Recombinant Rat Transforming Growth Factor Beta-1 Proprotein (TGFB1) Protein (His)

Name: Recombinant Rat Transforming Growth Factor Beta-1 Proprotein (TGFB1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-11014P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Rat Transforming Growth Factor Beta-1 Proprotein (TGFB1) Protein (His) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P17246
Target Symbol	TGFB1
Synonyms	Tgfb1; Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide; LAP); Transforming growth factor beta-1; TGF-beta-1)]
Species	Rattus norvegicus (Rat)
Expression System	Baculovirus
Tag	N-6His
Target Protein Sequence	LSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESADPEPEPEADYYAKEVTRVLMVDRNNAIYDKTKDITHSIYMFFNTSDIREAVPEPPLLSRAELRLQRFKSTVEQHVELYQKYSNNSWRYLGNRLLTPTDTPEWLSFDVTGVVRQWLNQGDGIQGFRFSAHCSCDSKDNVLHVEINGISPKRRGDLGTIHDMNRPFLLLMATPLERAQHLHSSRHRR
Expression Range	30-278aa
Protein Length	Partial
Mol. Weight	29.6 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. 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.; 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. 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'. Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. 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. 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.
Subcellular Location	[Latency-associated peptide]: Secreted, extracellular space, extracellular matrix.; [Transforming growth factor beta-1]: Secreted.
Protein Families	TGF-beta family
Database References	KEGG: rno:59086 STRING: 10116.ENSRNOP00000028051 UniGene: Rn.40136
Tissue Specificity	Abundant in the bone matrix.

Gene Functions References

High TGFB1 expression is associated with glomerular mesangial cell hypertrophy. PMID: 29397070
High TGFB1 expression is associated with liver fibrosis. PMID: 30243650
In the present study, we assessed the effect of boldine on the progression of kidney disease using the 2K1C hypertension model and identifying mediators in the RAS, such as TGF-β, that could be modulated by this alkaloid PMID: 29941815
Ang II induced epithelial-mesenchymal transition in renal tubular epithelial cells via Tgfb1. PMID: 29746862
LET suppression promoted BMSCs proliferation by up-regulating the expression of TGF-beta1 and activating Wnt/beta-catenin pathway. PMID: 29068476
These findings implicate TGFbeta1 as one of the important factors impairing drug induced CYP induction in co-cultures and suggests that caution needs to be exercised in the use of hepatocyte-fibroblast co-cultures for CYP induction studies. PMID: 29366910
This suggests that MG53 is a potential regulator of atrial fibrosis induced by the TGF-beta1/Smad pathway in patients with atrial fibrillation . PMID: 29233682
This suggests that soybean isoflavones could delay the process of renal interstitial fibrosis in DN rats by decreasing the expression of Wnt4, beta-catenin and TGF-beta1 in the renal interstitium, thus demonstrating that soybean isoflavones plus losartan have the best protective effects against diabetes-induced renal fibrosis. PMID: 29921370
The results of our study suggest that miR-142 inhibits proliferation and promotes apoptosis in ASMCs during airway remodeling in asthmatic rats by inhibiting TGF-beta expression via a mechanism involving the EGFR signaling pathway. PMID: 29949788
In cultured hippocampal neurons, TGF-[beta]1 prevented A[beta]1-42-induced APP, TNF-[alpha], Bax, cleaved caspase-3, and cleaved caspase-9 expression upregulation, and cell apoptosis, showing a neuroprotective effect of TGF-[beta]1. Silencing of the T[beta]R1 gene abolished the neuroprotective effect of TGF-[beta]1. PMID: 29200096
Acetyl-11-Keto-beta-Boswellic Acid is able to attenuate oxidative stress and profibrotic mechanisms, and improve vascular remodeling in hypertension through TGF-beta1/Smad3 pathway. PMID: 28009003
the truncated variant of gHGF (a double mutant of N-terminal hairpin and first kringle domains of gHGF, K132E and G134E, gmNK1) protein fused with His6 tag, the molecular weight of which was about 20.0kDa, which was expressed in Escherichia coli BL21 (DE3) and purified with Ni(2+)-affinity chromatography.gmNK1 inhibited protein expression levels of fibrosis-related Col I and alpha-SMA in TGF-beta1-activated HSC-T6 cells PMID: 28837849
The results suggest that the CIP4/Par6 complex plays an important role in the occurrence of epithelial-mesenchymal transition in TGF-beta1-stimulated epithelial kidney cells. PMID: 28848997
calcitonin and TGF-beta have roles in cartilage degeneration and nociception in an experimental rat model of osteoarthritis PMID: 27345362
Suggest a potentially mutual regulation between IGFBPrP1 and TGFbeta1, which activates hepatic stellate cells and extracellular matrix deposition. PMID: 28823370
Study demonstrated that the activation of transforming growth factor-beta1 (TGF-beta1) in mild traumatic brain injury (mTBI) correlated with the induction of free radical generating enzyme NADPH oxidase 1 (NOX1). Study study could establish the significance of TGF-beta1 in transforming the pathophysiology of mTBI into secondary injury. PMID: 28433746
TGF-Beta1 (and Egr-1) are up-regulated by sustained hyperosmolarity in the renal medulla. PMID: 28673338
The positive correlation between Reg1a and Tgfb1 genes expression was determined in the dynamics of stress-induced gastric lesions development and healing, which may indicate the involvement of Tgfb1 in acceleration of lesions healing. PMID: 29537200
In conclusion, PFD and Collagen-PVP decrease inflammation, fibrosis, TGFbeta-1 expression, and CD in the posttracheoplasty rats' scar. PMID: 28584818
TGFB1-expressing mesenchymal stem cells induce local tolerance in a rat liver transplantation model of acute rejection. PMID: 27333806
In the present study, isolated rat peritoneal mesothelial cells were treated with TGF-beta1 and/or IL-6 which elicited mesenchymal transition (MMT) as determined by morphologic and biochemical techniques ..Partial characterization of relevant signaling pathways identified Erk1/2 activation, which was enhanced by combined TGF-b1/IL-6 administration, as a crucial necessary factor in the transition.. PMID: 26825317
miR-497 could suppress TGFbeta1-induced pulmonary fibroblast proliferation and EIF3A, Collagen I and alpha-SMA protein levels. PMID: 28322466
could prevent cardiac fibroblasts from activation into myofibroblast and protect HUVEC against endothelial to mesenchymal transition. These effects may be mediated by inhibition of the TGFbeta pathway in both cardiac fibroblasts and HUVECs. PMID: 28303407
Administration of Methylglyoxal led to depletion of antioxidant enzymes, induction of fibrosis (p < 0.001), up-regulated expression of RAGE (3.5 fold), TGF-beta (4.4 fold), SMAD2 (3.7 fold), SMAD3 (6.0 fold), IL-6 (4.3 fold) and TNF-alpha (5.5 fold) in the heart tissues compared to control rats. PMID: 28091942
High TGFB1 expression is associated with pulmonary arterial hypertension. PMID: 29069575
Data suggest that white adipose tissues in various sites respond differently to distinct diet patterns regarding Tgfb expression and signaling pathways; here, energy-restricted and fat-restricted diet containing fish oil down-regulates expression of Tgfb in mesenteric adipose tissue and up-regulates expression of Tgfb in retroperitoneal adipose tissue. PMID: 27736730
Brd4 inhibition attenuates unilateral ureteral obstruction-induced fibrosis by blocking TGF-beta-mediated Nox4 expression. PMID: 28063381
Transforming growth factor beta 1 overexpression observably activated these two pathways, suggesting that Transforming growth factor beta 1 might participate in the modulation of vitamin D through regulating ERK and JNK pathways in Bone marrow-derived mesenchymal stem cells. PMID: 28817810
The data suggest that miR-155 plays a role in mediating TGF-beta1-induced podocyte injury via nephrin, desmin and caspase-9. PMID: 28719898
This paper provides evidence that TGF-beta stimulates prolonged EGFR transactivation, which is dependent on c-Src tyrosine kinase (Src). PMID: 28943431
Although TGF-beta promotes circulating regulatory T cells (Tregs)in female spontaneously hypertensive rats (SHR), it does not account for the sex difference in renal Tregs in SHR. PMID: 28679591
Mesenchymal stem cells could inhibit the process of chronic rejection of small intestine transplant. The mechanisms may include the inhibited function of these cells on lymphocyte proliferation, reduced infiltration of macrophages, and reduced expression of transforming growth factor beta1 and platelet-derived growth factor C. PMID: 28338461
this study shows that FTY720 attenuates renal fibrosis by TGF-beta signaling in fibroblasts PMID: 28658504
Apigenin ameliorated renal damage due to diabetic nephropathy by suppressing oxidative stress and fibrosis via MAPK-NF-kappaB-TNF-alpha and TGF-beta1-MAPK-fibronectin pathways. PMID: 28566504
High glucose stress suppresses SnoN while activating TGF-beta1 and Rnf111 (Arkadia) in renal tubular epithelial cells and diabetic rats. PMID: 28350874
The fibromodulin (Fm)-transforming growth factor (TGF)-beta1 nexus plays a crucial in fetal-type scarless skin repair. PMID: 27665369
mRNA/protein levels are increased in kidney remnants from 5/6 nephrectomized rats and strongly correlate with TGF-beta1 expression. PMID: 27714812
Data indicate transforming growth factor beta (TGFbeta) involvement in early activation of platelet-derived growth factor receptor beta (PDGFRbeta)+ pericytes in aristolochic acid induced acute kidney injury. PMID: 27379382
TGFbeta1 is involved in cholangiocarcinoma tumor progression and participates through miR-34a mediated downstream signaling cascades. PMID: 27364974
In high glucose-treated glomerular mesangial cells, TGR5 can suppress the NF-kappaB-mediated upregulation of fibronectin and TGF-beta1 by inhibiting RhoA/ROCK signaling via protein kinase A. PMID: 27470217
this study shows that TGF-beta1 vaccine attenuated diabetic nephropathy in OLETF rats through reduction of inflammation, improvement of kidney fibrosis and partial correction of glucose metabolism PMID: 27485077
No differences in fiber arrangement, structure, and nuclei form were noted in either group (P > 0.05). Our findings suggest that TGF-beta1 signaling is necessary for the regulation of tendon cross-link formation, as well as collagen and LOX gene transcription in an exercise-dependent manner. PMID: 27927626
Overexpression of IL-6 is sufficient to induce myofibroblastic proliferation, differentiation, and fibrosis, probably via increased TGF-beta1-mediated MMP2/MMP3 signaling during ischemic myocardial remodeling monoculture or coculture models under hypoxic conditions. PMID: 27348628
TGFbeta1 specifically elevates the expression level of TRPC6 mainly through Smad-dependent canonical pathway. The siRNA against TRPC6 abolished TGFbeta1-induced molecular and cellular phenotype changes, including myosin light chain phosphorylation, actin stress fiber formation, and cell migration. PMID: 28039055
in diabetes, retinal vessels become dependent on a small increase in TGF-beta signaling via activin receptor-like kinase 5 to maintain early integrity. PMID: 28162229
the application of TSLP short hairpin RNA caused a stark reversal of the TGF-beta1-induced cellular fibrosis. PMID: 27492484
this study shows that adipose-derived stem cells treatment attenuates renal interstitial fibrosis possibly through inhibition of epithelial-mesenchymal transition and inflammatory response via TGF-beta1 signaling pathway PMID: 28092863
Alloxan-induced renal damage is associated with alterations of p53, TGF-beta1, and extracellular matrix metalloproteinases. PMID: 28220578
Calcitriol may protect diabetic nephropathy from fibrosis via inhibition of TGF-beta1 and CIP4. PMID: 26097534
The in vitro and in vivo models revealed that lipid metabolism disorder and FK506 caused oxidative stress and a fibrogenic response. In addition, decreased levels of LOX1 markedly reduced the levels of TGFb1 in the in vitro model. PMID: 27633115

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.