You Searched For: Enzo Life Sciences

Catalog Number: (CA200062-960)

Supplier: Enzo Life Sciences

Description: Membrin, also known as GS27 (Golgi SNARE of 27K), is an integral membrane protein present on the surface of the Golgi apparatus. GS27 is a member of a protein complex that consists of cis-Golgi vesicle receptor syntaxin 5 and GS28, v-SNARE rbet1 and Rsec22, and Rsly1. These complexes are postulated to direct the fusion of ER-derived vesicles with vesicular tubular cluster (VTC), and the fusion of VTCs to form cis-Golgi compartment.

Supplier: Enzo Life Sciences

Description: GC UNC45 (general cell UNC45/unc45a) is an Hsp90 co-chaperone that has been shown to play a critical role in the chaperoning of myosin proteins as well as the progesterone receptor (PR). There are two known vertebrate isoforms of UNC45 that are functional orthologs of the C. elegans unc-45, an important protein in the development of organized body wall muscles. The vertebrate general cell form (GC UNC45/unc45a) is ubiquitously expressed, while the striated muscle-specific isoform (SM UNC45/unc45b) is found in cardiac and skeletal muscle. In vitro, GC UNC45 preferentially binds the Hsp90 beta isoform, and is specifically required for proper cellular distribution of Hsp90β but not Hsp90α.

Catalog Number: (CA200062-116)

Supplier: Enzo Life Sciences

Description: Protein Kinase C (PKC) is a large superfamily of serine/threonine kinases that mediate essential cellular signals required for activation, proliferation, differentiation and survival. There are at least ten PKC isotypes that are closely related in structure but that have distinct patterns of tissue distribution and function. The PKC isotypes can be subdivided into three classes based on primary structure and biochemical properties. These are: classical or conventional PKC isotypes (cPKC), novel PKC isotypes (nPKC) and atypical PKC isotypes (aPKC).

Catalog Number: (CA95046-132)

Supplier: Enzo Life Sciences

Description: Anti-HSP47 Mouse Monoclonal Antibody [clone: M16.10A1]

Supplier: Enzo Life Sciences

Description: HSFs (Heat Shock family of transcription factors), which consists of HSF 1-4, bind to highly conserved Heat shock elements (HSEs) in the promoter regions of heat shock genes, ultimately regulating the expression of Heat shock proteins (Hsps). On exposure to heat shock and other stresses, HSF1 localizes within seconds to discrete nuclear granules and on recovery from stress, HSF1 rapidly dissipates from the stress granules to a diffuse nucleoplasmic distribution.

Supplier: Enzo Life Sciences

Description: The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Catalog Number: (CA200062-834)

Supplier: Enzo Life Sciences

Description: Grp75 (Glucose regulated 75 kDa protein) is a member of the Hsp70 family. It is localized in the mitochondrial matrix, where, in concert with Hsp60, is thought to participate in the re-folding of proteins translocated into this organelle. Like its E. coli homolog DnaK, Grp75 possesses a cation-dependent ATPase activity thought to be central to its function as a chaperone.

Supplier: Enzo Life Sciences

Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Supplier: Enzo Life Sciences

Description: The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Supplier: Enzo Life Sciences

Description: The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Supplier: Enzo Life Sciences

Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Supplier: Enzo Life Sciences

Description: HSFs (Heat Shock family of transcription factors), which consists of HSF 1-4, bind to highly conserved Heat shock elements (HSEs) in the promoter regions of heat shock genes, ultimately regulating the expression of Heat shock proteins (Hsps). On exposure to heat shock and other stresses, HSF1 localizes within seconds to discrete nuclear granules and on recovery from stress, HSF1 rapidly dissipates from the stress granules to a diffuse nucleoplasmic distribution.

SDS

Catalog Number: (CA200063-318)

Supplier: Enzo Life Sciences

Description: Synapsin I, II and III belong to a family of neuron-specific phosphoproteins which maintain a reserve pool of vesicles in the vicinity of the active zone by tethering synaptic vesicles to each other and to an Actin-based cytoskeleton meshwork. They have been shown to regulate neurotransmitter release in mature synapses and to accelerate development of the nervous system.

Supplier: Enzo Life Sciences

Description: CaMKII (calmodulin-dependent kinase II) is an enzyme which is activated by increases in intracellular Ca2+ ion concentration and it has been proposed to be pivotal in regulating synaptic strength and maturation of synapses during development.  This process is thought to be critical in memory and learning and in establishing the specificity of synaptic connections. There are over two dozen alternative splice variants of CaMKII which are encoded by four genes, a, b, g, and d with apparent molecular masses of 50-60 kDa.  CaMKII is widely distributed in many tissues, but is highly expressed in brain. Several studies demonstrate that CaMKII is a multifunctional enzyme which modulates the synaptic strength by binding to a subunit of NMDA receptors and promoting the phosphorylation of this NMDA receptor subunit.  CaMKII also regulates DLG localization at synapses by co-localization with DLG in the same protein complex.  Experimental data suggest that CaMKII is critically involved in the development of morphine tolerance as well as dependence and inhibition of this enzyme may have some therapeutic benefit in the treatment of opiate tolerance and dependence.  It also has been demonstrated that d CaMKII isozyme is down-regulated in human tumor cells indicating a role for d CaMKII isozymes in cellular differentiation.  Changes in d CaMKII isozyme expression pattern in human hearts during heart failure suggest that CaMKII is important for regulation of heart function.  This immunoaffinity purified antibody detects proteins of 50-60 kDa, corresponding to apparent molecular mass of CaMKII isoforms on SDS-PAGE immunoblots, in samples from human, mouse, rat, bovine, hamster, guinea pig, chicken and rabbit origins. Recombinant rat calmodulin-dependent protein kinase II a subunits expressed in sf9 insect cells are also detected. As the sequences of the rat a, d, and g isoforms are conserved over this amino terminus region, this antibody is expected to recognize the d, g and a isoforms. This antibody is not expected to cross-react with the b isoform. Proteins of unknown identity, ~40, 45 and 90 kDa, may be detected on immunoblot analysis with some lysates.

SDS

Supplier: Enzo Life Sciences

Description: Calcineurin is a Ca2+/Calmodulin-dependent serine/threonine protein phosphatase. The active enzyme is a heterodimer consisting of a catalytic A subunit and a myristylated regulatory B subunit that binds calcium. Calcineurin, which is the target of immunosuppressant drugs such as cyclosporin A and FK506, controls the translocation of Nuclear factors of activated T-cells (NFAT), a family of transcriptional activators that control the expression of cytokine genes essential to immune response, from the cytosol into the nucleus of activated T-cells.

SDS

Catalog Number: (CA200061-466)

Supplier: Enzo Life Sciences

Description: Anthrax Lethal Factor (LF) is a zinc-dependent protease that cleaves mitogen-activated protein kinase kinase (MAPKK) and causes lysis of macrophages. LF, together with Protective Antigen, forms Lethal Toxin, which is the dominant virulence factor produced by B. anthracis and is the major cause of death in infected animals. Lethal toxin has been reported to trigger apoptosis in human melanoma cells.