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Key Documents

F1175

Sigma-Aldrich

Follistatin 300 human

≥90% (SDS-PAGE), recombinant, expressed in Sf21 cells, lyophilized powder, suitable for cell culture

Synonyme(s) :

FS 300

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About This Item

Numéro MDL:
Code UNSPSC :
51111800
Nomenclature NACRES :
NA.32

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in Sf21 cells

Pureté

≥90% (SDS-PAGE)

Forme

lyophilized powder

Puissance

0.1-0.4 mg per mL

Poids mol.

31 kDa

Conditionnement

pkg of 25 μg

Conditions de stockage

avoid repeated freeze/thaw cycles

Technique(s)

cell culture | mammalian: suitable

Impuretés

endotoxin, tested

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

human ... FST(10468)

Description générale

FST (follistatin) is an activin-binding protein, and exists in two isoforms due to alternate splicing, FS288 and FS315. It is a glycoprotein with a single chain, and acts as an activin antagonist. It has a high level of expression in fetal membranes and placenta.

Application

FST (follistatin) has been used for trophoblast fusion assay and the measure of hCG (human chorionic gonadotropin) concentration in hormone assays. It is also suitable for the development of chondrocytes from hESc (human embryonic stem cells) by a new 3-Stage directed differentiation protocol (DDP).

Actions biochimiques/physiologiques

FST (follistatin) binds to and regulates activins, which in turn are TGF (transforming growth factor)-β superfamily members. The expression level of FST and its binding partner activin A is elevated in inflammatory disorders. The activin A-follistatin system plays an essential role in the modulation of glucose and lipid metabolism, which might have an overall effect on fetal growth. In adipose tissue, it facilitates the adipogenic differentiation of progenitor cells.
High-affinity activin-binding protein that can act as an activin antagonist.

Forme physique

Lyophilized from a solution in 30% acetonitrile and 0.1% trifluoroacetic acid containing 1.25 mg bovine serum albumin.

Remarque sur l'analyse

The biological activity is measured by its ability to neutralize activin-induced bioactivity on K562 cells (erythroid differentiation).

Pictogrammes

Corrosion

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Eye Dam. 1 - Skin Irrit. 2

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

O Hashimoto et al.
The Journal of biological chemistry, 272(21), 13835-13842 (1997-05-23)
There are two types of the activin-binding protein follistatin (FS), FS-288 and FS-315. These result from alternative splicing of mRNA. FS-288 exhibits high affinity for cell-surface heparan sulfate proteoglycans, whereas FS-315 shows low affinity. To understand the physiological role of
Rachel A Oldershaw et al.
StemBook, 2012 Jun 10 (2013-05-10)
We have developed for hESc a new 3-Stage directed differentiation protocol (DDP) to generate chondrocytes, the specialized cells that form cartilage tissue. The protocol is segmented into stages that mimic the developmental processes that occur in cell lineage specification during
S Iemura et al.
Proceedings of the National Academy of Sciences of the United States of America, 95(16), 9337-9342 (1998-08-05)
In early development of Xenopus laevis, it is known that activities of polypeptide growth factors are negatively regulated by their binding proteins. In this study, follistatin, originally known as an activin-binding protein, was shown to inhibit all aspects of bone
Q Guo et al.
Molecular endocrinology (Baltimore, Md.), 12(1), 96-106 (1998-01-24)
Follistatin is an activin-binding protein that can act as an activin antagonist in vitro. Follistatin also binds heparin sulfate proteoglycans and may function as a reservoir for activins in vivo. In the mouse, follistatin mRNA is first detected in the
Rita Linko et al.
BMC infectious diseases, 14, 253-253 (2014-06-03)
Activin A and its binding protein follistatin (FS) are increased in inflammatory disorders and sepsis. Overexpression of activin A in the lung causes similar histopathological changes as acute respiratory distress syndrome (ARDS). ARDS and severe respiratory failure are complications of

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