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Merck

F1175

Sigma-Aldrich

Follistatin 300 human

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

Synonym(e):

FS 300

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About This Item

MDL-Nummer:
UNSPSC-Code:
51111800
NACRES:
NA.32

Biologische Quelle

human

Qualitätsniveau

Rekombinant

expressed in Sf21 cells

Assay

≥90% (SDS-PAGE)

Form

lyophilized powder

Wirksamkeit

0.1-0.4 mg per mL

Mol-Gew.

31 kDa

Verpackung

pkg of 25 μg

Lagerbedingungen

avoid repeated freeze/thaw cycles

Methode(n)

cell culture | mammalian: suitable

Verunreinigungen

endotoxin, tested

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

Angaben zum Gen

human ... FST(10468)

Allgemeine Beschreibung

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.

Anwendung

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. Wirkung

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.

Physikalische Form

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

Hinweis zur Analyse

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

Piktogramme

Corrosion

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Eye Dam. 1 - Skin Irrit. 2

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Die Dokumentenbibliothek aufrufen

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
Pascale Gerbaud et al.
Endocrinology, 152(12), 5017-5028 (2011-09-29)
Placental development is markedly abnormal in trisomy 21 (T21) pregnancies. We hypothesized that abnormal paracrine cross talk between the fetal mesenchymal core and the trophoblast might be involved in the defect of syncytiotrophoblast formation and function. In a large series

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