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Follistatin 315 (CT) (FSTL1, FS315)

Cat no: F9090-02A


Supplier: United States Biological
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Follistatin (FST) is a single-chain glycosylated protein of gonadal origin, originally identified as an antagonist of activin and suppressor of follicle stimulating hormone (FSH) synthesis/secretion. Alternative splicing of FST mRNA generates the two isoforms FS315 and FS288, the latter of which is the main cell-surface form and binds with high affinity to surface heparan sulphate proteoglycans, whilst FS315 binds with only low-affinity, and is considered to be the main circulating form of follistatin. As well as activin, FST interacts with other growth factors such as bone morphogenetic proteins (BMPs) -2, -4 and -7, myostatin, and growth differentiation factor 9 (GDF-9), playing a key role in cellular differentiation/proliferation, embryonic development and tissue repair. Applications: Suitable for use in ELISA, Western Blot, and Immunohistochemistry (paraffin). Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Positive Control: Testis Storage and Stability: May be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: F9090-02A
Reactivities: Human
Hosts: Mouse
Applications: ELISA, Immunohistochemistry, Western Blot
Size: 100ug
Form: Supplied as a liquid in PBS, 0.09% sodium azide.
P type: Mab
Isotype: IgG2a
Purity: Purified by Protein G affinity chromatography.
References: 1. McPherson, S.J. et al. (1999) Expression of activin A and follistatin core proteins by human prostate tumor cell lines. Endocrinology. 140: 5303-5309.
Additional info: Recognizes an epitope within the C-terminal region of human follistatin 315 (FS315). Does not cross-react with FS288.

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