Follistatin manufacturers
- FOLLISTATIN
-
- $155.00 / 1box
-
2024-06-04
- CAS:
- Min. Order: 1box
- Purity: 99.7%
- Supply Ability: 50000vials
- Follistatin
-
- $20.00/ Box
-
2024-05-29
- CAS:
- Min. Order: 1Box
- Purity: 99%
- Supply Ability: 1000 boxs
- Follistatin
-
- $100.00 / 10g
-
2024-05-27
- CAS:
- Min. Order: 1g
- Purity: 99.9%
- Supply Ability: 100kg
|
| Product Name: | Follistatin | | Synonyms: | FOLLISTATIN | | CAS: | | | MF: | | | MW: | 0 | | EINECS: | | | Product Categories: | | | Mol File: | Mol File | ![Follistatin Structure]() |
| | Follistatin Chemical Properties |
| | Follistatin Usage And Synthesis |
| Synthesis and release | FSH and forskolin stimulate follistatin synthesis in rat
granulosa cells. Follistatin synthesis in the rat anterior
pituitary is stimulated by activin via Smad proteins
and by the gonadotropin-releasing hormone (GnRH)
via cAMP signaling. Dexamethasone upregulates follistatin gene expression in osteoblasts. The peroxisome
proliferator-activated receptor (PPAR) γ downregulates
follistatin gene expression in intestinal epithelial cells. In the zebrafish, oocyte-derived bone morphogenetic
protein (BMP) stimulates follistatin production from
ovarian follicle cells. In the carp pituitary, activin stimulates follistatin production, but dopaminergic input from
the hypothalamus inhibits follistatin production. | | Biological functions | Follistatin 288 antagonizes the effects of activins in various cells and tissues by blocking the binding of activin to
their receptors. The exact functions of follistatin 315 and
follistatin-like 3 have not yet been clarified. Follistatin
also binds several members of the transforming growth
factor (TGF) β family, including myostatin and
several BMPs. Mice in which the follistatin gene was inactivated do
not survive long after birth due to a variety of skeletal
and cutaneous abnormalities. Overexpression of the follistatin gene resulted in the degeneration of seminiferous
tubules in male mice and defects in follicular development in female mice, when the mice show the highest
levels of follistatin expression. Granulosa cell-specific
inactivation of the follistatin gene results in reduced numbers of ovarian follicles and ovulation and elevated levels
of FSH in mice. Follistatin-like 3 knockout mice exhibited increased pancreatic islet size, enhanced circulating
insulin levels, and improved glucose tolerance. | | Clinical implications | Patients with septicemia show high serum concentrations of follistatin and activin. The exposure of bacterial
lipopolysaccharide induces an elevation in serum follistatin concentration in response to a rapid increase in the circulating activin A. Activin A promotes the release of
inflammatory cytokines such as TNF and IL-1, whereas
follistatin is able to suppress the release of these cytokines. Serum levels of follistatin increased in patients
with acute liver failure. | | Description | Follistatin is a single-chain glycoprotein structurally unrelated
to the inhibin and activin proteins. Follistatin binds activin
and neutralizes activin action. Follistatin was originally isolated from porcine and
bovine follicular fluid for its ability to suppress folliclestimulating hormone (FSH) secretion from the rat pituitary. Subsequently, it was discovered that follistatin
binds activin with high affinity. | | Physical properties | Mr 35,000 (follistatin 315), 32,000 (follistatin 288). pI
5.0–6.0 (follistatin 315), 8.0–9.0 (follistatin 288). Soluble
in water. | | Structure and conformation | There are three alternatively spliced products of the single follistatin gene: follistatin 288, follistatin 303, and follistatin 315. Follistatin 288 lacks the carboxyl-terminal Glurich acidic region of follistatin 315. Follistatin
303 is produced by the proteolysis of follistatin 315. Follistatins have two N-linked glycosylation sites, producing
different size variants. Follistatins 288 and 315 contain three
cysteine-rich follistatin domains of 73–77 aa residues and
have a similar binding affinity for activin. Both follistatins
have a biding site for heparin and heparan sulfate, a major
component of proteoglycans on the cell surface. Follistatin 288 shows high affinity for heparan
sulfate and is membrane-bound while follistatin 315 has
low affinity for cell-surface proteoglycans and is the predominant form in circulation. Additionally, follistatin-like
3 (follistatin-related protein, FSTL3) consists of two follistatin domains, but lacks the heparin binding site. Two follistatin molecules bind one activin molecule via the activin
β-subunits.
 |
| | Follistatin Preparation Products And Raw materials |
|