TGF-beta 3 Antibody Summary
25% cross‑reactivity with recombinant amphibian TGF-beta 5 is observed, less than 10% cross‑reactivity with TGF-beta 1, TGF-beta 1.2, and TGF-beta 2 is observed, and less than 5% cross-reactivity with recombinant human LAP (TGF-beta 1) is observed.
Accession # P10600
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of TGF‑ beta 3 by Western Blot. Western blot shows lysates of Saos‑2 human osteosarcoma cell line, L‑929 mouse fibroblast cell line, and A549 human lung carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-TGF‑ beta 3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-243-NA) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for TGF‑ beta 3 at approximately 67 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Human TGF‑ beta 3 by Simple WesternTM.
Simple Western lane view shows lysates of A549 human lung carcinoma cell line and Saos‑2 human osteosarcoma cell line, loaded at 0.2 mg/mL. A specific band was detected for TGF‑ beta 3 at approximately 67 kDa (as indicated) using 10 µg/mL of Goat Anti-TGF‑ beta 3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-243-NA) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody
(Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
TGF‑ beta 3 Inhibition of IL‑4-dependent Cell Proliferation and Neutralization by TGF‑ beta 3 Antibody. Recombinant Human TGF‑ beta 3 (Catalog # 243-B3) inhibits Recombinant Mouse IL‑4 (Catalog # 404-ML) induced proliferation in the HT‑2 mouse T cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Mouse IL‑4 (7.5 ng/mL) activity elicited by Recombinant Human TGF‑ beta 3 (0.1 ng/mL) is neutralized (green line) by increasing concentrations of TGF‑ beta 3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-243-NA). The ND50 is typically 0.01-0.05 µg/mL.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: TGF-beta 3
TGF-beta 3 (transforming growth factor beta 3) is one of three closely related mammalian members of the large TGF-beta superfamily that share a characteristic cystine knot structure (1‑7). TGF-beta 1, -2 and -3 are highly pleiotropic cytokines that are proposed to act as cellular switches that regulate processes such as immune function, proliferation and epithelial-mesenchymal transition (1‑4). Each TGF-beta isoform has some non-redundant functions; for TGF-beta 3, mice with targeted deletion show defects palatogenesis and pulmonary development (2). Human TGF-beta 3 cDNA encodes a 412 amino acid (aa) precursor that contains a 20 aa signal peptide and a 392 aa proprotein (8). A furin-like convertase processes the proprotein to generate an N-terminal 220 aa latency-associated peptide (LAP) and a C-terminal 112 aa mature TGF- beta 3 (8, 9). Disulfide-linked homodimers of LAP and TGF-beta 3 remain non-covalently associated after secretion, forming the small latent TGF-beta 3 complex (8‑10). Covalent linkage of LAP to one of three latent TGF-beta binding proteins (LTBPs) creates a large latent complex that may interact with the extracellular matrix (9, 10). TGF-beta is activated from latency by pathways that include actions of the protease plasmin, matrix metalloproteases, thrombospondin 1 and a subset of integrins (10). Mature human TGF-beta 3 shows 100%, 99% and 98% aa identity with mouse/dog/horse, rat and pig TGF-beta 3, respectively. It demonstrates cross-species activity (1). TGF-beta 3 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-beta RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-beta RI (also called activin receptor-like kinase (ALK) -5), or alternatively, ALK-1.This complex phosphorylates and activates Smad proteins that regulate transcription (3, 11, 12). Contributions of the accessory receptors betaglycan (also known as TGF-beta RIII) and endoglin, or use of Smad-independent signaling pathways, allow for disparate actions observed in response to TGF-beta in different contexts (11).
- Sporn, M.B. (2006) Cytokine Growth Factor Rev. 17:3.
- Dunker, N. and K. Krieglstein (2000) Eur. J. Biochem. 267:6982.
- Wahl, S.M. (2006) Immunol. Rev. 213:213.
- Chang, H. et al. (2002) Endocr. Rev. 23:787.
- Lin, J.S. et al. (2006) Reproduction 132:179.
- Hinck, A.P. et al. (1996) Biochemistry 35:8517.
- Mittl, P.R.E. et al. (1996) Protein Sci. 5:1261.
- Derynck, R. et al. (1988) EMBO J. 7:3737.
- Miyazono, K. et al. (1988) J. Biol. Chem. 263:6407.
- Oklu, R. and R. Hesketh (2000) Biochem. J. 352:601.
- de Caestecker, M. et al. (2004) Cytokine Growth Factor Rev. 15:1.
- Zuniga, J.E. et al. (2005) J. Mol. Biol. 354:1052.
Citations for TGF-beta 3 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 4
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Expression of versican V3 by arterial smooth muscle cells alters tumor growth factor beta (TGFbeta)-, epidermal growth factor (EGF)-, and nuclear factor kappaB (NFkappaB)-dependent signaling pathways, creating a microenvironment that resists monocyte adhesion.
Authors: Kang I, Yoon D, Braun K, Wight T
J Biol Chem, 2014;289(22):15393-404.
Sample Types: Whole Cells
Transforming growth factor Beta 3 is required for excisional wound repair in vivo.
Authors: Le M, Naridze R, Morrison J, Biggs L, Rhea L, Schutte B, Kaartinen V, Dunnwald M
PLoS ONE, 2012;7(10):e48040.
Sample Types: In Vivo
Activation of transforming growth factor-beta by the integrin alphavbeta8 delays epithelial wound closure.
Authors: Neurohr C, Nishimura SL, Sheppard D
Am. J. Respir. Cell Mol. Biol., 2006;35(2):252-9.
Sample Types: Whole Cells
Expression of growth factors and growth factor receptor in non-healing and healing ischaemic ulceration.
Authors: Murphy MO, Ghosh J, Fulford P, Khwaja N, Halka AT, Carter A, Turner NJ, Walker MG
Eur J Vasc Endovasc Surg, 2006;31(5):516-22.
Sample Types: Whole Tissue
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