TGF beta 2/TGFB2 Protein, Rhesus Macaque (HEK293, C-His)

Transforming growth factor-beta 2 (TGF-β2), an extracellular glycosylated protein, is a member of the TGF-β superfamily. TGFβ2 controls key physiological processes including cell migration, proliferation and differentiation via signalling through type I and type II receptors (TGFβR1 and TGFβR2). TGF-β2 is an immune suppressor involved in the development of immune tolerance, and also regulates embryonic development^[1][2]. TGF beta 2/TGFB2 Protein, Rhesus Macaque (HEK293, His) is produced in HEK293 cells  with a C-Terminal His-tag. It and consists of 414 amino acids (M1-S414).

In mammals, three different isoforms of TGF-β are described (TGF-β1, TGF-β2 and TGF-β3; transforming growth factor beta) to regulate apoptosis, proliferation, differentiation, migration and invasion processes utilising overlapping but not redundant mechanisms. All three isoforms are expressed in the liver, but their expression is differentially distributed among liver cell types. TGF-β2 expression in different liver cell types and is also associated with developmental defects and fibrotic diseases in mice^[1][2][3].
The sequence of amino acids in TGF-β2 proteins from different species is very stable, which leads to the conclusion that in the process of evolution, TGF-β2 has been only slightly altered, and that both in humans and in animals, its function is similar.
TGFβ2 is a transforming growth factor beta (TGFB) family cytokine, with members of this cytokine family playing broad regulatory roles and controlling key physiological processes including cell migration, proliferation and differentiation via signalling through type I and type II receptors (TGFβR1 and TGFβR2), with signals propagating via the downstream regulatory SMAD proteins. This TGFβ/SMAD pathway is frequently dysregulated in human cancer. TGFβ cytokines are capable of suppressing T cell growth in response to IL‐2. The degree of TGFβ2 expression correlated with the expression of several different markers of immune cell subsets within tumours. In addition, TGF-β2 regulates embryonic development and, therefore not surprisingly, global Tgfb2 null mice exhibit a wide range of developmental defects and perinatal mortality^[1][2][3].
TGF-β2 is an immune suppressor involved in the development of immune tolerance, and recombinant TGF-β2 incubation is more potent than TGF-β1 or TGF-β3 in suppressing macrophage inflammatory responses. TGF-β2 is shown to correlate with bad prognosis in intrahepatic CCAs and hepatocellular carcinoma. Mechanistically, canonical Smad signalling as well as crosstalk with Yap, Hippo, Wnt and β-catenin signalling have been demonstrated in the liver and other organs^[1][2][3].

Recombinant human TGF-β2 (1.25, 2.5, 5, 1, and 2 ng/mL; for 24 h) increases extracellular matrix (ECM) protein synthesis and secretion in optic nerve head (ONH) astrocytes and lamina cribrosa (LC) cells. TGF-β2 induces phosphorylation of canonical signaling proteins Smad2/3 but does not alter phosphorylation of non-canonical signaling proteins ERK1/2, p38, and JNK1/2 proteins in ONH astrocytes and LC cells^[4].

Measured by its binding ability in a functional ELISA. Immobilized Rhesus Macaque TGFB2 at 5 μg/mL (100 μL/well) can bind biotinylated LRRC32, The ED₅₀ for this effect is 0.3462 μg/mL.

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  Measured by its binding ability in a functional ELISA. Immobilized Rhesus Macaque TGFB2 at 5 μg/mL (100 μL/well) can bind biotinylated LRRC32, The ED₅₀ for this effect is 0.3462 μg/mL.

Rhesus Macaque

HEK293

C-6*His

F6ZJW6/NP_001253447.1 (L21-S414)

707540

Full Length of Mature Protein

LSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVPEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYRLESQQTNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS

Approximately 13-16 kDa & 40-60 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

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  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.