medicine

Recombinant human follistatin has several applications in scientific research and medicine:

  1. Muscle Growth and Regeneration: Follistatin’s ability to inhibit myostatin makes it a potential therapeutic agent for muscle-wasting diseases. By blocking myostatin, follistatin promotes muscle growth and regeneration.
  2. Inflammation and Tissue Repair: Follistatin’s role in modulating TGF-β signaling pathways makes it a valuable tool for studying inflammation and tissue repair mechanisms.
  3. Cancer Research: Follistatin’s interaction with activin and other growth factors is of interest in cancer research, as it may influence tumor growth and progression.
Stability and Storage

Recombinant human follistatin is typically lyophilized and stored at -20 to -70°C to maintain its stability . It is reconstituted in sterile PBS containing human or bovine serum albumin before use. Proper storage and handling are essential to preserve the protein’s activity and prevent degradation.

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