12561 Results for: "Enzo Life Sciences"

Supplier: Enzo Life Sciences

Coagulation factor IX is a 57kDa single chain polypeptide, with a normal concentration in human plasma of approximately 3 µg/ml. Factor IX deficiency and lack of coagulation activity is seen in patients suffering from the innate X-chromosome linked disorder, haemophilia B.

Supplier: Enzo Life Sciences

Surfactant protein A (SP-A) is synthesized and secreted by lung epithelial cells. It belongs to group III of the family of C-type lectins, members of which possess an overall structure consisting of multiple globular head regions linked by triple-helical, collagen-like, strands. This group also includes SP-D, and the serum proteins mannan-binding protein, conglutinin, and collectin-43, all of which bind to the C1q receptor found on a wide variety of cells. Both SP-D and SP-A enhance oxygen radical production by alveolar macrophages. The serum concentration is 45 ng/mL in healthy individuals.

Supplier: Enzo Life Sciences

Anti-Complement C5a Mouse Monoclonal Antibody [clone: C17/5]

Supplier: Enzo Life Sciences

Recommended Applications: ICC, IHC, IP, WB, Immunoelectron microscopy

Supplier: Enzo Life Sciences

FAT10 and FAT10 conjugates are rapidly degraded by the proteasome, a process which may involve interaction with NUB1L. FAT10 is also of interest in apoptosis.

Supplier: Enzo Life Sciences

The assembly of individual mammalian proteasome subunits into catalytically active 20S proteasome is a complex process, with biogenesis of the mammalian 20S proteasome occuring via precursor complexes containing α and unprocessed β subunits. The pro-peptides of the β subunits are thought to prevent premature conversion of the precursor complexes into matured particles and are needed for efficient β subunit incorporation. The complex biogenesis is tightly regulated, requiring additional components such as the maturation factor POMP (proteasome maturation protein), an ubiquitous protein in eukaryotic cells. Mammalian POMP is functionally related to but not interchangable with its yeast homologue Ump1. POMP is associated purely with the precursor intermediates and is degraded upon final maturation. Northern blot experiments have revealed that expression of POMP is induced after treatment with interferon γ.

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Enzo Life Sciences

Recommended Applications: IF, IHC (FS)

Species reactivity: Human, Sheep

Supplier: Enzo Life Sciences

Recommended Applications: IP, WB

Species reactivity:

Supplier: Enzo Life Sciences

Recommended Applications: IHC

Species reactivity: Rodent

Supplier: Enzo Life Sciences

Produced in E. coli. Human SUMO-1 is fused to a His-tag.

Supplier: Enzo Life Sciences

Produced in E. coli. Human pro-SUMO-1 is fused at the N-terminus to a His-tag.

Supplier: Enzo Life Sciences

Produced in HEK 293 cells.

Supplier: Enzo Life Sciences

Produced in E. coli. Human SUMO-2 is fused to a His-tag.

Supplier: Enzo Life Sciences

Anti-HSP90A Rat Monoclonal Antibody [clone: 9D2]

Supplier: Enzo Life Sciences

Host: Rabbit

Supplier: Enzo Life Sciences

Assay Buffer from the Ubiquitinylation Kits. Packaged as 5×1 ml.

Supplier: Enzo Life Sciences

Most comprehensive portfolio of heat shock protein (chaperone) products commercially available.

Supplier: Enzo Life Sciences

For the quantitative determination of human Cytochrome c in cell lysates

Supplier: Enzo Life Sciences

For the quantitative determination of human Osteopontin in culture supernatants, milk, plasma, and urine. Cited sample type includes serum.

Supplier: Enzo Life Sciences

Calmodulin inhibitor

Supplier: Enzo Life Sciences

cADPR antagonist.

Supplier: Enzo Life Sciences

TRPA1 activator.

Supplier: Enzo Life Sciences

ATPase inhibitor

Supplier: Enzo Life Sciences

PKC activator

Supplier: Enzo Life Sciences

HSP70 inhibitor

Supplier: Enzo Life Sciences

Novel inhibitor of ubiquitin C-terminal hydrolase L3 (IC50 = 0.6µM). Displays 125-fold greater selectivity over UCH-L1 (IC50 = 75µM).

Supplier: Enzo Life Sciences

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

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.