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Download COA here: Follistatin344_1mg.pdf
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Follistatin 344
Follistatin 344 is the synthetic version of the naturally occouring Follistatin, also known as activin-bindings protein, is a protein that in humans is encoded by the FST gene.[1][2] Follistatin is an autocrineglycoprotein that is expressed in nearly all tissues of higher animals.[2]
Its primary function is the binding and bioneutralization of members of the TGF-β superfamily, with a particular focus on activin, a paracrinehormone.
An earlier name for the same protein was FSH-suppressing protein(FSP). At the time of its initial isolation from follicular fluid, it was found to inhibit the anterior pituitary‘s secretion of follicle-stimulating hormone(FSH).
Biochemistry
Follistatin is part of the inhibin-activin-follistatin axis.
Three isoforms, FS-288, FS-300, and FS-315 have been reported. Two, FS-288 and FS-315, are created by alternative splicing of the primary mRNA transcript. FS-300 (porcine follistatin) is thought to be the product of posttranslational modification via truncation of the C-terminal domain from the primary amino-acid chain.
Although FS is ubiquitous, its highest concentration is in the female ovary, followed by the skin.
Follistatin is produced by folliculostellate (FS) cells of the anterior pituitary. FS cells make numerous contacts with the classical endocrine cells of the anterior pituitary including gonadotrophs.
Function
In the tissues activin has a strong role in cellular proliferation, thereby making follistatin the safeguard against uncontrolled cellular proliferation and also allowing it to function as an instrument of cellular differentiation. These roles are vital in tissue rebuilding and repair, and may account for follistatin’s high presence in the skin.
In the blood, activin and follistatin are involved in the inflammatory response following tissue injury or pathogenic incursion. The source of follistatin in circulating blood plasma has yet to be determined, but due to its autocrine nature speculation suggests the endothelial cells lining all blood vessels, or the macrophages and monocytes circulating within the whole blood, may be sources.
Follistatin is involved in embryo development. It has inhibitory action on bone morphogenic proteins (BMPs); BMPs induce the ectoderm to become epidermal ectoderm. Inhibition of BMPs allows neuroectodermto arise from ectoderm, a process which eventually forms the neural plate. Other inhibitors involved in this process are nogginand chordin.
Follistatin and BMPs are play a role in folliculogenesis within the ovary. The main role of follistatin in the oestrus/menstrus ovary appears to be progression of the follicle from early antral to antral/dominant. It is also involved in the promotion of cellular differentiation of the estrogen producing granulosa cells (GC) of the dominant follicle into the progesterone producing large lutein cells (LLC) of the corpus luteum.
References
- Ueno N, Ling N, Ying SY, Esch F, Shimasaki S, Guillemin R (December 1987). “Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone”. Proceedings of the National Academy of Sciences of the United States of America. 84 (23): 8282–8286. Bibcode:1987PNAS…84.8282U. doi:10.1073/pnas.84.23.8282. PMC 299526. PMID 3120188.
- Tortoriello DV, Sidis Y, Holtzman DA, Holmes WE, Schneyer AL (August 2001). “Human follistatin-related protein: a structural homologue of follistatin with nuclear localization”. Endocrinology. 142 (8): 3426–3434. doi:10.1210/endo.142.8.8319. PMID 11459787.
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