F1175
Follistatin 300 human
≥90% (SDS-PAGE), recombinant, expressed in Sf21 cells, lyophilized powder, suitable for cell culture
Synonym(s):
FS 300
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
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)
Related Categories
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).
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
Silvia Näf et al.
PloS one, 9(4), e92175-e92175 (2014-04-26)
The Activin A-Follistatin system has emerged as an important regulator of lipid and glucose metabolism with possible repercussions on fetal growth. To analyze circulating activin A, follistatin and follistatin-like-3 (FSTL3) levels and their relationship with glucose metabolism in pregnant women
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service