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Description: Host: Rabbit

Catalog Number: 89161-840

Supplier: Enzo Life Sciences

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Description: Host: Rabbit

Catalog Number: 89163-218

Supplier: Enzo Life Sciences

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Description: Host: Rabbit

Catalog Number: 89145-162

Supplier: Enzo Life Sciences

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Description: Host: Rabbit

Catalog Number: 89162-222

Supplier: Enzo Life Sciences

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Description: Proteasome 20S (Alpha Subunits) Antibody Sampler Pack

Catalog Number: 89162-268

Supplier: Enzo Life Sciences

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Description: The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits. Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings.  In addition to the 20S particle, the 26S complex contains over twenty additional proteins, ranging in molecular weight from 25 to 10kDa, located in a distinct complex called the ‘PA700 proteasome activator’ or the ‘19S complex’, and which determines substrate specificity and provides the multiple enzymatic functions necessary for proteolysis and viability. Systematic analysis of the sub-unit components have revealed at least six members to be ATPases belonging to a new family of ATPbinding proteins, together with a further fifteen sub-units that lack the capacity to bind ATP, isopeptidases and several other proteins thought to be responsible for the unfolding of a protein substrate prior to insertion into the proteolytic core of the 20S proteasome.

Catalog Number: 89162-232

Supplier: Enzo Life Sciences

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Description: CEA-related cell adhesion molecule 8 (CEACAM8) belongs to the carcinoembryonic antigen (CEA) gene family. It encodes a glycosylphosphatidylinositol (GPI)-linked glycoprotein with a molecular mass of of 95kD and is expressed in cells of the granulocyte-lineage. It is expressed in neutrophils and eosinophils and is characterized as a granulocyte-specific activation antigen. Therefore CEACAM8 could serve as a marker for granulocyte activities. Like all members of the CEA family, it consists of a single N domain, with structural homology to the immunoglobulin variable domains, followed by two immunoglobulin constant-like A and B domains.

Catalog Number: 89155-388

Supplier: Enzo Life Sciences

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Description: Host: Mouse, Isotype: IgG1

Catalog Number: 89166-080

Supplier: Enzo Life Sciences

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Description: Host: Mouse, Isotype: IgG1

Catalog Number: 89153-370

Supplier: Enzo Life Sciences

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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: 89142-062

Supplier: Enzo Life Sciences

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Description: Hsp40/Hdj1 is a cytosolic co-chaperone belonging to the class DnaJ, named after its homolog in E. coli. Hsp40 functions in protein folding by binding nascent peptides and unfolded substrates and facilitating substrate interaction with Hsp70. Binding of Hsp40 to Hsp70 increases Hsp70 ATP hydrolysis and substrate binding, which is reversed by the action of nucleotide exchange factors (GrpE in E. coli). Repeated cycles of Hsp40/Hsp70 peptide binding and ATP hydrolysis prevent premature folding and aggregation, promoting protein maturation throughout the cell.

Catalog Number: 89142-048

Supplier: Enzo Life Sciences

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Description: The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits.

Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. 120S Proteasomes degrade only unfolded proteins in an energy-independent manner, whereas 26S proteasomes degrade native and ubiquitinylated proteins in an ATP-dependent manner. The native protein substrates are recognised by subunits, some with ATP binding sites, of the outer 19S caps of the 26S proteasome.

Catalog Number: 89162-024

Supplier: Enzo Life Sciences

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Description: The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits. Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. 120S Proteasomes degrade only unfolded proteins in an energy-independent manner, whereas 26S proteasomes degrade native and ubiquitinylated proteins in an ATP-dependent manner. The native protein substrates are recognised by subunits, some with ATP binding sites, of the outer 19S caps of the 26S proteasome. The hybridoma secreting the antibody to subunits HC2, HC3, HC8, HC9, Iota and Zeta was generated by fusion of spenocytes from Balb/c mice which had recieved repeated immunisation with dinitrophenylated proteasomes.

Catalog Number: 89162-052

Supplier: Enzo Life Sciences

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Description: Endothelins are a family of peptides that are potent vasoconstrictors produced by mammalian vascular endothelial cells. The receptors for the endothelins are found on various tissues including, but not restricted to, lung and intestine.

Catalog Number: 89145-830

Supplier: Enzo Life Sciences

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Description: Host: Mouse, Isotype: IgG2b

Catalog Number: 89155-126

Supplier: Enzo Life Sciences

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Description: Host: Rat, Isotype: IgG2a

Catalog Number: 89155-294

Supplier: Enzo Life Sciences

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