You Searched For: ASSOCIATED+BAG+INC.

Supplier: Veltek Associates

Description: HYPO-CHLOR® saturated wipes are designed for intricate or sensitive locations where a spray down would create residues.

Catalog Number: (89106-684)

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.

SDS

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.

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.

SDS

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.

Supplier: Freudenberg Medical

Description: HelixMark® peristaltic pump platinum-cured silicone tubing is designed and manufactured for use with peristaltic pumps and other applications with higher effective forces. Peristaltic pump tubing undergoes a Special Stabilization Process (SSP), providing the additional benefits of superior strength, performance, and longer life. Tubing offers proven long wear and volumetric consistency over 8-,12- and 24-hour process runs.

Certificates

Catalog Number: (10334-370)

Supplier: Bioss

Description: This gene is significantly downregulated in primary brain tumors. The exact function of the protein encoded by this gene is unknown. Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitement of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays a important role for auditory synaptic responses. Involved in the suppression of glioma.

Catalog Number: (75932-096)

Supplier: Rockland Immunochemical

Description: Apoptosis is induced by certain cytokines including TNF and Fas ligand of the TNF family through their death domain containing receptors, TNF-R1 and Fas. Several novel death receptors including DR3, DR4, DR5, and DR6 were recently identified. Cell death signal is transduced by death domain containing adapter molecules through the interaction with death domain of these death receptors. A novel TNF-R1 interacting protein was recently identified and designated SODD for silencer of death domains. SODD associates with the death domain of TNF-R1 and prevents constitutive activation of TNF-R1 signaling. TNF treatment releases SODD and permits adapter molecules such as TRADD recruiting to the active TNF-R1 complex, which activates TNF signaling pathways. SODD also interacts with DR3. SODD is ubiquitously expressed in human tissues and cell lines.

Catalog Number: (14003-296)

Supplier: VELTEK ASSOCIATES, INC. MX

Description: DEC-GLASS® was developed for use in cleaning rotation cycles to remove residue left behind from disinfecting agents on glass or plexiglas surfaces.

Certificates

Catalog Number: (77674-918)

Supplier: Associated Bag

Description: Provides a tight seal every time for protection against dirt and moisture. Costs less than our premium brands. Meets FDA and USDA specifications for food contact.

New Product

Supplier: Globe Scientific

Description: These bags are designed for the safe transportation of specimens and documentation.

Catalog Number: (95059-394)

Supplier: KPL

Description: Hybridization bags are used for membrane incubation steps in Southern, Northern, and Western blotting protocols for such applications as hybridizations and washes, antibody and conjugate incubations, substrate application and film exposure.

Catalog Number: (75838-694)

Supplier: Globe Scientific

Description: The special glue closure of our specimen transport bags offer a liquid-tight tamper evident seal.

Supplier: KEYSTONE ADJUSTABLE CAP CO., INC.

Description: Ideal for pharmaceutical and biotech production applications.

Catalog Number: (78003-846)

Supplier: Total Filtration Services

Description: Pe25P1Sh polyester felt 25 micron size #1 steel ring w/handle

Catalog Number: (470093-374)

Supplier: SPORT SUPPLY GROUP, INC.

Description: Bag, mesh (32×36")