16885 Results for: "ENZO LIFE SCIENCES"

Supplier: Enzo Life Sciences

Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. KLK8 is one of the fifteen kallikrein subfamily member. The KLK8 enzyme exhibits distinct patterns of expression that suggest roles in brain plasticity and ovarian cancer.

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The most sensitive, specific and flexible alternative to more costly and time-consuming methods for oxytocin detection.

Supplier: Enzo Life Sciences

The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells contain isoforms Hsp90 alpha and Hsp90 beta, encoded by separate genes. The amino acid sequences of human and yeast Hsp90 alpha are 85% and 90% homologous to those of Hsp90 beta, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N -terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 functions as part of the cell

Supplier: Enzo Life Sciences

Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. KLK7 is one of the fifteen kallikrein subfamily members. The KLK7 enzyme is thought to be involved in the proteolysis of intercellular cohesive structures preceding desquamation, which is the shedding of the outermost layer of the epidermis.

Supplier: Enzo Life Sciences

Leukotrienes are metabolic products of arachidonic acid formed by the action of 5-lipoxygenase (5-LO), with the principal products being leukotrienes C4 (LTC4) and B4 (LTB4). Leukotriene B4 (LTB4) stimulates leukocyte functions including lysosomal enzyme release, adhesion, and aggregation of polymorphonuclear leukocytes. LTB4 has been implicated as a potent mediator of inflammatory diseases and immunoregulation. The cysteinyl leukotrienes (LTC4, LTD4, and LTE4) are formed by addition of cysteine derivatives to LTA4. The conversion of LTA4 to LTC4 by the enzyme LTC4 synthase limits the rate of cysteinyl leukotriene formation. Cysteinyl leukotrienes are potent lipid mediators in inflammation, inducing smooth muscle contractions and increased capillary permeability.

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Anti-TRAP1 Rabbit Polyclonal Antibody

Supplier: Enzo Life Sciences

Isolated from bovine eye lens.

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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.

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Enzo Life Sciences

The Insulin Receptor (InsR) is a heterodimeric receptor tyrosine kinase with an extracellular alpha-chain, a transmembrane domain and an intracellular beta-chain. InsR is activated upon binding of the peptide hormone insulin, leading to autophosphorylation of tyrosine residues 1146, 1150, and 1151 in the activation loop of the beta-chain. Additional autophosphorylation sites such as tyrosine residues 960, 972, 1316, and 1322 regulate the assembly of signal transduction complexes.

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Members of the TNF superfamily regulate immune responses and induce apoptosis. Two members of this family were identified and designated BAFF and April, respectively. Three receptors for BAFF were identified; these include: BCMA (B-cell maturation protein), TACI, and BAFF-R. BCMA, like TACI, binds BAFF and April. BAFF and its receptors induce B-Cell development and survival, activate NF-κB and c-jun N-terminal kinase, and are involved in B-Cell associated autoimmune diseases.

Supplier: Enzo Life Sciences

BAFF, or B-cell Activating Factor, is a member of the TNF superfamily also known as BLyS (B Lymphocyte Stimulator), TALL-1 (TNF- and ApoLrelated Leukocyte-expressed Ligand), and THANK (TNF Homologue that Activate Apoptosis, NF-κB and c-jun N-terminal Kinase). BAFF/BLyS was characterized as a B-cell activator since it induced B-cell proliferation and immunoglobulin secretion. Three receptors for BAFF were identified and designated TACI, BCMA, and BAFF-R. BAFF and its receptors are essential for B-cell development, survival, and humoral immune responses.

Supplier: Enzo Life Sciences

Anthrax Lethal Factor (LF) is a zinc-dependent protease that cleaves mitogen-activated protein kinase kinase (MAPKK) and causes lysis of macrophages. LF, together with Protective Antigen, forms Lethal Toxin, which is the dominant virulence factor produced by B. anthracis and is the major cause of death in infected animals. Lethal toxin has been reported to trigger apoptosis in human melanoma cells.

Supplier: Enzo Life Sciences

The Ras superfamily of small guanosine triphosphatases (GTPases) is traditionally subdivided into five families: Ras, Rho, Rab, Ran, and Arf. Rap1/Krev1 is a member of the Ras family of low molecular weight GTP-binding proteins1. Ras-like GTPases are ubiquitously expressed, evolutionarily conserved molecular switches that couple extracellular signals to various cellular responses. Rap1 is primarily found at the cytosolic side of intracellular membranes and has two isoforms: Rap1a and 1b2. Both isoforms have a molecular mass of 21 kDa and are isoprenylated at the carboxyl-terminal and phosphorylated by the cAMP-dependent protein kinase A (PKA)3. Rap1 cycles between a GTP-bound active form and a GDP-bound inactive form that is mediated by GTPase activating protein (GAP) and GDP dissociation stimulator (GDS)4,5. Activation occurs by a variety of extracellular stimuli through several conserved guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs). Rap1 is proposed to regulate Ras mediated signaling and may also be involved in the regulation of integrinmediated cell adhesion, although the mechanism of regulation is not known. Overexpression of Rap reverses the transformed phenotype induced by Ras, possibly by competing with Ras for interaction with Ras-GAP. Rap has been shown to participate in MAP kinase cascade activated by growth factor and maintaining human T cell anergic state by blocking IL-2 expression.

Supplier: Enzo Life Sciences

Bad is an ~22 kDa pro-apoptotic protein that aids in the initiation of cell death. It exhibits sequence homology to Bcl-2, a protein that prevents apoptosis, within its BH1 and BH2 domains. Bad is phosphorylated at several sites including Ser112, Ser136; phosphorylation by kinases like Akt is known to alter the effects of Bad. Bad has been demonstrated to be phosphorylated at Ser170.

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The Src homology 2 domain containing (Shc) adaptor protein links growth factor, cytokine, and antigen receptor stimulation to the Ras signaling pathway, and plays a critical role in insulin signaling, tumorigenesis, and hematopoietic cell growth and differentiation. Structurally, Shc is composed of an N-terminal phosphotyrosine binding (PTB) domain, a medial CH1 domain, and a C-terminal SH2 domain. Upon binding to activate cell-surface receptors, Shc is phosphorylated at three tyrosine residues (Tyr239, Tyr240, Tyr317) triggering recognition of Shc by SH2-containing proteins such as Grb2.

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For the quantitative determination of αB-Crystallin in cell lysates of human, mouse, rat, and cow origin.

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For the measurement of AdoMet-dependent methyltransferase activity in purified in vitro samples that do not contain reductants from any species.

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The RecA protein is a member of the RecA/Rad51 family of proteins which are ubiquitous among organisms from bacteria to humans. RecA protein of E. coli is a catalyst of DNA strand exchange in the early phase of homologous recombination involving the exchange of two aligned, nearly identical strands of DNA. RecA is also a key enzyme in recombinational repair of damaged DNA.

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Mycotoxin

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EGFR tyrosine kinase auto-phosphorylation inhibitor

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Potent inhibitor of JNK

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Potent multi-target inhibitor of Abl, PDGFRα, VEGFR2, FGFR1 and Src

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Potent c-MET and ALK inhibitor

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Selective MEK inhibitor

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Sensitive BNP fragment ELISA kit enabling detection of BNP fragment in serum and plasma.

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Highly specific active enzyme cleaves angiotensinogen to yield angiotensin I

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Potent inhibitor of GSK-3 ATP-binding site.

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Highly potent, ATP-competitive, and specific mTOR kinase inhibitor. Antiproliferative.

Supplier: Enzo Life Sciences

Potent, specific and orally active C5a receptor antagonist.