12524 Results for: "ENZO LIFE SCIENCES"

Supplier: Enzo Life Sciences

AIM2 is a strong candidate as a tumor suppressor as it is a member of the HIN-200 (hemopoietic interferon-inducible, nuclear proteins containing a 200 amino acid repeat) family of proteins that have been shown to regulate cell growth and survival. The HIN-200 family of proteins consists of four members in human, IFI 16, MNDA, AIM2 and IFIXl. It has been reported that AIM2 is a receptor for cytosolic dsDNA, which forms an inflammasome complex with ASC to activate caspase-1-mediated processing of IL-1β.

Supplier: Enzo Life Sciences

Indoleamine 2,3-dioxygenase (IDO) is an IFN-γ inducible gene. It catalyzes the degradation of the essential amino acid L-tryptophan to N-formylkynurenine. IDO has been implicated in protection against intracellular and extracellular pathogens. The mIDO-48 monoclonal antibody recognizes mouse IDO also known as Indolamine 2,3-dioxygenase, Indole 2,3-dioxygenase, and Indoleamine-pyrrole 2,3-dioxygenase. This antibody does not appear to react with human IDO. IDO is a ubiquitously expressed cytoplasm protein with a predicted molecular weight approximately 45 kDa. Indoleamine 2,3-dioxygenase (IDO) is one the best known IFN-γ inducible genes. The product of IDO gene catalyzes the degradation of the essential amino acid L-tryptophan to N-formylkynurenine. IDO has been implicated in protection against intracellular and extracellular pathogens. It also has been shown to maintain the special immune suppressive status of immune-privileged sites such as the brain, eyes, kidney, and placenta. The IDO antibody has been shown to be useful for western blotting and Immunohistochemistry.

Supplier: Enzo Life Sciences

Potent and selective inhibitor of VEGFR-2 (Flk-1, KDR). It displays a 100-fold greater potency for the unactivated form of the kinase (Ki=0.04µM) compared to the activated form (Ki=4µM).

Supplier: Enzo Life Sciences

Macrocyclic-triene antibiotic possessing potent immunosuppressant activity. It forms a complex with FKBP12 that binds to an effector, thus inhibiting IL-2 and other growth promoting lymphokines. The effectors were identified as FRAP (FKBP12 rapamycin-associated protein) and RAFT1 (rapamycin and KFBP12 target). Rapamycin/FKBP complex does not inhibit FRAP PI 4-kinase activity, but does inhibit FRAP autophosphorylation. Rapamycin induces inhibition of p70^s6k, p33^cdk2 and p34^cdc2. Selectively blocks signaling leading to the activation of p70/85 S6 kinase. Enhances apoptosis. Activator of autophagy both in vitro and in vivo.

Supplier: Enzo Life Sciences

mGluR1 and mGluR5 receptors signal through Gq/G11 that activates phospholipase C and ultimately produces an increase in inositol triphosphate and cytosolic Ca2+. More downstream signaling pathways include activation of PKC and modulation of Ca2+ and K+ ion channels. Activation of signaling pathways independent of G proteins has also been reported. mGluR1 is predominantly expressed in nervous tissue although expression in several non-neural cell types has also been described. In the brain it is highly expressed in the hippocampus, cerebellum, olfactory bulb and thalamus.

Supplier: Enzo Life Sciences

The IL-2 (human), EIA kit is a colorimetric immunometric enzyme immunoassay kit with results in 3 hours.

Supplier: Enzo Life Sciences

The BIOSCORE® Screening and amplification kit is a rapid and reliable method to determine the quality of genomic DNA isolated from formalin-fixed paraffin-embedded (FFPE) tissue samples before use in array-based genome-wide copy number analysis and other genomic profiling applications.

Supplier: Enzo Life Sciences

ROS inducer.

Supplier: Enzo Life Sciences

Recommended Applications: IHC (PS)

Species reactivity: Human

Supplier: Enzo Life Sciences

Novel Cell-free Sclerostin/LRP Binding Assay Ideal for Primary Inhibitor Screens.

Supplier: Enzo Life Sciences

Apoptosis inducing factor (AIF) is a mitochondrial inter-membrane flavoprotein that is ubiquitously expressed both in normal tissues and in a variety of cancer cell lines. AIF is synthesized as a nonapoptogenic precursor in the cytoplasm and efficiently imported into the mitochondrial inter-membrane space. Mature AIF protein is normally confined to the mitochondrial inter-membrane space. In a variety of different apoptosis-inducing conditions AIF translocates through the outer mitochondrial membrane to the cytosol and to the nucleus. Extra-mitochondrial AIF induces nuclear chromatin condensation and large scale (~50kb) DNA fragmentation.

Supplier: Enzo Life Sciences

VEGF (Vascular endothelial growth factor) is a potent polypeptide regulator of blood vessel function. VEGF promotes an array of responses in the endothelium, including hyperpermeability, endothelial cell growth, angiogenesis, and enhanced glucose transport. Several alternate splice isoforms of VEGF are known. Two high-affinity receptors for VEGF, VEGFR1 and VEGFR2, have been identified and characterized.

Supplier: Enzo Life Sciences

The tumor suppressor putative HLA-DR-associated proteins (PHAPs) were identified as important regulators of mitochondrial mediated apoptosis. PHAP appears to facilitate apoptosome mediated caspase-9 activation and to stimulate the mitochondrial apoptotic pathway. PHAP was also shown to oppose both ras- and myc mediated cell transformation.

Supplier: Enzo Life Sciences

Apaf-1 (Apoptosis protease-activating factor 1), a mammalian protein homologous to C. elegans CED-4, is an essential adaptor molecule and a key linker of the mitochondrial apoptotic pathway. Apaf-1 binds to Cytochrome c (Apaf-2) leading to the formation of a large multimeric complex. This complex recruits (through CARD) Procaspase-9 and once activated, caspase-9 (Apaf-3) dissociates. Activated caspase-9 in turn cleaves and activates caspase-3, one of the proteases responsible for the proteolytic cleavage of many key proteins in apoptosis. Apaf-1 can also associate with caspase-4, caspase-8 and Diva. Apaf-1 is ubiquitously expressed in human tissues.

Supplier: Enzo Life Sciences

VEGFR inhibitor

Supplier: Enzo Life Sciences

FAAH inhibitor

Supplier: Enzo Life Sciences

Calnexin (CNX), an unglycosylated resident ER transmembrane protein, together with Calreticulin (CRT), plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their monoglucosylated glycans. Calnexin associates with newly synthesized monomeric glycoproteins and only recognizes glycoproteins when they are incompletely folded. Furthermore, Calnexin has been demonstrated to function as a molecular chaperone capable of interacting with polypeptide segments of folding glycoproteins.

Supplier: Enzo Life Sciences

Sensitive, rapid ELISA kit to quantify human plasminogen, a glycoprotein involved in the dissolution of fibrin blood clots.

Supplier: Enzo Life Sciences

Ultra sensitive (1,2 pg/ml) ELISA kit, enabling reduced input sample and matrix interference, for the quantification of KIM-1, an early biomarker for kidney injury or disease.

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.

Supplier: Enzo Life Sciences

Highly sensitive ELISA kit for the detection of Arg8-Vasopressin in serum, plasma and tissue culture media.

Supplier: Enzo Life Sciences

Produced in E. coli. Human BAG-1S is fused at the N-terminus to a GST and His-tag.

Supplier: Enzo Life Sciences

The tetrapeptide KDEL, located at the carboxy-terminal sequences of luminal proteins, is a retrieval motif essential for the precise sorting of these proteins along the secretory pathway. KDEL proteins perform essential functions in the endoplasmic reticulum (ER) related to protein folding as well as assembly. The localization of chaperones and other soluble proteins to the ER is achieved by their continuous retrieval from post-ER compartments by the KDEL receptor (Erd2p), which is a membrane protein localized in the Golgi apparatus.

Supplier: Enzo Life Sciences

Protein phosphorylation is a complex biochemical process that is regulated by protein kinases that catalyze the transfer of the gamma-P of ATP to a recipient protein that acts as a substrate. This post-translational modification is primarily directed onto serine, threonine, and tyrosine amino acid residues within a protein. Changes in the phosphorylation status of phosphoproteins can alter their biological function, and aberrations in signal transduction cascades have been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders.

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.

Supplier: Enzo Life Sciences

Arachidonic acid uptake inhibitor

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.

Supplier: Enzo Life Sciences

The ALP (antileukoproteinase) or SLPI (secretory leukocyte peptidase inhibitor) protein is a secreted inhibitor which protects epithelial tissues from serine proteases. It is found in various secretions including seminal plasma, cervical mucus, and bronchial secretions, and has affinity for trypsin, leukocyte elastase, and cathepsin G. Its inhibitory effect contributes to the immune response by protecting epithelial surfaces from attack by endogenous proteolytic enzymes. The ALP protein is also thought to have broad-spectrum antibiotic activity.

Supplier: Enzo Life Sciences

This protein belongs to the serine protease family. The encoded protein contains a serine protease domain, a transmembrane domain, an LDL receptor-like domain, and a scavenger receptor cysteine-rich domain. Serine proteases are known to be involved in a variety of biological processes, whose malfunction often leads to human diseases and disorders. This protein was identified by its association with both congenital and childhood onset autosomal recessive deafness. This protein is expressed in fetal cochlea and many other tissues, and is thought to be involved in the development and maintenance of the inner ear or the contents of the perilymph and endolymph. This protein was also identified as a tumor-associated gene that is overexpressed in ovarian tumors. Alternatively spliced transcript variants have been described.

Supplier: Enzo Life Sciences

The ALP (antileukoproteinase) or SLPI (secretory leukocyte peptidase inhibitor) protein is a secreted inhibitor which protects epithelial tissues from serine proteases. It is found in various secretions including seminal plasma, cervical mucus, and bronchial secretions, and has affinity for trypsin, leukocyte elastase, and cathepsin G. Its inhibitory effect contributes to the immune response by protecting epithelial surfaces from attack by endogenous proteolytic enzymes. The ALP protein is also thought to have broad-spectrum antibiotic activity.