Other Proteins

Recombinant Human Sox2 (Legacy Tebubio ref. 167110-03). Sox2 belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and the determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development, including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4 into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the

Recombinant Human Sox2-TAT (Legacy Tebubio ref. 167110-03T). Sox2 belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and the determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development, including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4 into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and i

Recombinant Human Sox2-TAT (Legacy Tebubio ref. 167110-03T). Sox2 belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and the determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development, including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4 into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and i

Recombinant Human Lin28-TAT (Legacy Tebubio ref. 167110-06). Lin28 is a RNA-binding protein that belongs to a diverse family of structurally-related transcription factors. Lin28 is found abundantly in embryonic stem cells (ESCs), and to a lesser extent in placenta and testis. Lin28 has been shown to block let-7 microRNA processing and maturation, a necessary step in the differentiation of stem cells and certain cancer cell lines. Together with Sox2, Oct4, and Nanog, Lin28 can induce the reprogramming of primary human fibroblasts to a pluripotent state. Lin28 and other regulatory proteins can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing proteins into primary, as well as transformed, cells. Recombinant Human Lin28-TAT is a 24.4 kDa protein containing 222 amino acid residues, including a 13-residue C-terminal TAT peptide.

Recombinant Human Lin28-TAT (Legacy Tebubio ref. 167110-06). Lin28 is a RNA-binding protein that belongs to a diverse family of structurally-related transcription factors. Lin28 is found abundantly in embryonic stem cells (ESCs), and to a lesser extent in placenta and testis. Lin28 has been shown to block let-7 microRNA processing and maturation, a necessary step in the differentiation of stem cells and certain cancer cell lines. Together with Sox2, Oct4, and Nanog, Lin28 can induce the reprogramming of primary human fibroblasts to a pluripotent state. Lin28 and other regulatory proteins can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing proteins into primary, as well as transformed, cells. Recombinant Human Lin28-TAT is a 24.4 kDa protein containing 222 amino acid residues, including a 13-residue C-terminal TAT peptide.

Recombinant Human KLF4-TAT (Legacy Tebubio ref. 167110-08). KLF4 is a member of the Kruppel-like factor (KLF) family of zinc finger transcription factors. Members of this family share 3 contiguous C2H2-type zinc fingers at the carboxyl terminus that comprise the DNA-binding domain. KLF4 is highly expressed in skin and gut epithelial tissues, but is also found in various other cells and tissues, including vascular endothelial cells, lymphocytes, lung, and testis. It is an important regulator of the cell cycle, transcription, and cell differentiation. Together with Sox2, Oct4, and cMyc, KLF4 can induce the reprogramming of primary human fibroblasts to a pluripotent state. KLF4 and other transcription factors can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors into primary, as well as transformed, cells. Recombinant Human KLF4-TAT is

Recombinant Human KLF4-TAT (Legacy Tebubio ref. 167110-08). KLF4 is a member of the Kruppel-like factor (KLF) family of zinc finger transcription factors. Members of this family share 3 contiguous C2H2-type zinc fingers at the carboxyl terminus that comprise the DNA-binding domain. KLF4 is highly expressed in skin and gut epithelial tissues, but is also found in various other cells and tissues, including vascular endothelial cells, lymphocytes, lung, and testis. It is an important regulator of the cell cycle, transcription, and cell differentiation. Together with Sox2, Oct4, and cMyc, KLF4 can induce the reprogramming of primary human fibroblasts to a pluripotent state. KLF4 and other transcription factors can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors into primary, as well as transformed, cells. Recombinant Human KLF4-TAT is

Recombinant Human Vimentin (Legacy Tebubio ref. 167110-10). Vimentin is a class III intermediate filament protein predominantly found in cells of mesenchymal origins, such as vascular endothelium and blood cells, where it functions as a major cytoskeletal component. Due to its importance and abundance in the cytoskeletal structure of mesenchymally-derived cells, vimentin is frequently used as a developmental marker within cells of mesenchymal origin or cells undergoing epithelial-mesenchymal transition, which can occur during both normal and metastatic growth. An active participant within several critical processes of cellular organization and protein regulation, vimentin is involved in the anchorage of organelles within the cytoplasmic matrix, development of astrocytes, and the disassembly of cellular components during the execution phase of apoptosis. Abnormalities in the normal physiological pathways of vimentin have been implicated in deficient motility and directional migration in

Recombinant Human Vimentin (Legacy Tebubio ref. 167110-10). Vimentin is a class III intermediate filament protein predominantly found in cells of mesenchymal origins, such as vascular endothelium and blood cells, where it functions as a major cytoskeletal component. Due to its importance and abundance in the cytoskeletal structure of mesenchymally-derived cells, vimentin is frequently used as a developmental marker within cells of mesenchymal origin or cells undergoing epithelial-mesenchymal transition, which can occur during both normal and metastatic growth. An active participant within several critical processes of cellular organization and protein regulation, vimentin is involved in the anchorage of organelles within the cytoplasmic matrix, development of astrocytes, and the disassembly of cellular components during the execution phase of apoptosis. Abnormalities in the normal physiological pathways of vimentin have been implicated in deficient motility and directional migration in