protein

Human TGF Beta-1 monomer Recombinant

MBS553146

0.002 mg

145 USD

Recombinant Protein

Human TGF Beta-1 monomer Recombinant

TGF Beta-1 monomer

Human TGF Beta-1 Recombinant; tgf beta; transforming growth factor; TGFB1; tgf-b1

transforming growth factor beta-1; Transforming growth factor beta-1

TGF beta

TGFB1; TGFB; TGF-beta-1; LAP

TGFB1_HUMAN

E Coli

390

MPPSGLRLLL LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE ADYYAKEVTR VLMVETHNEI YDKFKQSTHS IYMFFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNNSWR YLSNRLLAPS DSPEWLSFDV TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT TGRRGDLATI HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS

>95%, as determined by SDS-PAGE and HPLC.

Recombinant TGF-b1 is lyophilized from 0.2 um filtered PBS solution pH 7.4.

Upon reconstitution, this cytokine can be stored in working aliquots at 2 degree - 8 degree C for one month, or at -20 degree C for six months. Avoid repeated freeze/thaw cycles.

Domain: cystine knot growth factor. Host Note: Optimized DNA sequence encoding Human Transforming Growth Factor Beta-1 mature chain was expressed in Escherichia Coli.

Endotoxin: Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/ug (1EU/ug). Reconstitution: A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers. Molecular Weight Note: Native human TGF-b1, generated by the proteolytic removal of the signal peptide and propeptide, the molecule has a calculated molecular mass of approximately 26 kDa. Recombinant TGF-beta 1 is a disulfide-linked monomer protein consisting of 113 amino acid residue subunits. TGF-beta 1 migrates as an approximately 12 - 13 kDa protein under reducing conditions in SDS-PAGE.

Cytokines

TGF-beta is the prototype of a protein family known as the TGF-beta superfamily. This family includes Inhibins, Activin A, MIS (M llerian inhibiting substance), BMP (bone morphogenetic proteins), dpp (decapentaplegic) and Vg-1. Type 1 receptors and type 2 receptors have a molecular mass of 53 and 75 kDa, respectively. Signaling through the receptor requires heterodimeric complexes between both types of receptors. The type 2 receptor has been shown to bind the ligand, but it is incapable of mediating TGF- beta responses in the absence of the type 1 receptor. The type 1 receptor is expressed predominantly in hematopoietic progenitor cells. The type 2 receptor encodes a protein with an intracellular domain that functions as a serine/threonine kinase. TGF-beta is the most potent known growth inhibitor for normal and transformed epithelial cells, endothelial cells, fibroblasts, neuronal cells, lymphoid cells and other hematopoietic cell types. TGF-beta inhibits the proliferation of T- lymphocytes by down- regulating predominantly IL- 2 mediated proliferative signals. It also inhibits the growth of natural killer cells in vivo and deactivates macrophages. TGF-beta blocks the antitumor activity mediated in vivo by IL-2 and transferred lymphokine- activated or tumor infiltrating lymphocytes.

cell cycle arrest by tgf-1 enhances rsv replication in lung epithelial cells . J. Virol., Sep 2009; 10.1128/JVI.00806-09. cutting edge: tgf- 1 and il-15 induce foxp3+ regulatory t cells in the presence of antigen stimulation . J. Immunol., Sep 2009; 183: 3574 - 3577. nuclear factor i-c links pdgf and tgf-1 signaling to skin wound healing progression . Mol. Cell. Biol., Sep 2009; 10.1128/MCB.01921-08. mesenchymal stem cells produce wnt isoforms and tgf1 that mediate proliferation and pro-collagen expression by lung fibroblasts . Am J Physiol Lung Cell Mol Physiol, Sep 2009; 10.1152/ajplung.90347.2008. mechanical forces and tgf 1 reduce podocyte adhesion through 3 1 integrin downregulation . Nephrol. Dial. Transplant., Sep 2009; 24: 2645 - 2655.

63025222

NP_000651.3

NM_000660.4

P01137

44,341 Da

ACE Inhibitor Pathway (198763); ALK1 Signaling Events Pathway (137968); Adipogenesis Pathway (198832); Amoebiasis Pathway (167324); Amoebiasis Pathway (167191); Cell Cycle Pathway (198811); Cell Cycle Pathway (83054); Cell Cycle Pathway (463); Chagas Disease (American Trypanosomiasis) Pathway (147809); Chagas Disease (American Trypanosomiasis) Pathway (147795)

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]

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; Motility/polarity/chemotaxis; Secreted. Chromosomal Location of Human Ortholog: 19q13.1. Cellular Component: extracellular space; proteinaceous extracellular matrix; microvillus; cell surface; cell soma; axon; Golgi lumen; 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; female pregnancy; SMAD protein nuclear translocation; 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 chemotaxis; positive regulation of smooth muscle cell differentiation; active induction of host immune response by virus; positive regulation of blood vessel endothelial cell migration; regulation of sodium ion transport; negative regulation of fat cell differentiation; negative regulation of blood vessel endothelial cell migration; lymph node development; positive regulation of protein secretion; positive regulation of transcription from RNA polymerase II promoter; response to progesterone stimulus; endoderm development; myelination; positive regulation of odontogenesis; 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; regulation of DNA binding; ureteric bud development; negative regulation of release of sequestered calcium ion into cytosol; salivary gland morphogenesis; positive regulation of cell proliferation; protein kinase B signaling cascade; protein export from nucleus; inflammatory response; positive regulation of exit from mitosis; aging; 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; protein amino acid phosphorylation; regulation of cell migration; hyaluronan catabolic process; regulation of apoptosis; response to vitamin D; negative regulation of neuroblast proliferation; positive regulation of superoxide release; transforming growth factor beta receptor signaling pathway; receptor catabolic process; germ cell migration; response to glucose stimulus; chondrocyte differentiation; negative regulation of mitotic cell cycle; defense response to fungus, incompatible interaction; T cell homeostasis; 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; lipopolysaccharide-mediated signaling pathway; response to wounding; 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

0.002 mg

145 USD

0.01 mg

220