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F2177 Sigma

Follistatin 288 from mouse

>95% (SDS-PAGE), recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder

Synonym: FS-288

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Properties

Related Categories Activins, Activins and Inhibins, Cell Biology, Cell Signaling and Neuroscience, Cytokines and Growth Factors,
recombinant   expressed in baculovirus infected Sf21 cells
assay   >95% (SDS-PAGE)
form   lyophilized powder
mol wt   calculated mol wt ~31 kDa
impurities   endotoxin, tested
storage temp.   −20°C
Gene Information   mouse ... Fst(14313)

Description

Analysis Note

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

Biochem/physiol Actions

High affinity activin-binding protein that can act as an activin antagonist.

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.

Packaging

25 μg in poly bottle

Physical form

Recombinant Mouse Follistatin 288 is supplied as a approximately 25 μg of protein lyophilized from a 0.2 μm filtered solution in 30% acetonitrile and 0.1% TFA containing 1.25 mg of bovine serum albumin.

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.

Price and Availability


All labs need water
Safety & Documentation

Safety Information

Symbol 
GHS05  GHS05
Signal word 
Danger
Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
3
Protocols & Articles
Peer-Reviewed Papers
15

References

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