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Recombinant GroEL (from E. coli)

Catalog Number: (ENZOALX201141C025)

Supplier: ENZO LIFE SCIENCES

Description: Produced in <i>E. coli</i>.

UOM: 1 * 25 µG

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Human recombinant alpha-Synuclein (from E. coli)

Catalog Number: (ENZOALX201265C100)

Supplier: ENZO LIFE SCIENCES

Description: Produced in <i>E. coli</i>. alpha-synuclein is a major component of Parkinson's disease aggregates and is implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders.

UOM: 1 * 100 µG

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Human recombinant Matriptase

Catalog Number: (ENZOALX201246U250)

Supplier: ENZO LIFE SCIENCES

Description: Recombinant human matriptase (aa 596-855) fused at the N-terminus to a His-tag.

UOM: 1 * 1 Vial

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Anti-Peptide Tyrosine Tyrosine Mouse Monoclonal Antibody

Catalog Number: (ENZOBPDABS029011)

Supplier: ENZO LIFE SCIENCES

Description: Peptide tyrosine-tyrosine (PYY) amide is a 36 amino-acid. PYY is a member of the pancreatic polypeptide (PP) family of peptides (neuropeptide Y (NPY), PYY and PP). While NPY is localized in neurons (both in the central and peripheral nervous system) and PP in the pancreatic islets, PYY is found in both neurons and the gut. PYY is released in response to food intake from the same endocrine cells (L cells) in the intestinal mucosa as the glucagon-like peptides, and inhibits gall bladder secretion, gut motility and pancreatic secretion. These effects are similar to those of PP and overlap with the gut inhibitory activity of GLP-1.

UOM: 1 * 1 mg

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Anti-HSP70 Mouse Monoclonal Antibody (AP (Alkaline Phosphatase))

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.

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Anti-HSPA8 Rabbit Polyclonal Antibody

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 Hsd70 cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

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