You Searched For: Enzo Life Sciences

Supplier: 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.

Catalog Number: (89153-792)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgG1

Catalog Number: (89153-870)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgG1

Catalog Number: (89153-788)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgM

Catalog Number: (89158-460)

Supplier: Enzo Life Sciences

Description: Fibronectins are high molecular weight, disulphide-linked, dimeric cell adhesion glycoproteins found in basement membranes and in the interstitial connective tissue matrix. A single fibronectin gene is subject to alternative splicing in a cell-type-, development- and age-regulated manner which gives rise to multiple molecular forms. In addition to their prominent role in adhesion, fibronectins have been reported to mediate various aspects of cellular interaction, including migration during development and wound-healing, haemostasis, and the regulation of cell growth and differentiation. Cellular fibronectins (cFn) are found in low amounts in normal human plasma and tissues, but they are abundant in the plasma of carcinoma patients and in the stroma of various carcinomas. In contrast, a soluble form of fibronectin produced by hepatocytes is readily detectable in plasma and becomes deposited in pericellular matrices and within tissues. This form of fibronectin, referred to as ‘plasma fibronectin’ (pFn), differs from cFn by the absence of an amino acid sequence, known as extra domain A1.

Catalog Number: (89163-172)

Supplier: Enzo Life Sciences

Description: Host: Rabbit

Catalog Number: (89153-564)

Supplier: Enzo Life Sciences

Description: Anti-Enhancer for ligands Monoclonal Antibody

Catalog Number: (89145-474)

Supplier: Enzo Life Sciences

Description: Host: Rabbit

Supplier: Enzo Life Sciences

Description: The tumor suppressor CYLD is a deubiquitinylating enzyme (DUB) that antagonises NF-κB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesised in response to cytokine stimulation. The DUB activity of CYLD is mediated by its C-terminal ubiquitin specific protease (USP) domain, pathogenic truncations and mutations of which are associated with the hypertrophic skin tumor cylindromatosis through disruption of the USP domain and subsequent loss of CYLD catalytic activity.

Catalog Number: (89153-332)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgG1

Catalog Number: (89162-934)

Supplier: Enzo Life Sciences

Description: Host: Rabbit

Supplier: Enzo Life Sciences

Description: α-Synuclein accumulates in Lewy bodies, which are intraneuronal cytoplasmic inclusions present in the brains of sporadic Parkinson's disease patients, and is implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders. α-Synuclein appears to associate with other proteins that aggregate and is found in β-amyloid plaques and neuritic tangles in Alzheimer's disease.

Catalog Number: (89162-936)

Supplier: Enzo Life Sciences

Description: Host: Rabbit

Catalog Number: (89153-602)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgG1

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.

Supplier: Enzo Life Sciences

Description: 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.