Product: TGF beta 1 Antibody
Catalog: AF1027
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Dog
Mol.Wt.: 44~65kD(precursor), 28kD(dimer), 15kD(monomer); 44kD(Calculated).
Uniprot: P01137
RRID: AB_2835389

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Product Info

Source:
Rabbit
Application:
WB: 1:500-1:2000, IHC: 1:50-1:200, IF/ICC 1:200, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Dog(100%)
Clonality:
Polyclonal
Specificity:
TGF beta1 Antibody detects endogenous levels of total TGF beta1.
RRID:
AB_2835389
Cite Format: Affinity Biosciences Cat# AF1027, RRID:AB_2835389.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Cartilage-inducing factor; CED; Differentiation inhibiting factor; DPD1; LAP; Latency-associated peptide; Prepro transforming growth factor beta 1; TGF beta 1; TGF beta; TGF beta 1 protein; TGF-beta 1 protein; TGF-beta-1; TGF-beta-5; TGF-beta1; TGFB; Tgfb-1; tgfb1; TGFB1_HUMAN; TGFbeta; TGFbeta1; Transforming Growth Factor b1; Transforming Growth Factor beta 1; Transforming growth factor beta 1a; transforming growth factor beta-1; transforming growth factor, beta 1; Transforming Growth Factor-ß1;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P01137 TGFB1_HUMAN:

Highly expressed in bone (PubMed:11746498, PubMed:17827158). Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA) (PubMed:11746498, PubMed:17827158). Colocalizes with ASPN in chondrocytes within OA lesions of articular cartilage (PubMed:17827158).

Description:
Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors.
Sequence:
MPPSGLRLLLLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Xenopus
0
Zebrafish
0
Chicken
0
Rabbit
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P01137 As Substrate

Site PTM Type Enzyme
K42 Sumoylation
K42 Ubiquitination
K56 Ubiquitination
N82 N-Glycosylation
K106 Ubiquitination
K163 Ubiquitination
K291 Ubiquitination
K309 Ubiquitination
Y317 Phosphorylation

Research Backgrounds

Function:

Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively.

Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1. Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia (Probable). Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1.

Transforming growth factor beta-1: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix. At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus. TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1. Once activated following release of LAP, TGF-beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal. While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency-associated peptide chain (LAP) and 'milieu molecules' (By similarity). Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (By similarity). At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development (By similarity). At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus. Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types.

PTMs:

Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive.

N-glycosylated. Deglycosylation leads to activation of Transforming growth factor beta-1 (TGF-beta-1); mechanisms triggering deglycosylation-driven activation of TGF-beta-1 are however unclear.

Subcellular Location:

Secreted>Extracellular space>Extracellular matrix.

Secreted.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Highly expressed in bone. Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA). Colocalizes with ASPN in chondrocytes within OA lesions of articular cartilage.

Subunit Structure:

Homodimer; disulfide-linked. Interacts with the serine proteases, HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated signaling. The HTRA protease activity is required for this inhibition (By similarity). May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling (By similarity). Interacts with CD109, DPT and ASPN. Latency-associated peptide: Homodimer; disulfide-linked. Latency-associated peptide: Interacts with Transforming growth factor beta-1 (TGF-beta-1) chain; interaction is non-covalent and maintains (TGF-beta-1) in a latent state; each Latency-associated peptide (LAP) monomer interacts with TGF-beta-1 in the other monomer. Latency-associated peptide: Interacts with LTBP1; leading to regulate activation of TGF-beta-1. Latency-associated peptide: Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs). Interacts with LRRC33/NRROS; leading to regulate activation of TGF-beta-1 in macrophages and microglia (Probable). Latency-associated peptide: Interacts (via cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release of the active TGF-beta-1. Latency-associated peptide: Interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction (By similarity). Latency-associated peptide: Interacts with HSP90AB1; inhibits latent TGFB1 activation. Transforming growth factor beta-1: Homodimer; disulfide-linked. Transforming growth factor beta-1: Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction.

Family&Domains:

The 'straitjacket' and 'arm' domains encircle the Transforming growth factor beta-1 (TGF-beta-1) monomers and are fastened together by strong bonding between Lys-56 and Tyr-103/Tyr-104.

The cell attachment site motif mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8) (PubMed:28117447). The motif locates to a long loop in the arm domain called the bowtie tail (PubMed:28117447). Integrin-binding stabilizes an alternative conformation of the bowtie tail (PubMed:28117447). Activation by integrin requires force application by the actin cytoskeleton, which is resisted by the 'milieu molecules' (such as LTBP1, LRRC32/GARP and/or LRRC33/NRROS), resulting in distortion of the prodomain and release of the active TGF-beta-1 (PubMed:28117447).

Belongs to the TGF-beta family.

Research Fields

· Cellular Processes > Cell growth and death > Cell cycle.   (View pathway)

· Cellular Processes > Cell growth and death > Cellular senescence.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Environmental Information Processing > Signaling molecules and interaction > Cytokine-cytokine receptor interaction.   (View pathway)

· Environmental Information Processing > Signal transduction > FoxO signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > TGF-beta signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Hippo signaling pathway.   (View pathway)

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Infectious diseases: Parasitic > Leishmaniasis.

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

· Human Diseases > Infectious diseases: Parasitic > Malaria.

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Specific types > Colorectal cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Renal cell carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Pancreatic cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Chronic myeloid leukemia.   (View pathway)

· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Gastric cancer.   (View pathway)

· Human Diseases > Immune diseases > Inflammatory bowel disease (IBD).

· Human Diseases > Immune diseases > Rheumatoid arthritis.

· Human Diseases > Cardiovascular diseases > Hypertrophic cardiomyopathy (HCM).

· Human Diseases > Cardiovascular diseases > Dilated cardiomyopathy (DCM).

· Organismal Systems > Development > Osteoclast differentiation.   (View pathway)

· Organismal Systems > Immune system > Th17 cell differentiation.   (View pathway)

· Organismal Systems > Immune system > Intestinal immune network for IgA production.   (View pathway)

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

References

1). Ai XY et al. Phenytoin silver: a new nanocompound for promoting dermal wound healing via comprehensive pharmacological action. Theranostics 2017 Jan 5;7(2):425-435 (PubMed: 28255340) [IF=11.600]

Application: WB    Species: human    Sample:

Figure 6. PnAg regulates gp130/Jak/Stat3 signaling pathway (A) and (B) NIH-3T3 and HaCat Cells were treated with PnAg at different concentrations and cell viability was tested using MTT analysis. (C) Wound healing assay reflected the effect of PnAg on cell migration. (D) Binding mode of PnAg in the active pocket of gp130. (E) and (F) MMPs activity and expression levels of Stat3, VEGF, TGFB-1, and TGFB1 detected using zymographic and Western blot assays. (G) Diagram of the proposed function of PnAg in wound inflammation and re-epithelialization controls.

Application: IHC    Species: rat    Sample:

Figure 2. PnAg promotes wound healing in SD rats. (A) Photographs of rat skin full-thickness excision wounds on different post-excision days. (B) Change in wound areas of SD rats after treatment; (C) and (D) Expression levels of collagen I, NF-κB, TGF-ß, MMP-2, and MMP-9 in tissues on day 7 and 17 detected by immunohistochemistry. (E) Histogram of protein expression levels in these tissues. (F) and (G) Histomorphological changes in wound tissues stained by Masson trichrome and HE on day 17.

2). Ding T et al. An in situ tissue engineering scaffold with growth factors combining angiogenesis and osteoimmunomodulatory functions for advanced periodontal bone regeneration. J Nanobiotechnology 2021 Aug 17;19(1):247. (PubMed: 34404409) [IF=10.435]

3). Tao HC et al. CD47 Deficiency in Mice Exacerbates Chronic Fatty Diet-Induced Steatohepatitis Through Its Role in Regulating Hepatic Inflammation and Lipid Metabolism. Front Immunol 2020 Feb 25;11:148 (PubMed: 32158445) [IF=8.786]

Application: IHC    Species: mouse    Sample: Liver

Figure S2. |Liver sections were IHC stained for TGF-β (a), IL-6 (b) and IL-10 (c). Three samples per group were examined, and representative images are shown (Scale bar represents 50 µm).

4). Li X et al. Degradation of Different Molecular Weight Fucoidans and Their Inhibition of TGF-β1 Induced Epithelial-Mesenchymal Transition in Mouse Renal Tubular Epithelial Cells. Int J Biol Macromol 2020 May 15;151:545-553. (PubMed: 32057857) [IF=8.025]

Application: IF/ICC    Species: Mouse    Sample: MTEC cells

Fig. 7. The result of cell immunofluorescence assay after LHXs and TGF-β1 treated MTEC for 24 and 48 h. Representative images (3 visual fields for each tissue analyzed) of immunolabeling for Fn and nuclear staining with DAPI. Scale bar, 50 ~μm.

5). Liu H et al. Danshensu alleviates bleomycin-induced pulmonary fibrosis by inhibiting lung fibroblast-to-myofibroblast transition via the MEK/ERK signaling pathway. Bioengineered 2021 Dec;12(1):3113-3124. (PubMed: 34187349) [IF=6.832]

Application: IF/ICC    Species: Mice    Sample: NIH3T3 cells

Figure 2. DSS inhibited TGF-β1-induced fibroblast-myofibroblast differentiation via inhibiting the MEK/ERK signaling pathway in NIH3T3 cells. (a) Immunofluorescence was conducted to evaluate the expression of α-SMA (red). Nucleus was stained with DAPI (blue). Scale bar: 50 μm. (b) Relative mRNA expression of Col1a1 and α-SMA. (c, d) Expressions of p-MEK1/2, MEK1/2, p-ERK1/2, ERK1/ 2 were detected by western blot. GAPDH was conducted as a loading control. One-way ANOVA, **p < 0.01, ***p < 0.001, ****p < 0.0001.

6). Li Y et al. Corilagin alleviates hypertrophic scars via inhibiting the transforming growth factor (TGF)-β/Smad signal pathway. Life Sci 2021 Apr 13;119483. (PubMed: 33862115) [IF=6.780]

Application: WB    Species: Human    Sample: Hypertrophic scar tissue

Fig. 5. Corilagin inhibited the protein levels of TGF-β1, TGFβRI and blocked the phosphorylation of Smad2 and Smad3, as well as affect the protein levels of MMPs and TIMPs. A. Western blot results showed the protein levels of TGF-β1, TGFβRI, and TGFβRII in HSFs incubated with corilagin for 3 days, GAPDH served as control. n = 3. B. Protein levels of phosphorylated and total Smad2 and Smad3 examined by western blot assay after HSFs were treated with corilagin for 3 days. GAPDH served as control. n = 3. C. Immunofluorescence staining of Smad2/3 in HSFs after treating with corilagin (0 μM) + TGF-β1 (0 ng/mL), corilagin (0 μM) + TGF-β1 (5 ng/mL) and corilagin (25 μM) + TGF-β1 (5 ng/mL) for 12 h. Smad2/3 is shown by green fluorescence and nuclei were stained with DAPI, which emits blue fluorescence. Scale bars = 50 μm. D. Protein levels of Smad7 examined by western blot assay after HSFs were treated with corilagin for 3 days. GAPDH served as control. n = 3. E. Protein levels of MMP2, MMP9, MMP13 and TIMP1 in HSFs after treatment with corilagin for 3 days. GAPDH served as control. n = 3. Data are show as mean ± SD. *p < 0.05, **p < 0.01, ***p < 0.001. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Application: IF/ICC    Species: Human    Sample: Hypertrophic scar tissue

Fig. 3. Corilagin repressed HSFs activation. A. Immunofluorescence staining for α-SMA of HSFs after incubation with corilagin (0 μM), corilagin (0 μM) + TGF-β1 (5 ng/mL) and corilagin (25 μM) + TGF-β1 (5 ng/mL) for 48 h. α-SMA is shown by green fluorescence and nuclei were stained with DAPI, which emits blue fluorescence. Scale bars = 50 μm. B. qRT-PCR results of α-SMA mRNA levels in HSFs after incubation with TGF-β1 and corilagin for 3 days. n = 3. C. α-SMA protein levels detected using western blot assay after treatment with TGF-β1 and corilagin for 3 days, and quantification results normalized to GAPDH. n = 3. Data are mean ± SD. *p < 0.05, ***p < 0.001. ns, no significance. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Application: WB    Species: human    Sample: HSFs

Fig. 5. |Corilagin inhibited the protein levels of TGF-β1, TGFβRI and blocked the phosphorylation of Smad2 and Smad3, as well as affect the protein levels of MMPs and TIMPs. A. Western blot results showed the protein levels of TGF-β1, TGFβRI, and TGFβRII in HSFs incubated with corilagin for 3 days, GAPDH served as control.n = 3.

7). Ding Y et al. Bryodulcosigenin attenuates bleomycin‐induced pulmonary fibrosis via inhibiting AMPK‐mediated mesenchymal epithelial transition and oxidative stress. Phytother Res 2022 Jul 6. (PubMed: 35794782) [IF=6.388]

8). Yu SS et al. M1-type microglia can induce astrocytes to deposit chondroitin sulfate proteoglycan after spinal cord injury. Neural Regen Res 2022 May;17(5):1072-1079. (PubMed: 34558535) [IF=6.058]

9). Zhang ZC et al. Highly Acylated Anthocyanins from Purple Sweet Potato ( Ipomoea batatas L.) Alleviate Hyperuricemia and Kidney Inflammation in Hyperuricemic Mice: Possible Attenuation Effects on Allopurinol. J Agric Food Chem 2019 Jun 5;67(22):6202-6211 (PubMed: 31091873) [IF=5.895]

Application: WB    Species: mouse    Sample: renal

Figure 4.| Western blot of HAA-PSP, allopurinol, and their combination on protein expression for TNF-α, TGF-β1, IL-6, IL-1β, ICAM-1, COX-2,and NF-κB p65 in renal tissue of hyperuricemic mice. The contents of target proteins were normalized to GAPDH. Values are expressed as the means ± SD (n = 8). Different letters marked above the bars are significantly different by an ANOVA multiple test (p < 0.05).

10). Yin L et al. Over-Expression of Inhibitor of Differentiation 2 Attenuates Post-Infarct Cardiac Fibrosis Through Inhibition of TGF-β1/Smad3/HIF-1α/IL-11 Signaling Pathway. Front Pharmacol 2019 Nov 13;10:1349 (PubMed: 31803053) [IF=5.810]

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