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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

Sinónimos:

FS 300

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About This Item

Número MDL:
Código UNSPSC:
51111800
NACRES:
NA.32

origen biológico

human

Nivel de calidad

recombinante

expressed in Sf21 cells

Ensayo

≥90% (SDS-PAGE)

Formulario

lyophilized powder

potencia

0.1-0.4 mg per mL

mol peso

31 kDa

envase

pkg of 25 μg

condiciones de almacenamiento

avoid repeated freeze/thaw cycles

técnicas

cell culture | mammalian: suitable

impurezas

endotoxin, tested

Nº de acceso UniProt

temp. de almacenamiento

−20°C

Información sobre el gen

human ... FST(10468)

Descripción general

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.

Aplicación

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).

Acciones bioquímicas o fisiológicas

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.

Forma física

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

Nota de análisis

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

Pictogramas

Corrosion

Palabra de señalización

Danger

Frases de peligro

Consejos de prudencia

Clasificaciones de peligro

Eye Dam. 1 - Skin Irrit. 2

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Visite la Librería de documentos

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
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
Rita Linko et al.
BMC infectious diseases, 14, 253-253 (2014-06-03)
Activin A and its binding protein follistatin (FS) are increased in inflammatory disorders and sepsis. Overexpression of activin A in the lung causes similar histopathological changes as acute respiratory distress syndrome (ARDS). ARDS and severe respiratory failure are complications of
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

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