Follistatin was detected in immersion fixed paraffin-embedded sections of human pituitary using Human Follistatin Monoclonal Antibody (Catalog # MAB669) at 25 µg/mL overnight at 4 °C. Tissue was stained using the ...read more
S. frugiperda insect ovarian cell line Sf 21-derived recombinant human Follistatin Gly30-Asp329 Accession # P19883
Specificity
Detects human Follistatin in direct ELISAs and Western blots. It recognizes the 288 aa, 300 aa, and 315 aa isoforms of human Follistatin. In direct ELISAs and Western blots, this antibody shows approximately 50% cross-reactivity with recombinant mouse Follistatin.
Source
N/A
Isotype
IgG2a
Clonality
Monoclonal
Host
Mouse
Gene
FST
Purity Statement
Protein A or G purified from ascites
Innovator's Reward
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Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Reconstitution Instructions
Reconstitute at 0.5 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Follistatin Antibody (85918) [Unconjugated]
follistatin isoform FST317
Follistatin
FS
FSActivin-binding protein
FST
Background
Follistatin
(FST) is a secreted glycoprotein that was first identified as a
follicle-stimulating hormone inhibiting substance in ovarian follicular
fluid (1, 2). Human Follistatin cDNA encodes a 344 amino acid (aa)
protein with a 29 aa signal sequence, an N-terminal atypical TGF binding
domain, three Follistatin domains that contain EGF-like and kazal-like
motifs, and a highly acidic C-terminal tail. The first Follistatin
domain (FS1) contains a heparin binding site, while FS1 and FS2 are most
critical for activin binding and neutralization (3, 4). In addition to
activin, Follistatin regulates bioavailability of many non-TGF-beta members
of the TGF-beta superfamily, such as BMP6, BMP7 and myostatin (5). It also
regulates hematopoietic stem cell adhesion to fibronectin via FS2, and
binds angiogenin via FS2 and FS3 (6, 7). Some Follistatin binding
partners will also bind Follistatin-like proteins such as FSL-3
(3, 5, 6). Of three Follistatin isoforms, the full-length mature
Follistatin (FST315) is the most abundant and the sole form in plasma,
but has lower binding affinity for both activins and heparins than
alternative isoforms (5, 8, 9). The acidic tail is missing in the splice
variant FST288 which shows the highest affinity for activins, while
a partial tail exists in the proteolytically produced FST303, which
shows intermediate activin affinity (5, 8, 9). FST315 shares 98% aa
identity with mouse, rat, equine and ovine FST, 99% with porcine and 97%
with bovine FST. Genetic deletion of Follistatin in mice, or expression
of only the FST288 form, is perinatally lethal due to defects of lung,
skin and musculoskeletal system (10). Expression of only the FST315
isoform allows survival, with defects in vascularization and female
fertility (10).
Shimasaki, S. et al. (1988) Proc. Natl. Acad. Sci. USA 85:4218.
Thompson, T.B. et al. (2005) Dev. Cell 9:535.
Sidis, Y. et al. (2005) Endocrinology 146:130.
Keutmann, H.T. et al. (2004) Mol. Endocrinol. 18:228.
Sidis, Y. et al. (2006) Endocrinology 147:3586.
Maguer-Satta, V. et al. (2006) Exp. Cell Res. 312:434.
Gao, X. et al. (2007) FEBS Lett. 581:5505.
Lerch, T.F. et al. (2007) J. Biol. Chem. 282:15930.
Schneyer, A.L. et al. (2004) J. Clin. Endocrinol. Metab. 89:5067.
Lin, S-Y. et al. (2008) Mol. Endocrinol. 22:415.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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