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.
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.
TGF‑ beta 3 in Human Brain. TGF‑ beta 3 was detected in immersion fixed paraffin-embedded sections of human brain using Goat Anti-TGF‑ beta 3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-243-NA) at 5 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to neuronal cell bodies. Staining was performed using our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
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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