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F2177

Sigma-Aldrich

Follistatin 288 from mouse

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

Sinónimos:

FS-288

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About This Item

MDL number:
MFCD03456879
UNSPSC Code:
51111800
NACRES:
NA.32
En este momento no podemos mostrarle ni los precios ni la disponibilidad

biological source

mouse

Quality Level

100

recombinant

expressed in baculovirus infected Sf21 cells

assay

>95% (SDS-PAGE)

form

lyophilized powder

potency

0.04-0.4 mg per mL

mol wt

calculated mol wt ~31 kDa

packaging

pkg of 25 μg

storage condition

avoid repeated freeze/thaw cycles

impurities

endotoxin, tested

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Este artículo
44864E6627L2376
cis-5,8,11,14,17-Eicosapentaenoic acid ≥99%

E2011

cis-5,8,11,14,17-Eicosapentaenoic acid

cis-5,8,11,14,17-Eicosapentaenoic acid analytical standard

44864

cis-5,8,11,14,17-Eicosapentaenoic acid

cis-5,8,11,14,17-Eicosapentaenoic acid sodium salt ≥99% (capillary GC)

E6627

cis-5,8,11,14,17-Eicosapentaenoic acid sodium salt

Linolenic acid ≥99%

L2376

Linolenic acid

form

liquid

form

-

form

film or powder

form

-

Quality Level

200

Quality Level

100

Quality Level

200

Quality Level

200

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

solubility

methanol: 50 mg/mL, clear, colorless

solubility

-

solubility

methanol: 50 mg/mL, clear to slightly hazy, colorless to faintly yellow

solubility

-

biological source

fish oil

biological source

fish oil

biological source

synthetic (organic)

biological source

-

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.[1][2][3]

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.[1] 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.[3]
High affinity activin-binding protein that can act as an activin antagonist.

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.

Analysis Note

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

pictograms

Corrosion
GHS05

signalword

Danger

hcodes

H315,H318

Hazard Classifications

Eye Dam. 1 - Skin Irrit. 2

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

  • Hoja de especificación

    • Elija entre una de las versiones más recientes:

    Certificados de análisis (COA)

    Lot/Batch Number
    MKCN4706
    MKBZ1581V
    070M2035
    116K1393
    123K0811

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    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
    S Dasgupta et al.
    Journal of postgraduate medicine, 58(3), 190-193 (2012-10-02)
    Out of a panel of 37 candidate genes tested for linkage with polycystic ovary syndrome (PCOS), the strongest evidence of linkage was reported in the follistatin (FST) gene region. Subsequently, a couple of studies outside India investigated the FST gene

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