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ENZO LIFE SCIENCES
Fournisseur:
ENZO LIFE SCIENCES
Description:
Necrosis inhibitor
Numéro de catalogue:
(ENZOALX2018120100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Produced in <i>E. coli</i>. Non-glycosylated protein, containing 54 amino acids, with a molecular weight of 6.3 kDa.
UOM:
1 * 1 EA
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
PARP inhibitor
Numéro de catalogue:
(ENZOALX380237M010)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Potent antibacterial antibiotic. It induces platelet aggregation by binding to a factor absent in people suffering from von Willebrand’s disease and is therefore an important diagnostic tool. Chiral selector for the separation of enantiomers by HPLC, TLC and electrophoresis.
UOM:
1 * 10 mg
New Product
Numéro de catalogue:
(ENZOALX380238M001)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Cation ionophore.
UOM:
1 * 1 mg
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
Potent and orally active Lck/Src inhibitor.
Fournisseur:
ENZO LIFE SCIENCES
Description:
Competitive inhibitor of HMG-CoA reductase. Suppresses TNF-induced NF-κB activation.
Fournisseur:
ENZO LIFE SCIENCES
Description:
Highly selective inhibitor of Akt1, Akt2 and Akt3
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.
Fournisseur:
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.
Fournisseur:
ENZO LIFE SCIENCES
Description:
Anti-KDEL Mouse Monoclonal Antibody [clone: 10C3]
Numéro de catalogue:
(ENZOADISPA815488E)
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.
UOM:
1 * 1 EA
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.
Numéro de catalogue:
(ENZOALX804167C100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Host: Mouse, Isotype: IgM
UOM:
1 * 1 EA
New Product
Numéro de catalogue:
(ENZOALX804220R100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Host: Mouse, Isotype: IgG3
UOM:
1 * 100 µl
New Product
Numéro de catalogue:
(ENZOALX804101C100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Host: Mouse, Isotype: IgG1
UOM:
1 * 1 EA
New Product
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