Procurou por: ENZO LIFE SCIENCES

Código de Artigo: (ENZOBMLP1340005)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Caspase substrate

UOM: 1 * 5 mg

Promoção

Fornecedor: ENZO LIFE SCIENCES

Descrição: Cysteine protease inhibitor

Código de Artigo: (ENZOBMLP1380025)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Cathepsin substrate

UOM: 1 * 25 mg

Promoção

Código de Artigo: (ENZOBMLP1180500)

Fornecedor: ENZO LIFE SCIENCES

Descrição: PKA substrate

UOM: 1 * 0,5 mg

Promoção

Código de Artigo: (ENZOBMLP1280001)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Fluorogenic substrate for several matrix metalloproteinases (MMPs).

UOM: 1 * 1 mg

Promoção

Código de Artigo: (ENZOBMLNS1120050)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Potent and selective serotonin uptake inhibitor (Ki=5.4nM). Modifies gene expression profile in Alzheimer lymphocytes. Clinically useful antidepressant.

UOM: 1 * 50 mg

Promoção

Código de Artigo: (ENZOBMLP1270001)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Reference peptide for OmniMMPTM fluorogenic substrate (BML-P126) and TACE (ADAM17) fluorogenic substrate (BML-P132). Ex.: 328 nm, Em.: 393 nm.

UOM: 1 * 1 mg

Promoção

Código de Artigo: (ENZOBMLNS5300050)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Serotonin receptor ligand

UOM: 1 * 50 mg

Promoção

Código de Artigo: (ENZOBMLNA1380020)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Na+ channel blocker, K+ channel activator

UOM: 1 * 20 mg

Promoção

Fornecedor: ENZO LIFE SCIENCES

Descrição: Kavain is one constituent of kava-kava, an herbal drug of the South Pacific islands, which displays anti-convulsive, anxiolytic, analgesic and muscle relaxing properties. Kavain inhibits voltage-dependent Na+ channels in rat CA1 hippocampal neurons. It displays protective effects in the MPTP mouse model of Parkinson's disease but potentiates NMDA toxicity in the developing hippocampus.

Código de Artigo: (ENZOBMLNH1070010)

Fornecedor: ENZO LIFE SCIENCES

Descrição: Histamine H₁ receptor antagonist. An antagonist of low affinity neurotensin receptors.

UOM: 1 * 10 mg

Promoção

Fornecedor: ENZO LIFE SCIENCES

Descrição: SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

Fornecedor: ENZO LIFE SCIENCES

Descrição: Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.

Fornecedor: ENZO LIFE SCIENCES

Descrição: 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.

Fornecedor: ENZO LIFE SCIENCES

Descrição: 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.

Fornecedor: ENZO LIFE SCIENCES

Descrição: 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.