TGF-beta1 active protein

Human TGF-beta1

Cat. Num. AAA695833

• Gene Names: TGFB1; CED; LAP; DPD1; TGFB; TGFbeta
• Reactivity: Species Reactivity: Human; Cross Reactivity: Chicken, Cow, Dog, Frog, Monkey, Mouse, Pig, Rabbit, Rat
• Purity: Above 98% as determined by SDS-PAGE Analysis.
• Synonyms: TGF-beta1; Human TGF-beta1; Recombinant Human TGF-beta1 (CHO cell derived); TGF-beta1 active protein

• Host: CHO cells
• Reactivity: Species Reactivity: Human; Cross Reactivity: Chicken, Cow, Dog, Frog, Monkey, Mouse, Pig, Rabbit, Rat
• Purity/Purification: Above 98% as determined by SDS-PAGE Analysis.
• Sequence: ALDTNYCFS STEKNCCVR QLYIDFRKD LGWKWIHEP KGYHANFCL GPCPYIWSL DTQYSKVLA LYNQHNPGA SAAPCCVPQ ALEPLPIVY YVGRKPKVE QLSNMIVRS CKCS

• Biological Activity: The ED50 was determined by TGF-beta1's ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is <= 0.05 ng/ml, corresponding to a specific activity of >= 2 x 107 units/mg
• Cell Type: T Cells, Treg cells
• Preparation and Storage: At -20 degree C

Testing Data

Related Product Information for TGF-beta1 active protein

The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-beta1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts and recently it has been implicated in the formation of skin tumors. Recombinant human TGF-beta1 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

Product Categories/Family for TGF-beta1 active protein

Innate Immunity; Stem Cell Research; Apoptosis; Cancer; Angiogenesis; Inflammation; Proliferation and Cell Cycle

NCBI and Uniprot Product Information

• NCBI GI #: 135674
• NCBI GeneID: 7040
• UniProt Accession #: P01137; Q9UCG4; A8K792
• Molecular Weight: 44,341 Da
• NCBI Official Full Name: Transforming growth factor beta-1
• NCBI Official Synonym Full Names: transforming growth factor, beta 1
• NCBI Official Symbol: TGFB1
• NCBI Official Synonym Symbols: CED; LAP; DPD1; TGFB; TGFbeta
• NCBI Protein Information: transforming growth factor beta-1; TGF-beta-1; latency-associated peptide; prepro-transforming growth factor beta-1
• UniProt Protein Name: Transforming growth factor beta-1
• UniProt Gene Name: TGFB1
• UniProt Synonym Gene Names: TGFB; TGF-beta-1; LAP
• UniProt Entry Name: TGFB1_HUMAN

NCBI Description

This gene encodes a member of the transforming growth factor beta (TGFB) family of cytokines, which are multifunctional peptides that regulate proliferation, differentiation, adhesion, migration, and other functions in many cell types. Many cells have TGFB receptors, and the protein positively and negatively regulates many other growth factors. The secreted protein is cleaved into a latency-associated peptide (LAP) and a mature TGFB1 peptide, and is found in either a latent form composed of a TGFB1 homodimer, a LAP homodimer, and a latent TGFB1-binding protein, or in an active form composed of a TGFB1 homodimer. The mature peptide may also form heterodimers with other TGFB family members. This gene is frequently upregulated in tumor cells, and mutations in this gene result in Camurati-Engelmann disease.[provided by RefSeq, Oct 2009]

Uniprot Description

TGFB1: 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. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Homodimer; disulfide-linked, or heterodimer with TGFB2. Secreted and stored as a biologically inactive form in the extracellular matrix in a 290 kDa complex (large latent TGF-beta1 complex) containing the TGFB1 homodimer, the latency-associated peptide (LAP), and the latent TGFB1 binding protein-1 (LTBP1). The complex without LTBP1 is known as the'small latent TGF-beta1 complex'. Dissociation of the TGFB1 from LAP is required for growth factor activation and biological activity. Release of the large latent TGF-beta1 complex from the extracellular matrix is carried out by the matrix metalloproteinase MMP3. May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling. 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. Interacts with CD109, DPT and ASPN. Activated in vitro at pH below 3.5 and over 12.5. Highly expressed in bone. Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA). Co-localizes with ASPN in chondrocytes within OA lesions of articular cartilage. Belongs to the TGF-beta family.

Protein type: Secreted, signal peptide; Secreted; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 19q13.1

Cellular Component: extracellular space; proteinaceous extracellular matrix; microvillus; cell surface; cell soma; Golgi lumen; axon; cytoplasm; extracellular region; plasma membrane; nucleus

Molecular Function: protein binding; enzyme binding; protein homodimerization activity; growth factor activity; protein heterodimerization activity; punt binding; cytokine activity; protein N-terminus binding; glycoprotein binding; antigen binding

Biological Process: extracellular matrix organization and biogenesis; positive regulation of apoptosis; positive regulation of transcription, DNA-dependent; SMAD protein nuclear translocation; female pregnancy; positive regulation of protein amino acid dephosphorylation; activation of NF-kappaB transcription factor; regulation of protein import into nucleus; positive regulation of MAP kinase activity; connective tissue replacement during inflammatory response; regulation of transforming growth factor beta receptor signaling pathway; negative regulation of ossification; cell cycle arrest; positive regulation of isotype switching to IgA isotypes; inner ear development; regulatory T cell differentiation; response to drug; positive regulation of interleukin-17 production; positive regulation of smooth muscle cell differentiation; positive regulation of chemotaxis; active induction of host immune response by virus; positive regulation of blood vessel endothelial cell migration; regulation of sodium ion transport; negative regulation of blood vessel endothelial cell migration; negative regulation of fat cell differentiation; lymph node development; positive regulation of protein secretion; positive regulation of transcription from RNA polymerase II promoter; response to progesterone stimulus; endoderm development; positive regulation of odontogenesis; myelination; negative regulation of phagocytosis; evasion of host defenses by virus; positive regulation of cellular protein metabolic process; myeloid dendritic cell differentiation; negative regulation of transcription from RNA polymerase II promoter; phosphate metabolic process; negative regulation of cell proliferation; negative regulation of T cell proliferation; ureteric bud development; regulation of DNA binding; negative regulation of release of sequestered calcium ion into cytosol; positive regulation of cell proliferation; salivary gland morphogenesis; protein kinase B signaling cascade; protein export from nucleus; inflammatory response; aging; positive regulation of exit from mitosis; epidermal growth factor receptor signaling pathway; mitotic cell cycle checkpoint; common-partner SMAD protein phosphorylation; positive regulation of phosphoinositide 3-kinase activity; positive regulation of bone mineralization; positive regulation of peptidyl-serine phosphorylation; SMAD protein complex assembly; positive regulation of protein kinase B signaling cascade; positive regulation of protein complex assembly; positive regulation of protein import into nucleus; response to hypoxia; epithelial to mesenchymal transition; negative regulation of cell-cell adhesion; negative regulation of cell growth; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of skeletal muscle development; mononuclear cell proliferation; regulation of cell migration; protein amino acid phosphorylation; hyaluronan catabolic process; regulation of apoptosis; response to vitamin D; negative regulation of neuroblast proliferation; positive regulation of superoxide release; receptor catabolic process; transforming growth factor beta receptor signaling pathway; germ cell migration; response to glucose stimulus; chondrocyte differentiation; negative regulation of mitotic cell cycle; T cell homeostasis; defense response to fungus, incompatible interaction; cell growth; tolerance induction to self antigen; regulation of striated muscle development; platelet activation; organ regeneration; negative regulation of DNA replication; virus-host interaction; hemopoietic progenitor cell differentiation; negative regulation of transcription, DNA-dependent; positive regulation of epithelial cell proliferation; positive regulation of collagen biosynthetic process; viral infectious cycle; response to estradiol stimulus; negative regulation of cell cycle; response to radiation; positive regulation of histone deacetylation; platelet degranulation; negative regulation of protein amino acid phosphorylation; response to wounding; lipopolysaccharide-mediated signaling pathway; adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains; negative regulation of epithelial cell proliferation; intercellular junction assembly and maintenance; regulation of binding; MAPKKK cascade; cellular calcium ion homeostasis; gut development; protein import into nucleus, translocation; ATP biosynthetic process; positive regulation of histone acetylation; positive regulation of protein amino acid phosphorylation; blood coagulation; negative regulation of myoblast differentiation; positive regulation of cell migration

Disease: Camurati-engelmann Disease; Cystic Fibrosis