5269 Results for: "Enzo Life Sciences"

Supplier: Enzo Life Sciences

CD40 is a 45-50 kDa type I membrane protein and a member of the tumor necrosis factor (TNF) receptor superfamily. CD40 is also known as pb50 or CDW40.  CD40 is expressed primarily by professional antigen-presenting cells and it is also expressed on non-immune cell types. The CD40 expressed by professional antigen-presenting cells plays a critical role in co-stimulation and antigen-presenting cell activation in T cell-dependent immune responses. Signals generated through CD40 in B cells are anti-apoptotic. These signals are also required for T cell-dependent B cell activation and proliferation, isotype switching, up-regulation of costimulatory receptors, germinal center formation and memory generation. CD40 signal transduction is initiated by binding trimeric CD40 ligand (CD40L) which is found on the surface of activated T cells.  CD40 engages several signalling pathways in B cells and these include NF-kB, the mitogen-activated protein kinases p38 and c-Jun N-terminal kinase. The 62 amino acid cytoplasmic domain (CD40c) of CD40 contains two linear TNF-receptor associated factor (TRAF) binding domains. The membrane proximal site of CD40c binds TRAF6 and the membrane distal site binds TRAF1, 2 and 3. CD40c is thought to mediate the CD40-dependant signalling pathways by recruitment of TRAF to this multimerized domain. CD40 ligation has also been shown to stimulate iNOS expression, and therefore NO production, by activating NF-kB in IFN-g treated microglial cells. NO derived from microglia has been implicated in the damage of myelin-producing oligodendrocytes in demyelinating disorders like multiple sclerosis (MS) and neuronal death during Alzheimer’s disease and brain trauma. Increased CD40-CD40 ligation has been implicated in the pathogenesis of several autoimmune inflammatory diseases, such as MS, arthritis and insulin-dependant diabetes.

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Produced in E. coli. Human LC3-I is fused at the N-terminus to a His-tag.

Supplier: Enzo Life Sciences

The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis. caspases are synthesized as inactive zymogens that can be cleaved to form active enzymes following the induction of apoptosis by stress or death receptors. Initiator caspases (e.g. caspase-8 and -10) are activated by dimerization of the zymogen on a dedicated adaptor protein. These activated initiator caspases in-turn cleave downstream effector or executioner caspases (e.g. caspase-3, -6, and -7) in a cascade-like manner, which cleave key cellular proteins that lead to the morphological changes associated with apoptotic cell death.

Supplier: Enzo Life Sciences

Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins at the neuromuscular junction during development. Agrin, MuSK, and Rapsyn are all essential components for AChR aggregation, through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface and induces AChR aggregation.

Supplier: Enzo Life Sciences

Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins during development at the neuromuscular junction. Agrin, MuSK and Rapsyn are all essential components for AChR aggregation through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface, and induces AChR aggregation. The central region contains two O-linked glycosylation sites and a domain homologous to domain III of laminin. The N-terminal region anchors agrin to the extracellular matrix via other basal membrane components. This region also contains a protease inhibitor domain and glycosaminoglycan attachment sites, increasing the predicted MW from 200kDa to ~600kDa. The diagram shown indicates the domain structure and functional regions of agrin, as well as domains required for AChR aggregation and alpha-dystroglycan and heparin binding.  Various agrin isoforms are generated by alternative splicing at the X, Y and Z sites, and differ in the presence or absence of small inserts. The isoforms can determine the biological activity of agrin and their expression in specific tissues and stages of development. While no difference in functional activity has been detected between splicing variants at site X, insertion of a 4 aa peptide at site Y modestly increases agrins nAChR clustering activity. Insertion of an 8 aa peptide at splicing site Z increases the clustering activity of soluble rat agrin 10,000 fold.

Supplier: Enzo Life Sciences

Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins at the neuromuscular junction during development.

Supplier: Enzo Life Sciences

APRIL (A proliferation-inducing ligand) is a member of the TNF family. APRIL stimulates B- and T-cell proliferation, triggers humoral immune responses, activates NF-κB, and induces cell death.

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Host: Rabbit

Supplier: Enzo Life Sciences

Host: Rabbit

Supplier: Enzo Life Sciences

CD51 (integrin αV subunit) associates with CD61 (integrin β3 subunit) binding to the RGD sequence in extracellular matrix proteins like vitronectin, fibrinogen, thrombospondin, von Willebrand factor and osteopontin. The αV/β3 heterodimer is expressed in endothelial cells, leukocytes, NK cells, macrophages, neutrophils, platelets and several malignant tumor cells and seems to play a role in embryo implantation, angiogenesis, wound healing and cancer. αV/β3  is also highly expressed in osteoclasts being important for bone resorption.

Supplier: Enzo Life Sciences

Host: Rabbit

Supplier: Enzo Life Sciences

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.

Supplier: Enzo Life Sciences

Host: Rabbit

Supplier: Enzo Life Sciences

Host: Goat

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Host: Rabbit

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 Hsp70 family of heat shock protiens 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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Cholesterol metabolite linked to breast cancer, neurodegenerative disease and metabolism.

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Host: Mouse, Isotype: IgG2b

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Anti-HSP90 Mouse Monoclonal Antibody [clone: 2D11B9]

Supplier: Enzo Life Sciences

DnaK possesses an autophosphorylation activity and a weak 5-nucleotidase activity, cleaving the 5 phosphate groups from both ribose and deoxyribose nucleotides. The role of DnaK in ATP-dependent protein-protein interactions has been extended to normal E. coli physiology, where, like eukaryotic Hsp70 homologs, it is thought to participate in the assembly/disassembly of protein complexes.

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Produced in E. coli.

Supplier: Enzo Life Sciences

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.

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Produced in E. coli.

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Inhibitor of caspase-1 and -4

Supplier: Enzo Life Sciences

Fluorogenic substrate for furin/SPC1/PACE/PCSK3 and other subtilisin/kexin-like proprotein convertases such as Kex2, SPC2/PC2/PCSK2, SPC3/PCSK1, PACE4/SPC4/PCSK6, SPC5/PC4/PCSK4, SPC6/PC5/PC6/PCSK5, and SPC7/LPC/PC7/PC8/PCSK7. Can be used on live cells. Ex: 340-360 nm, Em: 440-460 nm.

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Inhibitor of caspase-1 and -4

Supplier: Enzo Life Sciences

Viperin has been identified as a human cytomegalovirus and IFN-γ inducible protein. Its expression is activated by both TLR3-dependent and RIG-I-dependent pathways. Viperin inhibits influenza A virus release of infected cells by altering plasma membrane fluidity and the formation of lipid rafts. It acts on the lipid rafts by decreasing the activity of the enzyme farnesyl diphosphate synthase (FPPS) which is essential for isoprenoid biosynthesis.

Supplier: Enzo Life Sciences

Host: Rabbit

Supplier: Enzo Life Sciences

Aminopeptidase inhibitor.