TGFB1 Recombinant Human Protein
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Gibco™

TGFB1 Recombinant Human Protein

Recombinant Human TGF beta 1 (TGFB1) is a bioactive protein intended for use in cell culture applications. TGFB1 acts synergisticallyRead more
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Catalog number CTP9213
Price (TWD)
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Recombinant Human TGF beta 1 (TGFB1) is a bioactive protein intended for use in cell culture applications. TGFB1 acts synergistically with TGF-α in inducing transformation and acts as a negative autocrine growth factor. Dysregulation of TGFB1 activation and signaling may result in apoptosis. The lyophilized TGFB1 Recombinant Human is verified for activity through dose-dependent inhibition of proliferation of mouse HT-2 cells stimulated with mouse IL-4.

Highly Pure—minimizes interference from other proteins or contaminants
Active—get more results with less protein

High Purity
To help verify that GIBCO™ Recombinant growth factors are of the highest quality, each protein is analyzed for purity, along with structural homogeneity, to help ensure a biologically active protein. The purity of each GIBCO™ recombinant growth factor is verified by SDS-PAGE to be over 95% pure and to have endotoxin levels below 0.1 ng/μg.

High Biological Activity
All GIBCO™ Recombinant growth factors are verified for activity. Each lot has its own ED50 determined using an activity assay based on a specific function of the growth factor. The activity of our TGFB1 Recombinant Human growth factor is determined by the dose-dependent inhibition of proliferation of mouse HT-2 cells stimulated with mouse IL-4 to have an ED50 ≤0.2ng/mL. Optimal concentration for individual applications should be determined by a dose response assay.

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For Research Use Only. Not for use in diagnostic procedures.
Specifications
Activity0.05 ng/ml
BioassayInhibition of Proliferation of HT2 cells
ClassificationCarrier-Free
Endotoxin Level< 0.1 ng/μg
Expression SystemMammalian
Gene AliasTGF-β1
Molecular Weight (g/mol)25 kDa
Product LineGibco
Protein FamilyGrowth Factors & Receptors
Protein FormRecombinant, Ligand
Protein Length112 aa
Protein SubtypeTGFs (Transforming Growth Factors)
Purification MethodSequential Chromatography
Purity or Quality Grade95 %
Quantity1 mg
Research CategoryClinical Research, Neurobiology, Oncology, Stem Cell Research, Cardiovascular Research, Differentiation, Immunology, Bone Research
Shipping ConditionWet Ice
For Use With (Application)Cell Culture
FormLyophilized
RecombinantRecombinant
SpeciesHuman
Unit Size1 mg
Contents & Storage
2° to 8°C

Frequently asked questions (FAQs)

It looks like the recombinant protein vial I received from you is empty. Is this normal?

Gibco recombinant proteins are frequently formulated without carrier proteins or additives (e.g., BSA, HSA, sucrose, etc.) and no Gibco PeproTech recombinant protein contains a carrier protein. As a result, during lyophilization, the protein product may be deposited on the vial as a thin, and sometimes invisible, film instead of a pellet. The size of the pellet, if any, is not directly related to the quantity of the recombinant protein in the vial. Our quality control procedures assure that each vial contains the correct amount of product.

To ensure complete recovery of protein product, before opening a vial of lyophilized recombinant protein, we recommend centrifuging it in a microcentrifuge for 20-30 seconds to drive any protein that may be lodged in the cap or on the side to the bottom of the vial. After reconstitution, you can confirm the presence of product protein by running a small amount on SDS-PAGE. In general, a protein band with expected size should be visible with as little as 10 ng of protein loaded on an acrylamide gel.

Find additional tips, troubleshooting help, and resources within our Cell Culture Support Center.

Why does my recombinant protein not show activity in my own experiment?

Assay time is critical. Each assay needs to beoptimized and performed at the peak response time. Different cells may respond differently to a growth factor or cytokine. We suggest repeating our QC assay using same indicator cells as suggested in the manual to see if you can obtain a similar response. In addition, serum may be masking the response. Serum starvation might be needed for certain types of assays.

How should I store the reconstituted recombinant proteins?

Protein solutions are generally not very stable when frozen at low concentration. Upon freeze and thaw, some proteins in the solution may stick to the wall of the container, which results in significant reduction of protein concentration if the starting concentration was low. Therefore, carrier proteins are used to reduce such loss. The most commonly used carrier proteins include bovine serum albumin (BSA), human serum albumin (HSA), or fetal bovine serum (FBS). These carrier proteins are generally used at 0.1% concentration. As a rule of thumb, if the concentration of the recombinant protein is less than 0.5 mg/mL, it is a good idea to add some carrier protein

How do I store my lyophilized recombinant protein?

Lyophilized proteins can typically be stored at 2 to 8 degrees C for several weeks, or stored dessicated at -20 degrees C for long-term storage.

Citations & References (9)

Citations & References
Abstract
Transforming growth factor ß signaling upregulates the expression of human GDP-fucose transporter by activating transcription factor Sp1.
Authors:Xu YX, Ma A, Liu L
Journal:
PubMed ID:24069312
'GDP-fucose transporter plays a crucial role in fucosylation of glycoproteins by providing activated fucose donor, GDP-fucose, for fucosyltransferases in the lumen of the Golgi apparatus. Fucose-containing glycans are involved in many biological processes, which are essential for growth and development. Mutations in the GDP-fucose transporter gene cause leukocyte adhesion deficiency ... More
Mechanotransduction is enhanced by the synergistic action of heterotypic cell interactions and TGF-ß1.
Authors:Youssef J, Chen P, Shenoy VB, Morgan JR
Journal:FASEB J
PubMed ID:22375018
'With the use of planar substrates and collagen gels, the field of mechanotransduction has focused on the role of extracellular matrix stiffness, mechanical tension, and TGF-ß1 in generating a more contractile fibroblast. However, little is known about the role of cell-cell interactions in inducing cellular contraction. We used 3-dimensional self-assembled ... More
The anti-metastatic activity of collagenase-2 in breast cancer cells is mediated by a signaling pathway involving decorin and miR-21.
Authors:Soria-Valles C, Gutiérrez-Fernández A, Guiu M, Mari B, Fueyo A, Gomis RR, López-Otín C
Journal:
PubMed ID:23851508
'Matrix metalloproteinases (MMPs) have been traditionally implicated in cancer progression because of their ability to degrade the extracellular matrix. However, some members of the MMP family have recently been identified as proteases with antitumor properties. Thus, it has been described that collagenase-2 (MMP-8) has a protective role in tumor and ... More
Dextran derivatives modulate collagen matrix organization in dermal equivalent.
Authors:Frank L, Lebreton-Decoster C, Godeau G, Coulomb B, Jozefonvicz J
Journal:J Biomater Sci Polym Ed
PubMed ID:16800152
'Dextran derivatives can protect heparin binding growth factor implied in wound healing, such as transforming growth factor-beta1 (TGF-beta1) and fibroblast growth factor-2 (FGF-2). The first aim of this study was to investigate the effect of these compounds on human dermal fibroblasts in culture with or without TGF-beta1. Several dextran derivatives ... More
Alpha-2 Heremans Schmid Glycoprotein (AHSG) modulates signaling pathways in head and neck squamous cell carcinoma cell line SQ20B.
Authors:Thompson PD, Sakwe A, Koumangoye R, Yarbrough WG, Ochieng J, Marshall DR
Journal:
PubMed ID:24332981
'This study was performed to identify the potential role of Alpha-2 Heremans Schmid Glycoprotein (AHSG) in Head and Neck Squamous Cell Carcinoma (HNSCC) tumorigenesis using an HNSCC cell line model. HNSCC cell lines are unique among cancer cell lines, in that they produce endogenous AHSG and do not rely, solely, ... More