TGF beta 1/TGFB1 Protein, Human (112a.a, HEK293)

TGF beta 1/TGFB1 Protein is initially identified as a growth factor that induces the growth of rodent fibroblasts. TGF beta 1/TGFB1 Protein inhibits the cell cycle in the G1 phase. TGF beta 1/TGFB1 is an endogenous factor controlling apoptosis in normal and pathological tissues. TGF beta 1/TGFB1 Protein, Human (112a.a, HEK293) is a recombinant protein (A279-S390) produced by HEK293 cells^[1][2].

TGFβ is released from degranulating platelets and secreted by all of the major cell types participating in the repair process, including lymphocytes, macrophages, endothelial cells, smooth muscle cells, epithelial cells, and fibroblasts. Mammals express three isoforms of TGFβdesignated TGFβI, TGFβ2, and TGFβ3; TGFβ1 is the most abundant isoform in all tissues, and in human platelets it is the only isoform of the peptide. Certain cells such as retinal pigment epithelial cells secrete predominantly TGFβ2, and certain body fluids such as the aqueous and vitreous of the eye, amniotic fluid, saliva, and breast milk contain principally TGFβ2. TGFβ3 is the least studied of the TGFβ isoforms. It has been isolated from human umbilical cord and is secreted from certain cells, including myoblast celllines; however, it is usually less abundant than either TGFβ1 or TGFβ2 in both tissue and cell extracts^[1]. There are three fundamental directions of its activities: I. TGFβ1 regulates cell proliferation, growth, differentiation and cells movement. II. TGFβ1 has immunomodulatory effects. III. TGFβ1 has profibrogenic effects. TGFβ1 action can be local and systemic^[2].

Immobilized Human Mature TGF beta 1, No Tag at 0.5 μg/mL (100 μl/well) on the plate. Dose response curve for Human TGF-beta RII, mFc Tag with the EC₅₀ of <8 ng/mL determined by ELISA.

Human

HEK293

Tag Free

P01137 (A279-S390)

7040  [NCBI]

ALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS

14-15 kDa

Greater than 95% as determined by Tris-Bis PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of 50mM Glycine 150mM NaCl, pH 2.5. Normally 8% trehalose is added as protectant before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in 4mM HCl.

Stored at -20°C for 2 years. 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.

• [1]. K. Miyazono, et al. A role of the latent TGF-beta 1-binding protein in the assembly and secretion of TGF-beta 1. The EMBO Journal (1991)10:1091-1101.

  [2]. M Selvakumaran, et al. The novel primary response gene MyD118 and the proto-oncogenes myb, myc, and bcl-2 modulate transforming growth factor beta 1-induced apoptosis of myeloid leukemia cells. Mol Cell Biol. 1994 Apr;14(4):2352-60.  [Content Brief]

  [3]. Chambaz E.M., et al. Transforming Growth Factor-βs: A Multifunctional Cytokine Family. Implication in the Regulation of Adrenocortical Cell Endocrine Functions. 1991.

  [4]. Dulce Maroni, et al. TGFB1 disrupts the angiogenic potential of microvascular endothelial cells of the corpus luteum. Cell Sci. 2011 Jul 15;124(Pt 14):2501-10.  [Content Brief]

  [5]. Nan Wu, et al. LINC00941 promotes CRC metastasis through preventing SMAD4 protein degradation and activating the TGF-β/SMAD2/3 signaling pathway. Cell Death Differ. 2021 Jan;28(1):219-232.  [Content Brief]

  [6]. Hai Zhang, et al. Effects of transforming growth factor-beta 1 (TGF-beta1) on in vitro mineralization of human osteoblasts on implant materials. Biomaterials. 2003 May;24(12):2013-20.  [Content Brief]

  [7]. Paloma B Liton, et al. Cross-talk between TGF-beta1 and IL-6 in human trabecular meshwork cells. Mol Vis. 2009;15:326-34. Epub 2009 Feb 11.  [Content Brief]