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ENZO LIFE SCIENCES
Fournisseur:
ENZO LIFE SCIENCES
Description:
Potent and selective inhibitor of heme oxygenase (Ki=3nM), the enzyme that generates carbon monoxide (CO). Inhibits soluble guanylyl cyclase. Produces a time- and concentration-dependent inactivation of all three isoforms of nitric oxide synthase (IC50=0.8µM, 4.0µM, and 5.0µM for nNOS (NOS I), iNOS (NOS II) and eNOS (NOS III), respectively). Does not cross the blood-brain barrier. An useful tool to elucidate the role of CO in signal transduction and as a neurotransmitter.
Fournisseur:
ENZO LIFE SCIENCES
Description:
Nitric oxide donor
Numéro de catalogue:
(ENZOALX430004M010)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Nitric oxide donor
UOM:
1 * 10 mg
New Product
Numéro de catalogue:
(ENZOADI905770100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
The DNA damage checkpoint is a signal transduction pathway that has the ability to delay entry into mitosis. When DNA is damaged, the Check point kinases (CHKs) are known to act downstream of ATM to elicit appropriate responses such as cell cycle arrest. Chk1, for instance, is activated by ATM phosphorylation of serines 123, 178, 278, and 292 of the S phase-promoting cdc25A phosphatase and accelerates IR (ionizing radiation)induced degradation of cdc25A.
UOM:
1 * 1 EA
New Product
Numéro de catalogue:
(ENZOADI905765100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
The mTOR (mammalian target of rapamycin) pathway coordinates nutrient signals with growth factor dependent signaling. mTOR is organized in two independent protein complexes, mTORC1 and mTORC2. The mTORC1 complex containing mTOR, GβL/mLST8 and Raptor is sensitive to rapamycin, while the mTORC2 complex containing mTOR, GβL/mLST8, SIN1, and Rictor is rapamycin insensitive.
UOM:
1 * 1 EA
New Product
Numéro de catalogue:
(ENZOENZC34935)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Host: Mouse, Isotype: IgM
UOM:
1 * 0,5 mL
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
Potent inhibitor of Akt1, Akt2 and Akt3 activity.
Numéro de catalogue:
(ENZOENZC34931)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Host: Mouse, Isotype: IgG1
UOM:
1 * 0,5 mL
New Product
Numéro de catalogue:
(ENZOENZCHM1050005)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Streptogramin antibiotic
UOM:
1 * 5 mg
New Product
Numéro de catalogue:
(ENZOENZCHM1210005)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Cell permeable MIF antagonist with anti-inflammatory properties.
UOM:
1 * 5 mg
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
Cell-permeable, potent and AMP-competitive inhibitor of glycogen phosphorylase.
Fournisseur:
ENZO LIFE SCIENCES
Description:
Adenosine-5'-diphosphate monopotassium salt ≥87%
Numéro de catalogue:
(ENZOALX460003G010)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Precursor for coenzyme A biosynthesis.
UOM:
1 * 10 g
New Product
Fournisseur:
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.
Fournisseur:
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.
Numéro de catalogue:
(ENZOADISPA8136D)
Fournisseur:
ENZO LIFE SCIENCES
Description:
The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.
UOM:
1 * 50 µG
New Product
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