Mouse TGFB1 Recombinant Protein (RPPB0972)
- SKU:
- RPPB0972
- Product Type:
- Recombinant Protein
- Species:
- Mouse
- Uniprot:
- P04202
- Research Area:
- Growth Factors & Cytokines
Description
| Product Name: | Mouse TGFB1 Recombinant Protein |
| Product Code: | RPPB0972 |
| Size: | 10µg |
| Species: | Mouse |
| Target: | TGFB1 |
| Synonyms: | Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1. |
| Source: | Escherichia Coli |
| Physical Appearance: | Sterile Filtered colorless solution. |
| Formulation: | TGFB1 protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol. |
| Stability: | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°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. |
| Purity: | Greater than 85.0% as determined by SDS-PAGE. |
| Amino Acid Sequence: | MGSSHHHHHH SSGLVPRGSH MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGPCPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS |
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions which occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins which are very similar in that each is cleaved to yield a 112 amino acid polypeptide which remains associated with the latent portion of the molecule.
TGFB1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (279-390 a.a) and having a molecular mass of 15.2kDa.TGFB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
| UniProt Protein Function: | 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. |
| UniProt Protein Details: | Protein type:Motility/polarity/chemotaxis; Secreted; Secreted, signal peptide Cellular Component: proteinaceous extracellular matrix; extracellular space; cell surface; microvillus; cell soma; cell; axon; cytoplasm; extracellular region; nucleus; secretory granule 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; transforming growth factor beta receptor binding Biological Process: positive regulation of apoptosis; positive regulation of transcription, DNA-dependent; 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; regulation of transforming growth factor beta receptor signaling pathway; negative regulation of ossification; cell cycle arrest; positive regulation of isotype switching to IgA isotypes; T cell differentiation; regulatory T cell differentiation; positive regulation of interleukin-17 production; regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; positive regulation of smooth muscle cell differentiation; positive regulation of chemotaxis; negative regulation of immune response; 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 cell division; regulation of MAPKKK cascade; 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; T cell activation; wound healing; positive regulation of cellular protein metabolic process; myeloid dendritic cell differentiation; negative regulation of transcription from RNA polymerase II promoter; phosphate metabolic process; response to organic substance; negative regulation of cell proliferation; CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment; negative regulation of T cell proliferation; mammary gland development; regulation of DNA binding; negative regulation of release of sequestered calcium ion into cytosol; positive regulation of cell proliferation; protein kinase B signaling cascade; protein export from nucleus; inflammatory response; 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 peptidyl-serine phosphorylation; SMAD protein complex assembly; regulation of cell proliferation; positive regulation of protein kinase B signaling cascade; cell proliferation; positive regulation of protein complex assembly; negative regulation of interleukin-17 production; positive regulation of protein import into nucleus; epithelial to mesenchymal transition; negative regulation of cell growth; negative regulation of cell-cell adhesion; negative regulation of skeletal muscle development; mononuclear cell proliferation; protein amino acid phosphorylation; hyaluronan catabolic process; regulation of apoptosis; negative regulation of neuroblast proliferation; transforming growth factor beta receptor signaling pathway; receptor catabolic process; positive regulation of superoxide release; germ cell migration; chondrocyte differentiation; defense response to fungus, incompatible interaction; T cell homeostasis; negative regulation of mitotic cell cycle; cell growth; tolerance induction to self antigen; regulation of striated muscle development; organ regeneration; skeletal muscle development; cell activation; organ morphogenesis; negative regulation of DNA replication; hemopoietic progenitor cell differentiation; negative regulation of transcription, DNA-dependent; positive regulation of epithelial cell proliferation; positive regulation of collagen biosynthetic process; defense response; response to estradiol stimulus; negative regulation of cell cycle; regulation of interleukin-23 production; positive regulation of histone deacetylation; negative regulation of protein amino acid phosphorylation; lipopolysaccharide-mediated signaling pathway; adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains; skeletal development; negative regulation of epithelial cell proliferation; intercellular junction assembly and maintenance; regulation of binding; MAPKKK cascade; morphogenesis of a branching structure; cellular calcium ion homeostasis; protein import into nucleus, translocation; ATP biosynthetic process; positive regulation of histone acetylation; positive regulation of protein amino acid phosphorylation; negative regulation of myoblast differentiation; negative regulation of T cell activation; growth; positive regulation of cell migration |
| UniProt Code: | P04202 |
| NCBI GenInfo Identifier: | 135675 |
| NCBI Gene ID: | 21803 |
| NCBI Accession: | P04202.1 |
| UniProt Related Accession: | P04202 |
| Molecular Weight: | 44,310 Da |
| NCBI Full Name: | Transforming growth factor beta-1 |
| NCBI Synonym Full Names: | transforming growth factor, beta 1 |
| NCBI Official Symbol: | Tgfb1�� |
| NCBI Official Synonym Symbols: | Tgfb; Tgfb-1; TGFbeta1; TGF-beta1�� |
| NCBI Protein Information: | transforming growth factor beta-1; TGF-beta 1; TGF-beta-1; regulatory protein; transforming growth factor-beta 1 |
| UniProt Protein Name: | Transforming growth factor beta-1 |
| UniProt Synonym Protein Names: | |
| Protein Family: | Transforming growth factor |
| UniProt Gene Name: | Tgfb1�� |
| UniProt Entry Name: | TGFB1_MOUSE |
