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Human Follistatin Recombinant

FST

accession:  P19883
   Size A     10ug   $ 160
   Size B      50ug  $480
   Size C      1mg  $ 4700
Domain  :  Follistatin
Gene  : 
Catalog no. :  RKP19883

Source:
Optimized DNA sequence encoding Human Follistatin mature chain was expressed in Hek293 cells.

 
Molecular weight:

Native human Follistatin, generated by the proteolytic removal of the signal peptide and propeptide,the molecule has a calculated molecular mass of approximately 31 kDa.

Recombinant Follistatin is a disulfide-linked monomer protein consisting of 296 amino acid residue subunits,  due to glycosylation migrates as an approximately 45 kDa protein under non-reducing and reducing conditions in SDS-PAGE.


 
Purity:
>95%, as determined by SDS-PAGE and HPLC

 
Biological Activity:
The ED(50) was determined by the  ability to neutralize Activin A inhibitory effect of mouse MPC-11 cells and was determined to be  0.1-0.4 µg/ml in the presence of 7.5 ng/ml Activin A.

 
Protein Sequence:

(*)Complete precursor sequence shown, expressed chain highlighted 
 
Endotoxin:
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

 
Presentation:
Recombinant Human Follistatin was  lyophilized  at 1mg/ml containing no additives.

 
Reconstitution:
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.

 
Storage:
The lyophilized protein is stable for at least 2 years from date of receipt at -20° C.
Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity. 

Avoid repeated freeze/thaw cycles.

 
Usage:
This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.

follistatin



Related Publications:
structure of myostatin·follistatin-like 3: n-terminal domains of follistatin-type molecules exhibit alternate modes of binding
J. Biol. Chem., Jan 2012; 287: 1043 - 1053.
the type 1 insulin-like growth factor receptor (igf-ir) pathway is mandatory for the follistatin-induced skeletal muscle hypertrophy
Endocrinology, Jan 2012; 153: 241 - 253.
short-term energy deprivation alters activin a and follistatin but not inhibin b levels of lean healthy women in a leptin-independent manner
J. Clin. Endocrinol. Metab., Dec 2011; 96: 3750 - 3758.
the expression of activins, their type ii receptors and follistatin in human fallopian tube during the menstrual cycle and in pseudo-pregnancy
Hum. Reprod., Dec 2011; 26: 3346 - 3354.
energy deprivation alters in a leptin- and cortisol-independent manner circulating levels of activin a and follistatin but not myostatin in healthy males
J. Clin. Endocrinol. Metab., Nov 2011; 96: 3416 - 3423.




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