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mouse Thrombopoietin Recombinant

TPO

accession:  P40226
   Size A     2ug   $ 70
   Size B      10ug  $160
   Size C      1mg  $ 3900
Domain  :  four helix cytokine core
Gene  :  THPO
Catalog no. :  RKP40226
Source:
Optimized DNA sequence encoding mouse TPO erythropoeitin like domain  was expressed in Escherichia Coli.

 
Molecular weight:

Native mouse TPO, generated by the proteolytic removal of the signal peptide
and propeptide, The molecule has a calculated molecular mass of approximately 19 kDa. 

Recombinant mouse TPO is a disulfide-linked monomer protein consisting of 175 amino acid residue subunits, and migrates as an approximately 19 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE.


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

 
Biological Activity:
The ED(50) was determined by the dose-dependent proliferation of human MO7e cells  was found to be less than 1.0 ng/ml.

 
Protein Sequence:
        10         20         30         40         50         60 
MELTDLLLAA MLLAVARLTL SSPVAPACDP RLLNKLLRDS HLLHSRLSQC PDVDPLSIPV 

        70         80         90        100        110        120 
LLPAVDFSLG EWKTQTEQSK AQDILGAVSL LLEGVMAARG QLEPSCLSSL LGQLSGQVRL 

       130        140        150        160        170        180 
LLGALQGLLG TQLPLQGRTT AHKDPNALFL SLQQLLRGKV RFLLLVEGPT LCVRRTLPTT 

       190        200        210        220        230        240 
AVPSSTSQLL TLNKFPNRTS GLLETNFSVT ARTAGPGLLS RLQGFRVKIT PGQLNQTSRS 

       250        260        270        280        290        300 
PVQISGYLNR THGPVNGTHG LFAGTSLQTL EASDISPGAF NKGSLAFNLQ GGLPPSPSLA 

       310        320        330        340        350 
PDGHTPFPPS PALPTTHGSP PQLHPLFPDP STTMPNSTAP HPVTMYPHPR NLSQET 
(*)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 mouse TPO was lyophilized from a 0.2 μm filtered PBS solution.

 
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.

 

 

Thrombopoietin

TPO, known also as TSF (thrombopoiesis stimulating factor), for mediator substances that function as natural stimulators of megakaryocytopoiesis and thus, promote the differentiation of platelets. TPO stimulates an increase in the sizes and numbers of megakaryocytes. It also increases the number of small acetyl-cholinesterase positive cells that are early precursor cells of the megakaryocytic lineage. TPO is a protein of 332 amino acids that shows significant homology with Epo (erythropoietin) in its N-terminal domain. A comparison of human and porcine TPO sequences shows 83 % identity between the erythropoietin-like domains but only 67 % between the C- terminal domains.

Related Publications:
effect of the non-peptide Thrombopoietin receptor agonist eltrombopag on bone marrow cells from patients with acute myeloid leukemia and myelodysplastic syndrome
Blood, Aug 2009; 10.1182/blood-2009-04-219493.
association of hereditary thrombocythemia and distal limb defects with a Thrombopoietin gene mutation
Blood, Aug 2009; 114: 1655 - 1657.
Thrombopoietin controls proliferation of embryonic multipotent hematopoietic progenitors
Genes Cells, Jul 2009; 14: 851 - 860.
second generation Thrombopoietin agents for treatment of chronic idiopathic thrombocytopenic purpura in adults
Journal of Oncology Pharmacy Practice, Jun 2009; 10.1177/1078155209337668.
ligand-independent Thrombopoietin mutant receptor requires cell surface localization for endogenous activity
J. Biol. Chem., May 2009; 284: 11781 - 11791.




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