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TGF b 1 recombinant protein :: Transforming Growth Factor-Beta 1 Recombinant Protein

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Catalog # MBS142349
Unit / Price
  0.002 mg  /  $140 +1 FREE 8GB USB
  0.01 mg  /  $205 +1 FREE 8GB USB
  0.1 mg  /  $1,030 +1 FREE 8GB USB
TGF b 1 recombinant protein
Product Name

Transforming Growth Factor-Beta 1 (TGF b 1), Recombinant Protein

Popular Item
Also Known As

Recombinant Human Transforming Growth Factor-Beta 1, GST tag

Product Synonym Names
TGF b 1 Human, GST; Transforming Growth Factor-Beta 1 Human Recombinant, GST Tag; Transforming growth factor beta-1; TGF-beta-1; CED; DPD1; TGFB; TGF b 1 GST
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Length
390
Sequence
KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS
OMIM
131300
3D Structure
ModBase 3D Structure for P01137
Host
E Coli
Purity/Purification
Greater than 80.0% as determined by SDS-PAGE.
Form/Format
The protein solution (500 ug/ml) contains 50mM Tris-HCl, pH-7.5 and 10mM L-glutathione (reduced).
Sterile Filtered solution.
Preparation and Storage
Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Other Notes
Small volumes of TGF b 1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
TGF b 1 recombinant protein
Description: The Recombinant Human TGF-b1 (aa 309-391) is purified by standard chromatographic techniques and shows a 35kDa band on SDS-PAGE (including GST tag).

Introduction: Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
NCBI/Uniprot data below describe general gene information for TGF b 1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
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  [Similar Products]
NCBI Official Synonym Symbols
CED; LAP; DPD1; TGFB; TGFbeta
  [Similar Products]
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  [Similar Products]
UniProt Synonym Gene Names
TGFB; TGF-beta-1; LAP  [Similar Products]
UniProt Entry Name
TGFB1_HUMAN
NCBI Summary for TGF b 1
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 Comments for TGF b 1
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: proteinaceous extracellular matrix; extracellular space; cell surface; microvillus; 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; 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 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; salivary gland morphogenesis; positive regulation of cell proliferation; 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 growth; negative regulation of cell-cell adhesion; 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; transforming growth factor beta receptor signaling pathway; positive regulation of superoxide release; receptor catabolic process; germ cell migration; response to glucose stimulus; chondrocyte differentiation; defense response to fungus, incompatible interaction; negative regulation of mitotic cell cycle; 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; positive regulation of histone deacetylation; response to radiation; 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: Cystic Fibrosis; Camurati-engelmann Disease
Precautions
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Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

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