You Searched For: Enzo Life Sciences

Catalog Number: (CA200063-164)

Supplier: Enzo Life Sciences

Description: Rap1, which is a member of the Ras family of GTP-binding proteins, cycles between an active GTP-bound and an unactive GDP-bound form that is mediated by GTPase activating protein (GAP). Rap1 is proposed to regulate Ras-mediated signaling and may also be involved in the regulation of Integrin-mediated cell adhesion although the mechanism of regulation is not known.

Catalog Number: (CA200062-880)

Supplier: Enzo Life Sciences

Description: Postsynaptic density protein 95 kDa (PSD-95), also known as Synapse associated protein 90 kDa (SAP90), is a brain specific protein that is highly similar to the Drosophila dlg tumor suppressor protein. PSD-95 is a member of membrane associated proteins that are localized beneath the postsynaptic membrane of synapses in the CNS. PSD-95 interacts with NMDA receptor and Shaker-type K+ channels and contributes to their clustering and localization at the synaptic spines in hippocampal neurons and the pinceau terminal of cerebellar basket cells, respectively.

Catalog Number: (CA200062-026)

Supplier: Enzo Life Sciences

Description: MEK is a dual specificity kinase capable of phosphorylating both tyrosine and threonine residues. The MEK family, which is also known as MAP kinase kinase, phosphorylates MAP kinases on the conserved T-X-Y motif; phosphorylation of MAPK by MEK results in an increase in MAPK activity. MEK is involved in a diverse array of cellular processes such as stress-activated response, apoptosis, cytokine-induced cell proliferation, and DNA recombination during meiosis.

Supplier: Enzo Life Sciences

Description: Bassoon is a 420 kDa protein that localizes at the presynaptic nerve terminals and is believed to play a role in the structural and functional organization of the synaptic vesicle cycle. Bassoon is concentrated at sites opposite to postsynaptic densities in synaptic terminals and in cultured neurons, it is found to colocalize with GABA (A) and glutamate (GluR1) receptors. These observations suggested that they serve specific functions at synaptic junctions and may be involved in organization of the cytoskeleton at the site of neurotransmitter release.

Supplier: Enzo Life Sciences

Description: 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.

Catalog Number: (CA200062-774)

Supplier: Enzo Life Sciences

Description: Grp94 (Glucose-regulated protein 94) is an abundant resident endoplasmic reticulum (ER) lumenal stress protein, which together with cytosolic Hsp90 belongs to the Hsp90 family of molecular chaperones. Grp94 expression is upregulated by stress conditions such as glucose starvation and heat shock, which promote protein misfolding or unfolding. In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells.

Supplier: Enzo Life Sciences

Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Supplier: Enzo Life Sciences

Description: 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.

SDS

Catalog Number: (CA95057-948)

Supplier: Enzo Life Sciences

Description: SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

SDS

Supplier: Enzo Life Sciences

Description: Dehydrins are a family of proteins that become abundant during dessication in seedlings and embryos of cereal crop plants including barley, corn, wheat, and rice. Dehydrin proteins have a highly conserved lysine-rich block (KIKEKLPG) found near the carboxy terminus which appears to be characteristic of, and unique to Dehydrins.

Catalog Number: (CA200062-426)

Supplier: Enzo Life Sciences

Description: Hypoxia inducible factor-1 (HIF-1) is a transcriptional complex which regulates systemic, local and intracellular homeostatic responses elicited by hypoxia. HIF-1 is a heterodimer of HIF-1alpha and HIF-1beta. HIF-1beta is constitutively expressed and serves as a dimerization partner for several other transcription factors, while HIF-1alpha and the closely related HIF-2 are unique to HIF-1 and their expression is tightly regulated by cellular oxygen concentration. HIF-1 regulates a diverse group of genes, including erythropoietin, VEGF, glucose transporters, heme oxygenase, and NOS.

Catalog Number: (CA200062-422)

Supplier: Enzo Life Sciences

Description: The phosphoprotein BVR (Biliverdin Reductase) is an oxireductase which catalyzes the reduction of the gamma-meso bridge of Biliverdin to Bilirubin. BVR is unique among all enzymes characterized to date because BVR has dual pH/dual cofactor requirements. The reductase is highly conserved in its primary structure and molecular properties and uses NADH in the acidic range (peak activity at pH~6.7), whereas NADPH is utilized in the basic range (peak activity at pH ~8.7).

Supplier: Enzo Life Sciences

Description: Ubiquitin (Ub) plays a very important role in regulated non-lysosomal ATP dependent protein degradation. The protein to be degraded is conjugated to Ub and the ubiquinated protein is then selectively degraded by the 26S complex, a multicatalytic cytosolic and nuclear protease. The Ub-proteasome proteolytic pathway, which is a complex process, is implicated to be of great importance for regulating numerous cellular processes.

Catalog Number: (CA200061-462)

Supplier: Enzo Life Sciences

Description: The exotoxin produced by B. anthracis is composed of three proteins: a cell-receptor binding protein known as Protective Antigen (PA), and two enzymes, Edema Factor (EF) and Lethal Factor (LF). An 83 kDa form of PA binds to a cell surface receptor and, upon proteolytic activation to a 63 kDa fragment, heptamerizes to form a membrane channel that mediates the entry of three molecules of LF or EF into the cells. PA and LF form Lethal Toxin, which is the dominant virulence factor produced by B. Anthracis and is the major cause of death in infected animals.

Catalog Number: (CA200061-474)

Supplier: Enzo Life Sciences

Description: Osteopontin (OPN) is an acidic extracellular matrix cell adhesion protein that is relatively abundant not only in bone matrix, plasma, urine, and milk, but is also found in malignant and atherogenic tissues. Phosphorylation, glycosylation and calcium modifications allow intact and fragmented Osteopontin to direct a variety of diverse responses including tissue remodeling, inflammation and cell survival. Plasma Osteopontin has been shown to provide prognostic information in breast, prostate, colon, and lung cancers as well as metastatic carcinomas. The notable presence of Osteopontin in a variety of tumors is strongly correlated to pathological stage, suggesting its critical role in tumor invasiveness, progression and metastasis. In addition, Osteopontin inhibits inducible nitric oxide synthase activity, thereby protecting tumor cells from NO-mediated macrophage cytotoxic attack. Osteopontin is found in atherosclerotic plaques and may drive a number of diabetic vascular pathologies.

Catalog Number: (CA200061-484)

Supplier: Enzo Life Sciences

Description: Cytochrome c, which is a critical component of the electron transport chain, is a component of the functional apoptosome. Upon release from the mitochondria, cytochrome c binds to the adaptor proteins Apaf-1 and procaspase-9 to form a cytosolic apoptosome complex. This event results in activation of procaspase-9 and its subsequent cleavage and activation of caspase-3 leading to the degradation of a series of cellular substrates and subsequently cell death.