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Image Unavailable-89359-612

Anti-HO-1 Mouse Monoclonal Antibody [clone: HO-1-1]

Catalog Number: (89359-612)
Supplier: Genetex
Description: Heme oxygenase (HO) is a microsomal enzyme that catalyzes the oxidation of heme to the antioxidant molecules, biliverdin and carbon monoxide. HO consists of two homologous isozymes, an inducible HO1 and a constitutively expressed HO2. HO1 is induced by a wide variety of stimuli including conditions of oxidative stress, inflammatory agents, transforming growth factor beta and heat shock. The increase in expression of HO1 is thought to be a cellular defense mechanism against oxidative stress since elevated HO could eventually generate more bilirubin, an anti-oxidant.
Image Unavailable-75953-460

Anti-HSPD1 Mouse Monoclonal Antibody (CF488A) [clone: HSPD1/780]

Supplier: Biotium
Description: This antibody recognizes a 60 kDa protein, identified as the heat shock protein 60 (hsp60). A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (HSPs), more appropriately called as stress response proteins (SRPs). Hsp60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial hsp60, but also against its mammalian homolog.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®488A is a green fluorescent dye (Ex/Em 490/515 nm) with excellent brightness and photostability. The dye is minimally charged for less non-specific binding. CF®488A also is compatible with super-resolution imaging by TIRF.

Image Unavailable-10240-676

Anti-HSPB1 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Catalog Number: (10240-676)
Supplier: Bioss
Description: Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
Image Unavailable-75930-712

Anti-TP53INP1 Rabbit Polyclonal Antibody

Catalog Number: (75930-712)
Supplier: Rockland Immunochemical
Description: p53DINP1 antibody detects human p53DINP1. Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible gene was identified recently and designated p53DINP1 (for p53-dependent damage-inducible nuclear protein 1) and SIP (for stress induced protein) in human and mouse. A p53DINP1 antisense oligonucleotide inhibits and overexpression of p53DINP1 enhances Ser46 phosphorylation of p53, induction of p53AIP1, and cell death induced by DNA double-strand breaks. p53DINP1 may regulate p53-dependent apoptosis through phosphorylation at Ser46 and induction of p53AIP1. The p53DINP1/SIP gene encodes two proteins of 27 and 18 kDa in human and mouse termed p53DINP1-alpha and p53DINP1-beta or SIP27 and SIP18. p53DINP1/SIP is expressed in many tissues and induced by a variety of stress agents including UV stress, mutagenic stress, heat shock, and oxidative stress. Anti-p53DINP1 antibodies are ideal for investigators involved in Apoptosis and Cancer research.
Image Unavailable-75951-608

Anti-HSPD1 Mouse Monoclonal Antibody (CF594) [clone: HSPD1/780]

Supplier: Biotium
Description: This antibody recognizes a 60 kDa protein, identified as the heat shock protein 60 (hsp60). A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (HSPs), more appropriately called as stress response proteins (SRPs). Hsp60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial hsp60, but also against its mammalian homolog.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®594 is a deep red fluorescent dye (Ex/Em 593/614 nm). It yields the brightest conjugates among spectrally similar dyes, and has excellent photostability.

Image Unavailable-10240-668

Anti-HSPB1 Rabbit Polyclonal Antibody (Cy5®)

Catalog Number: (10240-668)
Supplier: Bioss
Description: Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
Image Unavailable-10240-674

Anti-HSPB1 Rabbit Polyclonal Antibody (FITC (Fluorescein Isothiocyanate))

Catalog Number: (10240-674)
Supplier: Bioss
Description: Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
Image Unavailable-10240-672

Anti-HSPB1 Rabbit Polyclonal Antibody (Cy7®)

Catalog Number: (10240-672)
Supplier: Bioss
Description: Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
Image Unavailable-10449-362

Anti-HSPA6 Rabbit Polyclonal Antibody (Cy5®)

Catalog Number: (10449-362)
Supplier: Bioss
Description: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Sequence similarities Belongs to the heat shock protein 70 family.
Image Unavailable-10240-670

Anti-HSPB1 Rabbit Polyclonal Antibody (Cy5.5®)

Catalog Number: (10240-670)
Supplier: Bioss
Description: Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
Image Unavailable-10449-348

Anti-HSPA6 Rabbit Polyclonal Antibody

Catalog Number: (10449-348)
Supplier: Bioss
Description: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Sequence similarities Belongs to the heat shock protein 70 family.
Image Unavailable-10449-360

Anti-HSPA6 Rabbit Polyclonal Antibody (Cy3®)

Catalog Number: (10449-360)
Supplier: Bioss
Description: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Sequence similarities Belongs to the heat shock protein 70 family.
Image Unavailable-75928-588

Anti-Hsf1 Rat Monoclonal Antibody (FITC) [Clone: 4B4]

Catalog Number: (75928-588)
Supplier: Rockland Immunochemical
Description: HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function (2). The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF) (3, 4, 5). Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization (6). There are two main heat shock factors, 1 and 2. Mouse HSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form (7, 8). Various experiments have suggested that HFS2 may have roles in differentiation and development (9, 10, 11). Anti-HSF1 Antibody is ideal for research in Genetics, Transcription, Cell Signaling and pathways including ERK and MAPK.
Image Unavailable-75928-598

Anti-Hsf1 Rat Monoclonal Antibody (HRP) [Clone: 10H4]

Catalog Number: (75928-598)
Supplier: Rockland Immunochemical
Description: HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function (2). The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF) (3, 4, 5). Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization (6). There are two main heat shock factors, 1 and 2. Mouse HSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form (7, 8). Various experiments have suggested that HFS2 may have roles in differentiation and development (9, 10, 11). Anti-HSF1 Antibody is ideal for research in Genetics, Transcription, Cell Signaling and pathways including ERK and MAPK.
Image Unavailable-75928-582

Anti-Hsf1 Rat Monoclonal Antibody (BAC) [Clone: 10H4]

Catalog Number: (75928-582)
Supplier: Rockland Immunochemical
Description: HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function (2). The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF) (3, 4, 5). Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization (6). There are two main heat shock factors, 1 and 2. Mouse HSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form (7, 8). Various experiments have suggested that HFS2 may have roles in differentiation and development (9, 10, 11). Anti-HSF1 Antibody is ideal for research in Genetics, Transcription, Cell Signaling and pathways including ERK and MAPK.
Image Unavailable-75928-548

Anti-Hsf1 Rat Monoclonal Antibody [Clone: 4B4]

Catalog Number: (75928-548)
Supplier: Rockland Immunochemical
Description: HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function (2). The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF) (3, 4, 5). Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization (6). There are two main heat shock factors, 1 and 2. Mouse HSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form (7, 8). Various experiments have suggested that HFS2 may have roles in differentiation and development (9, 10, 11). Anti-HSF1 Antibody is ideal for research in Genetics, Transcription, Cell Signaling and pathways including ERK and MAPK.
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