FST Human, His

Follistatin Human Recombinant, His Tag
Cat. No.
BT23366
Source
E. coli.
Synonyms
FST, FS, Activin-binding protein.
Appearance
Purity
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.

Product Specs

Introduction
Follistatin is a protein that regulates follicle-stimulating hormone (FSH) release. It exists in two forms, FST317 and FST344, created by alternative splicing. Research suggests a potential link between follistatin and polycystic ovary syndrome (PCOS), a hormonal disorder. Follistatin counteracts the effects of activin, effectively inhibiting FSH production in the pituitary gland.
Description
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.
Formulation
The FST His Tag protein solution was passed through a 0.4 micrometer filter and then lyophilized. The initial concentration before lyophilization was 0.5mg/ml in a buffer of 20mM TRIS and 20mM NaCl at a pH of 7.5.
Solubility
To prepare a working solution, add deionized water to the lyophilized pellet to achieve a concentration of approximately 0.5mg/ml. Allow the pellet to dissolve completely. This product is not sterile. Before using in cell culture, ensure sterility by filtering the solution through a sterile filter.
Stability
Store the lyophilized FST His at -20°C. After reconstitution, aliquot the solution to minimize freeze-thaw cycles. Reconstituted FST His can be stored at 4°C for up to two weeks without degradation.
Synonyms
FST, FS, Activin-binding protein.
Source
E. coli.
Amino Acid Sequence
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

Product Science Overview

Structure and Function

Follistatin is known for its ability to bind and neutralize members of the transforming growth factor-beta (TGF-β) superfamily, particularly activin . By binding to activin, follistatin functions as an activin antagonist, thereby inhibiting the biosynthesis and secretion of pituitary FSH . This interaction is crucial for regulating various physiological processes, including reproductive functions, cell growth, and differentiation .

Expression and Role in the Body

Follistatin is expressed in numerous tissues beyond the gonads, including the brain, adrenal glands, bone marrow, and placenta . It plays a significant role in early embryogenesis and is involved in local regulatory functions in these tissues . The activin-follistatin system is particularly important in the anterior pituitary, the classical target tissue for inhibin .

Recombinant Human Follistatin (His Tag)

Recombinant human follistatin, tagged with a histidine (His) tag, is produced using expression systems such as HEK293 cells . The His tag facilitates purification and detection of the protein. The recombinant protein is typically lyophilized and can be reconstituted for use in various research applications . It is measured for its ability to neutralize activin-mediated inhibition on cell proliferation, with an effective dose (ED50) typically ranging from 5-40 ng/mL .

Applications in Research

Recombinant human follistatin is widely used in research to study its role in various biological processes and diseases. It has been linked to conditions such as polycystic ovary syndrome (PCOS) and hyperandrogenemia . Additionally, follistatin’s regulatory roles in extragonadal tissues make it a valuable tool for investigating its functions in different physiological contexts .

Storage and Handling

Lyophilized recombinant follistatin is stable for up to 12 months when stored at -20 to -80°C . Once reconstituted, the protein solution can be stored at 4-8°C for 2-7 days, and aliquots can be kept at -20°C for up to 3 months . It is typically formulated in sterile PBS with added protectants such as trehalose, mannitol, and Tween80 .

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