TGF beta 1/TGFB1 LAP Protein, Human (Biotinylated, HEK293, His-Avi)

The latency-associated peptide (LAP) of the transforming growth factor β-1 (TGF-β-1) proprotein is an important precursor that forms a complex with TGF-β-1. LAP maintains the latent state of TGF-β-1 during storage in the extracellular matrix, ensuring controlled activation. Interactions with “environmental molecules” such as LTBP1, LRRC32/GARP, and LRRC33/NRROS intricately regulate TGF-β-1 activation. LRRC33/NRROS influences the activation of macrophages and microglia, while LRRC32/GARP controls the activation of activated regulatory T cells. Interactions with integrins induce conformational changes in LAP, releasing active TGF-β-1. LAP orchestrates controlled TGF-β-1 activation in different physiological contexts. Recombinant human TGF beta 1/TGFB1 LAP (biotinylated, expressed in HEK293 cells, Avi-tagged) is a biotinylated, Avi-tagged LAP protein expressed in HEK293 cells^[1][2].

TGF beta 1/TGFB1 Protein (transforming growth factor beta 1) is a multifunctional cytokine, which is synthesized by almost all cells. TGF beta 1/TGFB1 Protein has a high ability to bind with TGFbRII^[3].
The sequence of amino acids in TGFb1 proteins from different species is very stable, which leads to the conclusion that in the process of evolution, TGFb has been only slightly altered, and that both in humans and in animals, its function is similar. TGF beta 1/TGFB1 Protein is secreted as an inactive peptide, forming part of a ‘latent complex’ consisting of a mature TGFB1 dimer non-covalently bound to its latency-associated peptide (LAP) and, via LAP, to latent TGFB-binding proteins (LTBPs). Activated TGF beta 1/TGFB1 Protein binds to ubiquitously expressed cell-surface TGFB1 type I receptors (TGFBRI) and type II receptors (TGFBRII), which are transmembrane serine/threonine kinases^[4].
TGF beta 1/TGFB1 Protein regulates cell proliferation, growth, differentiation and cells movement. TGFb1 has immunomodulatory effects. TGF beta 1/TGFB1 Protein has profibrogenic effects. TGF beta 1/TGFB1 Protein action can be local and systemic. TGF beta 1/TGFB1 Protein plays a driving role in development, fibrosis and cancer^[4].

Immobilized Human ITGAV&ITGB6,His Tag at 1 μg/mL (100 μL/Well) on the plate. Dose response curve for Biotinylated Human LAP(TGF beta 1), His Tag with the EC₅₀ of ≤0.42 μg/mL determined by ELISA

Human

HEK293

N-His;N-Avi

P01137 (L30-R278, C33S)

7040  [NCBI]

40-50 kDa

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

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4. 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 ddH₂O.

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]