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Leverandør: Biotium
Beskrivelse: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Leverandør: Biotium
Beskrivelse: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Leverandør: Biotium
Beskrivelse: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Varenummer: (BOSSBS-13202R)
Leverandør: Bioss
Beskrivelse: Xenopus winged-helix factor, xFAST-1 (forkhead activin signal transducer-1) is a transcription factor that forms a complex with the receptor-regulated Smad protein, Smad2, and directly binds to activin response elements on DNA (1,2). The human homolog FAST-1 and the corresponding mouse homolog, designated FAST-2, share significant sequence homology with xFAST-1, including a conserved N-terminal forkhead domain that consists of 110 amino acid residues and is essential for binding DNA and regulating transcription in embryogenesis, in tumorigenesis and in the maintenance of differentiated cell states (3,4). FAST-1 and FAST-2 also contain a distinct C-terminal Smad interaction domain that is required for the association with various Smad proteins, including Smad2, Smad3 and Smad4 (3,5). Expression of FAST-1 and FAST-2 is predominantly observed during early development, with lower levels detected in adult tissues (6,7). FAST-1 and FAST-2 mediated DNA binding is attenuated by both TFGß and activin, indicating that these FAST proteins mediate TFGß induced signal transduction (3).
UOM: 1 * 100 µl


Leverandør: Biotium
Beskrivelse: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Leverandør: Biotium
Beskrivelse: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Varenummer: (BOSSBS-9854R-A680)
Leverandør: Bioss
Beskrivelse: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl


Varenummer: (BOSSBS-9430R-A555)
Leverandør: Bioss
Beskrivelse: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl


Varenummer: (BOSSBS-9430R-A680)
Leverandør: Bioss
Beskrivelse: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl


Varenummer: (BOSSBS-9430R-FITC)
Leverandør: Bioss
Beskrivelse: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl


Varenummer: (BOSSBS-9854R-A750)
Leverandør: Bioss
Beskrivelse: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl


Varenummer: (BOSSBS-13202R-CY3)
Leverandør: Bioss
Beskrivelse: Xenopus winged-helix factor, xFAST-1 (forkhead activin signal transducer-1) is a transcription factor that forms a complex with the receptor-regulated Smad protein, Smad2, and directly binds to activin response elements on DNA (1,2). The human homolog FAST-1 and the corresponding mouse homolog, designated FAST-2, share significant sequence homology with xFAST-1, including a conserved N-terminal forkhead domain that consists of 110 amino acid residues and is essential for binding DNA and regulating transcription in embryogenesis, in tumorigenesis and in the maintenance of differentiated cell states (3,4). FAST-1 and FAST-2 also contain a distinct C-terminal Smad interaction domain that is required for the association with various Smad proteins, including Smad2, Smad3 and Smad4 (3,5). Expression of FAST-1 and FAST-2 is predominantly observed during early development, with lower levels detected in adult tissues (6,7). FAST-1 and FAST-2 mediated DNA binding is attenuated by both TFGß and activin, indicating that these FAST proteins mediate TFGß induced signal transduction (3).
UOM: 1 * 100 µl


Varenummer: (BOSSBS-13202R-CY7)
Leverandør: Bioss
Beskrivelse: Xenopus winged-helix factor, xFAST-1 (forkhead activin signal transducer-1) is a transcription factor that forms a complex with the receptor-regulated Smad protein, Smad2, and directly binds to activin response elements on DNA (1,2). The human homolog FAST-1 and the corresponding mouse homolog, designated FAST-2, share significant sequence homology with xFAST-1, including a conserved N-terminal forkhead domain that consists of 110 amino acid residues and is essential for binding DNA and regulating transcription in embryogenesis, in tumorigenesis and in the maintenance of differentiated cell states (3,4). FAST-1 and FAST-2 also contain a distinct C-terminal Smad interaction domain that is required for the association with various Smad proteins, including Smad2, Smad3 and Smad4 (3,5). Expression of FAST-1 and FAST-2 is predominantly observed during early development, with lower levels detected in adult tissues (6,7). FAST-1 and FAST-2 mediated DNA binding is attenuated by both TFGß and activin, indicating that these FAST proteins mediate TFGß induced signal transduction (3).
UOM: 1 * 100 µl


Varenummer: (BOSSBS-13202R-HRP)
Leverandør: Bioss
Beskrivelse: Xenopus winged-helix factor, xFAST-1 (forkhead activin signal transducer-1) is a transcription factor that forms a complex with the receptor-regulated Smad protein, Smad2, and directly binds to activin response elements on DNA (1,2). The human homolog FAST-1 and the corresponding mouse homolog, designated FAST-2, share significant sequence homology with xFAST-1, including a conserved N-terminal forkhead domain that consists of 110 amino acid residues and is essential for binding DNA and regulating transcription in embryogenesis, in tumorigenesis and in the maintenance of differentiated cell states (3,4). FAST-1 and FAST-2 also contain a distinct C-terminal Smad interaction domain that is required for the association with various Smad proteins, including Smad2, Smad3 and Smad4 (3,5). Expression of FAST-1 and FAST-2 is predominantly observed during early development, with lower levels detected in adult tissues (6,7). FAST-1 and FAST-2 mediated DNA binding is attenuated by both TFGß and activin, indicating that these FAST proteins mediate TFGß induced signal transduction (3).
UOM: 1 * 100 µl


Varenummer: (BOSSBS-13202R-A350)
Leverandør: Bioss
Beskrivelse: Xenopus winged-helix factor, xFAST-1 (forkhead activin signal transducer-1) is a transcription factor that forms a complex with the receptor-regulated Smad protein, Smad2, and directly binds to activin response elements on DNA (1,2). The human homolog FAST-1 and the corresponding mouse homolog, designated FAST-2, share significant sequence homology with xFAST-1, including a conserved N-terminal forkhead domain that consists of 110 amino acid residues and is essential for binding DNA and regulating transcription in embryogenesis, in tumorigenesis and in the maintenance of differentiated cell states (3,4). FAST-1 and FAST-2 also contain a distinct C-terminal Smad interaction domain that is required for the association with various Smad proteins, including Smad2, Smad3 and Smad4 (3,5). Expression of FAST-1 and FAST-2 is predominantly observed during early development, with lower levels detected in adult tissues (6,7). FAST-1 and FAST-2 mediated DNA binding is attenuated by both TFGß and activin, indicating that these FAST proteins mediate TFGß induced signal transduction (3).
UOM: 1 * 100 µl


Varenummer: (BOSSBS-13202R-CY5)
Leverandør: Bioss
Beskrivelse: Xenopus winged-helix factor, xFAST-1 (forkhead activin signal transducer-1) is a transcription factor that forms a complex with the receptor-regulated Smad protein, Smad2, and directly binds to activin response elements on DNA (1,2). The human homolog FAST-1 and the corresponding mouse homolog, designated FAST-2, share significant sequence homology with xFAST-1, including a conserved N-terminal forkhead domain that consists of 110 amino acid residues and is essential for binding DNA and regulating transcription in embryogenesis, in tumorigenesis and in the maintenance of differentiated cell states (3,4). FAST-1 and FAST-2 also contain a distinct C-terminal Smad interaction domain that is required for the association with various Smad proteins, including Smad2, Smad3 and Smad4 (3,5). Expression of FAST-1 and FAST-2 is predominantly observed during early development, with lower levels detected in adult tissues (6,7). FAST-1 and FAST-2 mediated DNA binding is attenuated by both TFGß and activin, indicating that these FAST proteins mediate TFGß induced signal transduction (3).
UOM: 1 * 100 µl


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