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F1175

Sigma-Aldrich

Follistatin 300 human

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

Synonym(s):

FS 300

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About This Item

MDL number:
UNSPSC Code:
51111800
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in Sf21 cells

Assay

≥90% (SDS-PAGE)

form

lyophilized powder

potency

0.1-0.4 mg per mL

mol wt

31 kDa

packaging

pkg of 25 μg

storage condition

avoid repeated freeze/thaw cycles

technique(s)

cell culture | mammalian: suitable

impurities

endotoxin, tested

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... FST(10468)

General description

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).

Biochem/physiol Actions

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.

Physical form

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

Analysis Note

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

Pictograms

Corrosion

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Eye Dam. 1 - Skin Irrit. 2

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
S Dasgupta et al.
Journal of postgraduate medicine, 58(3), 190-193 (2012-10-02)
Out of a panel of 37 candidate genes tested for linkage with polycystic ovary syndrome (PCOS), the strongest evidence of linkage was reported in the follistatin (FST) gene region. Subsequently, a couple of studies outside India investigated the FST gene

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