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TB-500(Thymosin Beta 4)2mg
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TB-500(Thymosin Beta 4)2mg

Item 12662



What is TB500?

TB-500 is a synthetic version of the naturally occurring peptide present in virtually all human and animal cells, Thymosin Beta 4 (TB500). It is a first-in-class drug candidate that promotes the following*:

  • Endothelial (blood vessels) cell differentiation
  • Angiogenesis (growth of new blood cells from pre-existing vessels) in dermal tissues
  • Keratinocyte migration
  • Collagen deposition; and
  • Decreases inflammation.

One of TB500 key mechanisms of action is its ability to regulate the cell-building protein, Actin, a vital component of cell structure and movement. Of the thousands of proteins present in cells, actin represents up to 10% of the total proteins which therefore plays a major role in the genetic makeup of the cell.

This potent peptide is a member of a ubiquitous family of 16 related molecules with a high conservation of sequence and localization in most tissues and circulating cells in the body. TB500 not only binds to actin, but also blocks actin polymerization and is the actin-sequestering molecule in eukaryotic cells.

TB500 was identified as a gene that was up-regulated four-to-six fold during early blood vessel formation and found to promote the growth of new blood cells from the existing vessels. This peptide is present in wound fluid and when administered subcutaneously, it promotes wound healing, muscle building and speeds up recovery time of muscles fibres and their cells.

An additional key factor of TB500 is that it promotes cell migration through a specific interaction with actin in the cell cytoskeleton. It has been demonstrated that a central small amino acid long-actin binding domain has both blood cell reproduction and wound healing characteristics. These characteristics are uncovered by accelerating the migration of endothelial cells and keratinocytes. It also increases the production of extracellular matrix-degrading enzymes.

Research confirms that TB500 is a potent, naturally occurring wound repair factor with anti-inflammatory properties. TB500 is different from other repair factors, such as growth factors, in that it promotes endothelial and keratinocyte migration. It also does not bind to the extracellular matrix and has a very low molecular weight meaning it can travel relatively long distances through tissues.
 

 

TB-500 offers many benefits to the equine world in performance racing. Recent trials by some of the world’s leading trainers on their prize winning equine members of both genders, have been credited by a huge boost in their race-day results, something long desired in the racing world.

These trials along with clinical trials have indicated the following benefits associated with the use of TB-500 on mares and stallions*:

  • Increased muscle growth with huge increases in endurance and strength noted
  • Relaxed muscle spasm
  • Improved muscle tone
  • Increases the exchange of substance between cells
  • Encourages tissue repair
  • Stretches connective tissue
  • Helps maintain flexibility
  • Reduces inflammation of tissue in joint
  • Enhances nutritional components in the animal
  • Prevents the formation of adhesions and fibrous bands in muscles, tendons and ligaments.

When these proven benefits are viewed in conjunction with the fact that 60% of a horse’s body weight is muscle, it is clear to see the full potential of TB500can be reveled in by majority of the horse’s body.

FAQ

 

  1. Can TB-500 be used in conjunction with other supplements or anti-biotics?
    As TB-500 is a synthetic version of the naturally occurring peptide found in all animal cells, it does not pose as a foreign substance to the body. This means the product can be safely used in conjunction with any supplement or anti-biotic and not compromise the effect of these substances.
     
  2. What are the side effects of using TB-500?
    Post clinical safety trials and trials with some of the world’s most renowned equine trainers, there have been no noted side effects with the use of TB-500. It is not an oil-based solution and therefore poses no threat to the exterior complexion of the animal. One side effect which can be taken as being adverse at times is the increase in energy levels experienced by the animal. While in training and on the race track this poses a huge benefit, in recovery spells and transport between stables this can become a problem.
     
  3. How often can TB-500 be administered?
    Horses - Use one 10mg vial every week for a 6 week period
    Greyhound - Use half of one 10mg vial every week for 6 weeks
     
  4. Do I have to keep TB-500 refrigerated?
    TB-500 does not require refrigeration. It is to be stored at room temperature in a non humid environment. However, for greyhound usage where only half a vial (1ml) is used at a time, it is advised the vial be refrigerated and used within an 8 day period. 
     
  5. Does TB-500 contain any illegal or banned substances?
    TB-500 is 100% drug free and chemical free. As a result, TB-500 DOES NOT SWAB.
     
  6. What is the purity of TB500
    TB500 is 95% pure and ranks as one of the highest purity sources of Thymosin Beta 4 available in the world.
     

Beta thymosins

 

NMR structure of a β-thymosin. Both thymosin α1 [1] and β-thymosins are intrinsically unstructured proteins, i.e. they lack a stable fold when free in aqueous solution. This structure, mostly alpha helix, was artificially stabilised by an organic solvent.[2] The thymosin illustrated, originally named β9 is the cow orthologue of human β10

Beta thymosins are a family of proteins which have in common a sequence of about 40 amino acids similar to the small protein thymosin β4. They are found almost exclusively in multicellular animals. Thymosin β4 was originally obtained from the thymus in company with several other small proteins which although named collectively "thymosins" are now known to be structurally and genetically unrelated and present in many different animal tissues.

Monomeric β-thymosins, i.e. those of molecular weight similar to those originally isolated from thymus by Goldstein, are found almost exclusively in cells of multicellular animals.[4] The single known exception is in a choanoflagellate, significantly a single-celled organism regarded as the closest living relative of animals. [5] Although found in very early diverged animals such as sponges, monomeric thymosins are absent from arthropods and nematodes, which do nevertheless possess proteins, known as β-thymosin repeat proteins, which are constructed from several end-to-end repeats of β-thymosin sequences.[6] Genomics has shown that tetrapods (land vertebrates) each express three monomeric β-thymosins, which are the animal species' equivalents (orthologues) of human β4, β10 and β15 thymosins, respectively. The human thymosins are encoded by the genes TMSB4X, TMSB10 and TMSB15A and TMSB15B. (In humans, the proteins encoded by the two TMSB15 genes are identical.) Bony fish in general express orthologues of these same three, plus an additional copy of the β4 orthologue.[7]

Relation to the WH2 sequence module

The N-terminal half of β-thymosins bears a strong similarity in amino acid sequence to a very widely distributed sequence module, the WH2 module. (Wasp Homology Domain 2 - the name is derived from Wiskott-Aldrich syndrome protein).[8][9] Evidence from X-ray crystallography shows that this part of β-thymosins binds to actin in a near-identical manner to that of WH2 modules, both adopting as they bind, a conformation which has been referred to as the β-thymosin/WH2 fold. β-thymosins may therefore have evolved by addition of novel C-terminal sequence to an ancestral WH2 module.[10] However, sequence similarity searches designed to identify present-day WH2 domains[11] fail to recognise β-thymosins, (and vice versa) and the sequence and functional similarities may result from convergent evolution.[12]

Biological activities of thymosin β4

The archetypical β-thymosin is β4 (product in humans of the TMSB4X gene), which is a major cellular constituent in many tissues. Its intracellular concentration may reach as high as 0.5 mM.[13] Following Thymosin α1, β4 was the second of the biologically active peptides from Thymosin Fraction 5 to be completely sequenced and synthesized.[14]

Actin binding

Thymosin β4 was initially perceived as a thymic hormone. However this changed when it was discovered that it forms a 1:1 complex with G (globular) actin, and is present at high concentration in a wide range of mammalian cell types.[15] When appropriate, G-actin monomers polymerize to form F (filamentous) actin which together with other proteins that bind to actin comprise cellular microfilaments. Formation by G-actin of the complex with β-thymosin (= "sequestration") opposes this.

Due to its profusion in the cytosol and its ability to bind G-actin but not F-actin, thymosin β4 is regarded as the principal actin-sequestering protein in many cell types. Thymosin β4 functions like a buffer for monomeric actin as represented in the following reaction:[16]

F-actin ↔ G-actin + Thymosin β4 ↔ G-actin/Thymosin β4

Release of G-actin monomers from thymosin β4 occurs as part of the mechanism that drives actin polymerization in the normal function of the cytoskeleton in cell morphology and cell motility.

The sequence lkktet, which starts at residue 17 of the 43-aminoacid sequence of thymosin beta-4, and is strongly conserved between all β-thymosins, together with a similar sequence in WH2 domains, is frequently referred to as "the actin-binding motif" of these proteins, although modelling based on X-ray crystallography has shown that essentially the entire length of the β-thymosin sequence interacts with actin in the actin-thymosin complex.[17]

"Moonlighting"

In addition to its intracellular role as the major actin-sequestering molecule in cells of many multicellular animals, thymosin β4 shows a remarkably diverse range of effects when present in the fluid surrounding animal tissue cells. Taken together, these effects suggest that thymosin has a general role in tissue regeneration. This has suggested a variety of possible therapeutic applications, and several have now been extended to animal models and human clinical trials.

It is considered unlikely that thymosin β4 exerts all these effects via intracellular sequestration of G-actin. This would require its uptake by cells, and moreover, in most cases the cells affected already have substantial intracellular concentrations.

The diverse activities related to tissue repair may depend on interactions with receptors quite distinct from actin and possessing extracellular ligand-binding domains. Such multi-tasking by, or "partner promiscuity" of, proteins has been referred to as protein moonlighting.[18] Proteins such as thymosins which lack stable folded structure in aqueous solution, are known as intrinsically unstructured proteins (IUPs). Because IUPs acquire specific folded structures only on binding to their partner proteins, they offer special possibilities for interaction with multiple partners.[19] A candidate extracellular receptor of high affinity for thymosin β4 is the β subunit of cell surface-located ATP synthase, which would allow extracellular thymosin to signal via a purinergic receptor.[20]

Some of the multiple activities of thymosin β4 unrelated to actin may be mediated by a tetrapeptide enzymically-cleaved from its N-terminus, N-acetyl-ser-asp-lys-pro, brand names Seraspenide or Goralatide, best known as an inhibitor of the proliferation of haematopoietic (blood-cell precursor) stem cells of bone marrow.

Tissue regeneration

Work with cell cultures and experiments with animals have shown that administration of thymosin β4 can promote migration of cells, formation of blood vessels, maturation of stem cells, survival of various cell types and lowering of the production of pro-inflammatory cytokines. These multiple properties have provided the impetus for a world-wide series of on-going clinical trials of potential effectiveness of thymosin β4 in promoting repair of wounds in skin, cornea and heart.[21]

Such tissue-regenerating properties of thymosin β4 may ultimately contribute to repair of human heart muscle damaged by heart disease and heart attack. In mice, administration of thymosin β4 has been shown to stimulate formation of new heart muscle cells from otherwise inactive precursor cells present in the outer lining of adult hearts,[22] to induce migration of these cells into heart muscle[23] and recruit new blood vessels within the muscle.[24]

Anti-inflammatory role for sulfoxide

In 1999 researchers in Glasgow University found that an oxidised derivative of thymosin β4 (the sulfoxide, in which an oxygen atom is added to the methionine near the N-terminus) exerted several potentially anti-inflammatory effects on neutrophil leucocytes. It promoted their dispersion from a focus, inhibited their response to a small peptide (F-Met-Leu-Phe) which attracts them to sites of bacterial infection and lowered their adhesion to endothelial cells. (Adhesion to endothelial cells of blood vessel walls is pre-requisite for these cells to leave the bloodstream and invade infected tissue). A possible anti-inflammatory role for the β4 sulfoxide was supported by the group's finding that it counteracted artificially-induced inflammation in mice.

The group had first identified the thymosin sulfoxide as an active factor in culture fluid of cells responding to treatment with a steroid hormone, suggesting that its formation might form part of the mechanism by which steroids exert anti-inflammatory effects. Extracellular thymosin β4 would be readily oxidised to the sulfoxide in vivo at sites of inflammation, by the respiratory burst.[25]

Terminal deoxynucleotidyl transferase

Thymosin β4 induces the activity of the enzyme terminal deoxynucleotidyl transferase in populations of thymocytes (thymus-derived lymphocytes). This suggests that the peptide may contribute to the maturation of these cells.[14]

Clinical applications

Thymosin β4 has been tested in multicenter trials sponsored jointly by RegeneRx Biopharmaceuticals Inc (Rockville, MD, USA) and Sigma Tau (Pomezia, Italy) in the United States and Europe in patients with bed sores, ulcers caused by venostasis, and [[Epidermolysis bullosa simplex] and was found to accelerate bed sore and stasis ulcer repair by one month. The epidermolysis bullosa trial is still enrolling. It has also been tested in patients with chronic neurotrophic corneal epithelial defects and found to promote repair.

Levels of human thymosin β15 in urine have shown promise as a diagnostic marker for prostate cancer which is sensitive to potential aggressiveness of the tumour [26]

β-thymosin repeat proteins

Distribution

These proteins, which typically contain 2-4 repeats of the β-thymosin sequence, are found in all phyla of the animal kingdom, with the probable exception of sponges[27] The sole mammalian example, a dimer in mouse, is synthesised by transcriptional read-through between two copies of the mouse β15 gene, each of which is also transcribed separately.[28] A uniquely multiple example is the protein thypedin of Hydra which has 27 repeats of a β-thymosin sequence.[29]

Biological activities

β-thymosin repeat proteins resemble the monomeric forms in being able to bind to actin, but sequence differences in one example studied, a three-repeat protein Ciboulot of the fruit fly Drosophila, allow binding to ends of actin filaments, an activity which differs from monomer sequestration.[30]

These proteins became of interest in neurobiology with the finding that in the nudibranch (sea slug) Hermissenda crassicornis, the protein Csp24 (conditioned stimulus pathway phosphoprotein-24), with 4 repeats, is involved in simple forms of learning: both one-trial enhancement of the excitability of sensory neurons in the conditioned stimulus pathway, [31], and in multi-trial Pavlovian conditioning [32].

References

1.       ^ Grottesi A, Sette M, Palamara T, Rotilio G, Garaci E, Paci M (1998). "The conformation of peptide thymosin alpha 1 in solution and in a membrane-like environment by circular dichroism and NMR spectroscopy. A possible model for its interaction with the lymphocyte membrane". Peptides 19 (10): 1731–8. doi:10.1016/S0196-9781(98)00132-6. PMID 9880079.

2.       ^ a b PDB 1HJ0; Stoll R, Voelter W, Holak TA (May 1997). "Conformation of thymosin beta 9 in water/fluoroalcohol solution determined by NMR spectroscopy". Biopolymers 41 (6): 623–34. doi:10.1002/(SICI)1097-0282(199705)41:6<623::AID-BIP3>3.0.CO;2-S. PMID 9108730. "The thymosin is β9, bovine orthologue of human β10. Stabilised by organic solvent, the structure was determined by NMR. (Free β-thymosins lack a stable fold in solution)"

3.       ^ Stoll R, Voelter W, Holak TA (May 1997). "Conformation of thymosin beta 9 in water/fluoroalcohol solution determined by NMR spectroscopy". Biopolymers 41 (6): 623–34. doi:10.1002/(SICI)1097-0282(199705)41:6<623::AID-BIP3>3.0.CO;2-S. PMID 9108730.

4.       ^ "Family: Thymosin (PF01290)". Pfam. Wellcome Trust Sanger Institute.

5.       ^ "XYM2758.rev XYM Monosiga brevicollis rapidly growi... - EST result".

6.       ^ Manuel M, Kruse M, Müller WE, Le Parco Y (October 2000). "The comparison of beta-thymosin homologues among metazoa supports an arthropod-nematode clade". J. Mol. Evol. 51 (4): 378–81. doi:10.1007/s002390010100. PMID 11040289.

7.       ^ Edwards J (March 2010). "Vertebrate beta-thymosins: conserved synteny reveals the relationship between those of bony fish and of land vertebrates". FEBS Lett. 584 (5): 1047–53. doi:10.1016/j.febslet.2010.02.004. PMID 20138884.

8.       ^ Paunola E, Mattila PK, Lappalainen P (February 2002). "WH2 domain: a small, versatile adapter for actin monomers". FEBS Lett. 513 (1): 92–7. doi:10.1016/S0014-5793(01)03242-2. PMID 11911886.

9.       ^ "Family: WH2 (PF02205)". Pfam. Wellcome Trust Sanger Institute.

10.   ^ Dominguez R (September 2007). "The beta-thymosin/WH2 fold: multifunctionality and structure". Ann. N. Y. Acad. Sci. 1112: 86–94. doi:10.1196/annals.1415.011. PMID 17468236.

11.   ^ "Family: WH2 (PF02205)". Pfam. Wellcome Trust Sanger Institute.

12.   ^ Edwards J (August 2004). "Are beta-thymosins WH2 domains?". FEBS Lett. 573 (1–3): 231–2; author reply 233. doi:10.1016/j.febslet.2004.07.038. PMID 15328003.

13.   ^ Hannappel E (September 2007). "beta-Thymosins". Ann. N. Y. Acad. Sci. 1112: 21–37. doi:10.1196/annals.1415.018. PMID 17468232.

14.   ^ a b Low TL, Hu SK, Goldstein AL (February 1981). "Complete amino acid sequence of bovine thymosin beta 4: a thymic hormone that induces terminal deoxynucleotidyl transferase activity in thymocyte populations". Proc. Natl. Acad. Sci. U.S.A. 78 (2): 1162–6. doi:10.1073/pnas.78.2.1162. PMC 319967. PMID 6940133.

15.   ^ Safer D, Elzinga M, Nachmias VT (March 1991). "Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable". J. Biol. Chem. 266 (7): 4029–32. PMID 1999398.

16.   ^ Lodish, Harvey F. (2000). "Chapter 18. Cell Motility and Shape I: Microfilaments. 18.2. The Dynamics of Actin Assembly". Molecular cell biology. San Francisco: W.H. Freeman. ISBN 0-7167-3706-X.

17.   ^ Xue B, Aguda AH, Robinson RC (September 2007). "Models of the actin-bound forms of the beta-thymosins". Ann. N. Y. Acad. Sci. 1112: 56–66. doi:10.1196/annals.1415.010. PMID 17468228.

18.   ^ Jeffery CJ (January 1999). "Moonlighting proteins". Trends Biochem. Sci. 24 (1): 8–11. doi:10.1016/S0968-0004(98)01335-8. PMID 10087914.

19.   ^ Tompa P, Szász C, Buday L (September 2005). "Structural disorder throws new light on moonlighting". Trends Biochem. Sci. 30 (9): 484–9. doi:10.1016/j.tibs.2005.07.008. PMID 16054818.

20.   ^ Freeman KW, Bowman BR, Zetter BR (November 2010). "Regenerative protein thymosin {beta}-4 is a novel regulator of purinergic signaling". FASEB J. doi:10.1096/fj.10-169417. PMID 21106936.

21.   ^ Philp D, Kleinman HK (April 2010). "Animal studies with thymosin beta, a multifunctional tissue repair and regeneration peptide". Ann. N. Y. Acad. Sci. 1194: 81–6. doi:10.1111/j.1749-6632.2010.05479.x. PMID 20536453.

22.   ^ Smart N, Bollini D, Dubé KN, Vieira JM, Zhou B, Davidson S, Yellon D, Riegler J, Price AN, Lythgoe MF, Pu WT, Riley PR (June 2011). "De novo cardiomyocytes from within the activated adult heart after injury". Nature 474 (7353). doi:10.1038/nature10188. PMID 21654746. Lay summary – BBC News.

23.   ^ Smart N, Riley PR (February 2009). "Derivation of epicardium-derived progenitor cells (EPDCs) from adult epicardium". Curr Protoc Stem Cell Biol Chapter 2: Unit2C.2. doi:10.1002/9780470151808.sc02c02s8. PMID 19235142.

24.   ^ Riley PR, Smart N (December 2009). "Thymosin beta4 induces epicardium-derived neovascularization in the adult heart". Biochem. Soc. Trans. 37 (Pt 6): 1218–20. doi:10.1042/BST0371218. PMID 19909250.

25.   ^ Young JD, Lawrence AJ, MacLean AG, et al. (December 1999). "Thymosin beta 4 sulfoxide is an anti-inflammatory agent generated by monocytes in the presence of glucocorticoids". Nat. Med. 5 (12): 1424–7. doi:10.1038/71002. PMID 10581087..

26.   ^ Hutchinson LM, Chang EL, Becker CM, et al. (July 2005). "Use of thymosin beta15 as a urinary biomarker in human prostate cancer". Prostate 64 (2): 116–27. doi:10.1002/pros.20202. PMID 15666387.

27.   ^ Pekka Lappalainen (2007). Actin-Monomer-Binding Proteins. Boston, MA: Landes Bioscience and Springer Science+Business Media, LLC. ISBN 0-387-46407-7.

28.   ^ Dhaese S, Vandepoele K, Waterschoot D, Vanloo B, Vandekerckhove J, Ampe C, Van Troys M (April 2009). "The mouse thymosin beta15 gene family displays unique complexity and encodes a functional thymosin repeat". J. Mol. Biol. 387 (4): 809–25. doi:10.1016/j.jmb.2009.02.026. PMID 19233202.

29.   ^ Herrmann D, Hatta M, Hoffmeister-Ullerich SA (November 2005). "Thypedin, the multi copy precursor for the hydra peptide pedin, is a beta-thymosin repeat-like domain containing protein". Mech. Dev. 122 (11): 1183–93. doi:10.1016/j.mod.2005.07.003. PMID 16169708.

30.   ^ Carlier MF, Hertzog M, Didry D, Renault L, Cantrelle FX, van Heijenoort C, Knossow M, Guittet E (September 2007). "Structure, function, and evolution of the beta-thymosin/WH2 (WASP-Homology2) actin-binding module". Ann. N. Y. Acad. Sci. 1112: 67–75. doi:10.1196/annals.1415.037. PMID 17947587.

31.   ^ Redell JB, Xue-Bian JJ, Bubb MR, Crow T (August 2007). "One-trial in vitro conditioning regulates an association between the beta-thymosin repeat protein Csp24 and actin". Neuroscience 148 (2): 413–20. doi:10.1016/j.neuroscience.2007.06.023. PMID 17681698.

32.   ^ "Proteomic Analysis of Post-Translational Modifications in Conditioned Hermissenda". Retrieved 6 November 2011.

 



Drug makes hearts repair themselves

Man having heart attack

More people are surviving heart attacks, but that means more are living with heart failure

A drug that makes hearts repair themselves has been used in research on mice.

The damage caused by a heart attack had previously been considered permanent.

But a study in the journal Nature showed the drug, thymosin beta 4, if used in advance of a heart attack, was able to "prime" the heart for repair.

The British Heart Foundation described repair as the "holy grail of heart research", but said any treatment in humans was years away.

Due to advances in health care the number of people dying from coronary heart disease is falling.

But those living with heart failure are on the rise - more than 750,000 people have the condition in the UK alone.

Wake up

The researchers at University College London looked at a group of cells which are able to transform into different types of heart tissue in an embryo.

UK Heart statistics

Deaths from coronary heart disease

  • 1961 - 165,216
  • 2001 - 117,743
  • 2009 - 80,223

Estimated people living with heart failure

  • 1961 - 100,000
  • 1971 - 300,000
  • 2010 - 750,000

Source: British Heart Foundation

In adults epicardium-derived progenitor cells line the heart, but have become dormant.

Scientists used a chemical, thymosin beta 4, to "wake them up".

Professor Paul Riley, from the University College London, said: "The adult epicardial cells which line the muscle of the heart can be activated, move inward and give rise to new heart muscle."

"We saw an improvement in the ejection fraction, in the ability of the heart to pump out blood, of 25%."

As well as pumping more blood, the scar tissue was reduced and the walls of the heart became thicker.

Peter Weissberg, medical director of the British Heart Foundation, said he was "very excited" about the research but warned the scale of improvement seen in animals was rarely seen in humans.

Heart

Epicardium derived progenitor cells (in red) lining the heart

However, he argued that even a small improvement would have a dramatic impact on people's quality of life.

"A normal heart has lots of spare capacity. In patients with heart failure it is working flat out just to sit down [and] it's like running a marathon," he said.

"You could turn a patient from somebody who's gasping while sitting in a chair to somebody who can sit comfortably in a chair."

Advance therapy

The mice needed to take the drug in advance of a heart attack in order for it to be effective. As the researchers put it, "the priming effect is key".

If a similar drug could be found to be effective in humans, then the researchers believe it would need to be prescribed in a similar way to statins.

Professor Riley said "I could envisage a patient known to be at risk of a heart attack - either because of family history or warning signs spotted by their GP - taking an oral tablet, which would prime their heart so that if they had a heart attack the damage could be repaired."


http://scholar.google.com/scholar?hl=en&q=Thymosin+Beta-4+tumor&as_sdt=1%2C21&as_ylo=2008&as_vis=0

http://medivetdirect.com/documents/brouchure/TB500broucure.pdf

http://medivetdirect.com/documents/productinserts/tb500-productinsert.pdf

http://medivetdirect.com/documents/research/TB500_research.pdf


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