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ENZO LIFE SCIENCES
Numéro de catalogue:
(ENZOENZ42506)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Cyanine 5-UTP (Enhanced) can replace UTP as a substrate for T7 RNA polymerase in labeling systems that generate labeled probes through in vitro transcription. Probes generated by these methods are suitable for multicolor fluorescence analysis, specifically dual-color expression arrays in conjunction with cyanine 3-UTP.
UOM:
1 * 250 Nmo
New Product
Numéro de catalogue:
(ENZOENZ42809)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Bio-N⁶-ddATP (Biotin-N⁶-(2’,3’-dideoxy)adenosine-5’ triphosphate) can be used for 3’-end labelling of single-stranded or double-stranded DNA. It is especially useful as a substrate for terminal transferase for the 3’-terminal addition of a single Bio-N⁶-ddAMP. It is also a substrate for Taq DNA Polymerase and other DNA polymerases.
UOM:
1 * 25 Nmo
New Product
Numéro de catalogue:
(ENZOENZ52253)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Neuronal detection
UOM:
1 * 10 mg
New Product
Numéro de catalogue:
(ENZOENZ52303)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Mitochondria dye
UOM:
1 * 100 mg
New Product
Numéro de catalogue:
(ENZOALX200606M001)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Purified from human brain by method of Määttä <i>et al..</i>
UOM:
1 * 1 mg
New Product
Numéro de catalogue:
(ENZOALX850249KI01)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Kit utilises Live-dye™, a cell permeable green fluorescent dye (Ex(max): 488 nm; Em(max): 518 nm), to stain live cells. Dead cells can be easily stained by propidium iodide (PI), a red fluorescent dye (Ex(max): 488 nm; Em(max): 615 nm), which in viable cells is actively pumped out of the cytoplasm.
UOM:
1 * 1 KIT
New Product
Numéro de catalogue:
(ENZOBMLNA1410010)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Na+ channel activator
UOM:
1 * 1 EA
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
Highly potent and selective serotonin uptake inhibitor
Numéro de catalogue:
(ENZOBMLP1990010)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Substrate for cathepsin S and cathepsin L
UOM:
1 * 10 mg
New Product
Numéro de catalogue:
(ENZOBMLPI1460010)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Argatroban is a synthetic peptidomimetic thrombin inhibitor which is in clinical use. It presents significant advantages as an anticoagulant in deep vein thrombosis, stroke prevention in atrial fibrillation and thromboembolic disease and especially in patients with coronary artery disease and heparin-induced thrombocytopenia.
UOM:
1 * 10 mg
New Product
Numéro de catalogue:
(ENZOALX350150M001)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Type I ribosome inactivating protein (RIP). Depurinates RNA in ribosomes, thus inhibiting protein synthesis in eukaryotic cells, which results in cell death. Widely used to construct immunotoxins composed of cell-targeted antibodies. As a type I RIP it lacks the lectin subunit and is practically non-toxic to intact cells.
UOM:
1 * 1 mg
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
Calnexin (CNX), an unglycosylated resident ER transmembrane protein, together with Calreticulin (CRT), plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their monoglucosylated glycans. Calnexin associates with newly synthesized monomeric glycoproteins and only recognizes glycoproteins when they are incompletely folded. Furthermore, Calnexin has been demonstrated to function as a molecular chaperone capable of interacting with polypeptide segments of folding glycoproteins.
Numéro de catalogue:
(ENZOADISPA850F)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Grp94 (Glucose-regulated protein 94) is an abundant resident endoplasmic reticulum (ER) lumenal stress protein, which together with cytosolic Hsp90 belongs to the Hsp90 family of molecular chaperones. Grp94 expression is upregulated by stress conditions such as glucose starvation and heat shock, which promote protein misfolding or unfolding. In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells.
UOM:
1 * 200 µG
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:
Anti-HSP90B Rabbit Polyclonal Antibody
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.
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