You Searched For: ENZO LIFE SCIENCES

Supplier: ENZO LIFE SCIENCES

Description: Nuclear factor kappa-B (NFk) B) functions as a sequence specific transcriptional activator that binds to the intronic enhancer of kappa light chain gene in B lymphocytes. NF-kB is a heterodimer consisting of a 50 kDa DNA binding subunit (p50) and a 65 kDa transactivation subunit (p65/RelA) (ref. 3), both of which exhibit sequence homology to the protooncogene c-Rel. p50 has an isoform called p49/p52, and both proteins derive from the amino-terminal of precursor protein p105 and p100, respectively. The p50/p65 heterodimer remains in inactive form in the cytosol as a complex with its inhibitor, IkB. Upon stimulation of cells by a variety of stimuli, including lipopolysaccharide (LPS), pro-inflammatory cytokines like interleukin-1 and tumor necrosis factor, and viral infection, IkB becomes phosphorylated and degraded by the proteosome. The active NF-kB heterodimer translocates into the nucleus and induces gene expression.

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Supplier: ENZO LIFE SCIENCES

Description: Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

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Catalog Number: (ENZOADINBA202200)

Supplier: ENZO LIFE SCIENCES

Description: Anti-SMN1 Mouse Monoclonal Antibody [clone: 2B1]

UOM: 1 * 200 µG

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Catalog Number: (ENZOADIMSA150E)

Supplier: ENZO LIFE SCIENCES

Description: Thioredoxins act as antioxidants by reducing the proteins by cysteine thiol-disulfide exchange. Several plasmid expression vectors have been constructed that direct the synthesis of foreign polypeptides in E. coli as fusions with C-terminal Thioredoxin (TrxA) to offer soluble expression of normally insoluble or difficult to express proteins such as cytokines and growth factors.

UOM: 1 * 100 µG

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Catalog Number: (ENZOADIKASMA013E)

Supplier: ENZO LIFE SCIENCES

Description: MEKKs (Mitogen activated protein kinase kinase kinases) are serine-threonine kinases that act as the first tier of cellular MAP kinase pathways by activation of MAP/ERK kinases, or MEKs. Many enzymes with MEKK activity have been identified, including MEKK1-4, Raf, MLK3, TAK, and DLK. MEKKs generally display little similarity outside of their catalytic kinase domains. MEKK1-4 are nearly 50% identical within their catalytic domains, and are known to regulate Erk, Jnk, and p38 MAP kinase pathways. MEKK2 and MEKK3 bind MEK5 via conserved PB1 domains, leading to downstream activation of Erk5.

UOM: 1 * 100 µl

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Supplier: ENZO LIFE SCIENCES

Description: Hsp60 is a member of the chaperonin family of heat shock proteins, with homologs functioning in the cytosol and mitochondria to fold nascent and aggregated proteins. Hsp60 is the eukaryotic homolog of the E. coli GroEL protein, and forms a multimeric complex in the mitochondria with Hsp10 (Cpn10) to form a large central cavity in which ATP-dependent protein folding takes place. TRiC/CCT, a eukaryotic relative of Hsp60, is expressed in the cytosol and participates in the folding of actin and tubulin substrates, but lacks any association with an Hsp10-like co-factor.

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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.

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Supplier: ENZO LIFE SCIENCES

Description: The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible Hsp90 alpha and constitutive Hsp90 beta isoforms that are encoded by separate genes. The amino acid sequences of human and yeast Hsp90 alpha are 85% and 90% homologous to those of Hsp90 beta, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular protein in most cells. Hsp90 functions as part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers.

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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.

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Catalog Number: (ENZOADISPA885J)

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.

UOM: 1 * 1 mg

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Supplier: ENZO LIFE SCIENCES

Description: Hsp65 is a member of the Hsp60 family of heat shock proteins isolated from Mycobacterium bovis BCG. Hsp65 from M. bovis is identical to that of M. tuberculosis, and similar to that of M. leprae, two highly pathogenic strains of mycobacterium. Hsp65 is the immunodominant antigen during mycobacterial infection and vaccination, and has been linked to the development of autoimmune adjuvant arthritis in rats.

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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.

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Supplier: ENZO LIFE SCIENCES

Description: The mammalian PDI (Protein disulfide-isomerase) family encompasses several highly divergent proteins which are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum by catalyzing the rearrangement of disulfide bonds.

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Supplier: ENZO LIFE SCIENCES

Description: Produced in <i>E. coli</i>. Human αB-Crystallin is fused at the N-terminus to a His-tag.

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Catalog Number: (ENZOADI801339)

Supplier: ENZO LIFE SCIENCES

Description: Cell lysis buffer 4, Enzo Life Sciences

UOM: 1 * 100 mL

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Catalog Number: (ENZOADI900002)

Supplier: ENZO LIFE SCIENCES

Description: For the quantitative determination of TXB2 in culture supernatants, plasma, serum, saliva, and urine from any species. Cited sample types include cell lysate, coronary effluent, liver perfusate, platelets, rectal dialysate, and whole blood.

UOM: 1 * 1 KIT

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