<p><a href="/goto?url=http://www.acrobiosystems.com/" target="_blank"><strong>A</strong></a><a href="/goto?url=http://www.acrobiosystems.com/" target="_blank"><strong>CRO</strong></a><a href="/goto?url=http://www.acrobiosystems.com/" target="_blank">Biosystems </a></p><p><strong>Recombinant Human TGF-Beta 2 Protein </strong></p><p><strong>Cat. # </strong><a href="/goto?url=http://www.acrobiosystems.com/P171-Human-TGF-beta2-Protein.html" target="_blank"><strong>TG2-H4213 </strong></a></p><p><strong>For Research and Further Cell Culture Manufacturing Use </strong></p><p><strong>Bioactivity: </strong><br><strong>Source: </strong></p><p>The bio-activity was determined by its ability to inhibit IL-4 induced HT-2 cell proliferation. <strong>ED</strong><sub style="top: 0.2025em;"><strong>50</strong></sub><strong>&lt;0.1 </strong></p><p><strong>ng/ml</strong>, corresponding to a specific activity of <strong>&gt;1X10</strong><sub style="top: 0.2em;"><strong>7 </strong></sub><strong>Unit/mg </strong></p><p>Recombinant Human TGF Beta 2 Protein (rhTGFB2) Ala 303 - Ser 414 (Accession # <strong>NP_003229.1</strong>) was produced in human HEK293&nbsp;cells at ACRObiosystems. </p><p><strong>Molecular Characterization: </strong><br><strong>Formulation: </strong></p><p>rhTGFB2 contains no “tags” and has a calculated MW of 12.7 kDa (monomer). DTT-reduced protein migrates as a 13 kDa polypeptide and the non-reduced cystinelinked homodimer migrates as a 25 kDa protein. <br>Lyophilized from 0.22 μm filtered solution in TFA, acetonitrile. Normally Mannitol or Trehalose are added as protectants before lyophilization. </p><p>Contact us for customized product format or formulation. </p><p><strong>Endotoxin: </strong></p><p>Less than 1.0 EU per μg of the rhTGFB2 by the LAL method. </p><p><strong>Reconstitution: </strong></p><p>See Certificate of Analysis for details of reconstitution instruction and specific concentration. </p><p><strong>Purity: </strong><br><strong>Storage: </strong></p><p>&gt;98% as determined by SDS-PAGE of reduced (+) and non-reduced (-) rhTGFB2. </p><p><strong>Avoid repeated freeze-thaw cycles. </strong></p><p>No activity loss was observed after storage at: </p><p><strong>SDS-PAGE: </strong></p><p>••</p><p>4-8℃ for 1 year in lyophilized state 4-8℃ for 1 month under sterile conditions after reconstitution </p><p><em>The purity of rhTGFB2 was determined by SDS- PAGE of &nbsp; reduced (+) and non-reduced (-) rhTGFB2 and staining overnight with Coomassie Blue. </em></p><p>•</p><p>-20 ℃ to -70&nbsp;℃ for 3 months under sterile conditions after reconstitution </p><p><strong>Background: </strong></p><p>Transforming growth factor beta 2 ( TGFB2) is also known as TGF-β2, TGF-beta2, Glioblastoma-derived T-cell suppressor factor, G-TSF, BSC-1 cell growth inhibitor, Polyergin, Cetermin, and is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is a secreted protein known as a cytokine that performs many cellular functions and has a vital role during embryonic development. Mature human TGF-β2 shows 100% aa identity with porcine, canine, equine and bovine TGF-β2, and 97% aa identity with mouse and rat TGF-β2. It demonstrates crossspecies activity [1]. It is an extracellular glycosylated protein. It is known to suppress the effects of interleukin dependent T-cell tumors. The increased levels of TGF beta 2 triggered a neuronal cell death pathway related to Alzheimer's disease (AD) by binding to the extracellular domain of amyloid beta precursor protein (APP). The upregulation of the TGF beta 2 level is a common pathological feature of AD brains and suggests that it may be closely linked to the development of neuronal death related to AD. TGF-beta regulates key mechanisms of tumor development, namely immunosuppression, metastasis, angiogenesis, and proliferation. TGF beta 2 suppression is a promising therapeutic approach for malignant tumor therapy.[2-3] Please contact us via <a href="mailto:[email protected]" target="_blank"><strong>[email protected]</strong></a><strong>, </strong>if you have any question on this product. </p><p><strong>References: </strong></p><p>(1) Sporn, M.B., 2006, Cytokine Growth Factor Rev. 17:3-7. (2) Noguchi A. et al., 2010, Int J Neurosci. 120(3): 168-75. (3) Schlingensiepen KH. et al., 2006, Cytokine Growth Factor Rev. 17(1-2): 129-39. </p><p><a href="/goto?url=http://www.acrobiosystems.com/" target="_blank"><strong>http://www.acrobiosystems.com </strong></a></p>