Anti-Follistatin Clone 17/2

Follistatin is a single-chain glycosylated protein that inhibits follicle stimulating hormone (FSH) release. Alternative splicing of Follistatin mRNA yields two isoforms, FS315 and FS288. FS288 is the main cell-surface form and binds to surface heparin sulphate proteoglycans. Clone 17/2 recognizes recombinant human Follistatin 288, allowing for detection of FSH levels using various analysis methods. This antibody also works in a two site ELISA with Clone 29/9.

Catalogue No. Target Research Areas Applications Size Price (£)
17/2-100UG Follistatin
(FS288)
Endocrinology
Cancer
Fertility
Immunology
Neurosciences
ELISA
WB
IHC
ICC
0.1mg 347.00

Form in stock: IgG, purified – 1.0 mg/mL. Also available as unpurified supernatant.
Host: Mouse
Specificity: Recognizes human Follistatin isoform FS288, raised against recombinant human FS288.
Human Histology positive control: Testis
Fusion partner: Spleen cells immunised from immunised Balb/c mice were fused with cells of the SP2/0 myeloma cell line.
Storage: Store at +4°C or -20°C. Avoid repeated freezing and thawing.
Shelf life: 18 months from date of dispatch.
Regulatory/ Restrictions: For research and commercial purposes.

Application Suggested Dilution
Western Blot 1 μg/mL 1
Immunohistochemistry – Paraffin 10 μg/mL 1
ELISA 1 μg/mL 3
Immunocytochemistry 70 μg/mL 2
  1. Stephen J. McPherson, Sally L. Mellor, Hong Wang, Lee W. Evans, Nigel P. Groome, Gail P. Risbridger; Expression of Activin A and Follistatin Core Proteins by Human Prostate Tumor Cell Lines. Endocrinology 1999; 140 (11): 5303-5309.
  2. Gregor Majdic, Allan S. McNeilly, Richard M. Sharpe, Lee R. Evans, Nigel P. Groome, Philippa T. K. Saunders; Testicular Expression of Inhibin and Activin Subunits and Follistatin in the Rat and Human Fetus and Neonate and During Postnatal Development in the Rat. Endocrinology1997; 138 (5): 2136-2147.
  3. LW Evans, S Muttukrishna, and NP Groome Development, validation and application of an ultra-sensitive two-site enzyme immunoassay for human follistatin J Endocrinol 156 (2) 275-282.
  4. Fitzgerald, A. M., Benz, C., Clark, A. F., & Wordinger, R. J. (2012). The Effects of Transforming Growth Factor-β2 on the Expression of Follistatin and Activin A in Normal and Glaucomatous Human Trabecular Meshwork Cells and Tissues. Investigative Ophthalmology & Visual Science53(11), 7358–7369. IHC, Dilution used 1:100
  5. Hands, J.R., Abel, P., Ashton, K. et al. Investigating the rapid diagnosis of gliomas from serum samples using infrared spectroscopy and cytokine and angiogenesis factors Anal Bioanal Chem (2013) 405: 7347. IHC-P, Dilution used 1:500
  6. Mabuchi, Y., Yamoto, M., Minami, S., Umesaki, N.”Immunohistochemical localization of inhibin and activin subunits, activin receptors, and Smads in ovarian clear cell adenocarcinoma”. Oncology Reports 15.2 (2006): 291-296. IHC-P, Dilution used 70 μg/mL

Clone 17/2 used to detect immunoreactivity with FS288 by IHC-P

Immunolocalization of FS315 and FS288 to PC3 and LNCaP cell lines. Positive immunoreactivity for FS315 localized to the cytoplasm of the epithelial tumor cell lines LNCaP (A) and PC3 (B) using H10 antibody, no immunoreactivity was present if the antibody was preabsorbed with FS315 peptide (inset Ainset B). Mouse IgG antibody controls were negative (inset Cinset D). (McPherson, S.J. et al. 1999)

Concentration used: 10 μg/mL
Dilution used: 1:50

Western Blots showing binding of 17/2 to isoforms of FS288

A. Protein bands corresponding to the approximate 31 and 35K molecular weight isoforms of FS were detected in PC3 media (lane 2) and lanes containing hrFS288 protein (lane 1). (McPherson, S.J. et al. 1999)

Concentration used: 1 μg/mL