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SRP3045

Sigma-Aldrich

Follistatin human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Synonym(s):

FS, activins-binding protein

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

potency

0.1-0.4 μg/mL

mol wt

31.5 kDa

packaging

pkg of 20 μg

technique(s)

cell culture | mammalian: suitable

impurities

<1.0 EU/μg endotoxin, tested

color

white to off-white

suitability

suitable for molecular biology

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... FST(10468)

General description

Research area: Cell Signaling

Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. The gene is mapped to human chromosome 5q11.2. Recombinant human Follistatin is a 31.5kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.

Application

Follistatin human has been used to suppress myostatin signaling. It has also been used as an inhibitor of activin A.

Biochem/physiol Actions

Follistatin is a multifunctional secreted protein that binds to ligands of the TGF (transforming growth factor)-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as an activin antagonist whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle-stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF (transforming growth factor)-β ligands including BMP (bone morphogenetic protein)-2,-4,-6,-7, Myostatin, GDF-11 (growth differentiation factor 11), and TGF-b1. In gonads, it is responsible for oocyte competence and embryo development. In the pituitary gland, it causes cyclic changes in FSH production in the estrous cycle. Follistatin also participates in bone metabolism. It controls inflammation, fibrosis, and tissue repair. Levels of plasma follistatin increase in polycystic ovary syndrome and type 2 diabetes. Follistatin might also be involved in tumor progression, including apoptosis, angiogenesis, and metastasis.

Sequence

GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCN

Physical form

Lyophilized from 10 mM sodium phosphate, 50 mM sodium chloride, pH 7.5.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

13 - Non 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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Serum Levels of Follistatin Are Positively Associated With Serum-Free Thyroxine Levels in Patients With Hyperthyroidism or Euthyroidism.
Tseng FY, et al.
Medicine, 95, e2661-e2661 (2016)
Regulation of ovarian function by the TGF-beta superfamily and follistatin.
Lin SY, et al.
Reproduction (Cambridge, England), 126, 133-148 (2003)
Myostatin knockout drives browning of white adipose tissue through activating the AMPK-PGC1a-Fndc5 pathway in muscle.
Shan T, et al.
Faseb Journal, 27, 1981-1989 (2013)
S Inouye et al.
Endocrinology, 129(2), 815-822 (1991-08-01)
Follistatin is a glycosylated monomeric protein originally isolated from ovarian follicular fluid based on its ability to specifically inhibit pituitary FSH release. To further explore the physiological role of follistatin, we have expressed recombinant human follistatins with 315 (rhFS-315) and
Inhibins, activins, and follistatins: the saga continues.
L V DePaolo
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), 214(4), 328-339 (1997-04-01)

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