14670 Results for: "ENZO LIFE SCIENCES"

Supplier: Enzo Life Sciences

The multifunctional, multi-compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the soluble paralog of the ER membrane protein Calnexin (Cnx). Crts three domains include a 180 residue N-terminal domain, a proline-rich P-domain (residues 189-288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P-domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N-glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

Supplier: Enzo Life Sciences

Hsp47, also known as colligin and gp46, is an ER-resident collagen-specific stress glycoprotein involved in the synthesis and assembly of varoius collagens as a molecular chaperone.

Supplier: Enzo Life Sciences

Calreticulin (CRT) is a multifunctional, multi-compartmental protein most abundant in the ER lumen. CRT contains the ER-retrieval sequence, KDEL, and has been best characterized as a soluble molecular chaperone of new or misfolded proteins and a Ca2+- binding protein. Both CRT and its membrane bound homolog, Calnexin (CNX) interact with proteins and glycoproteins that have monoglucosylated N-glycans. The CRT/CNX cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligimerization, regulates ER degradation, and provides quality control by preventing incompletely folded glycoproteins from exiting to the Golgi complex.

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

Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.

Supplier: Enzo Life Sciences

The Hsp60 of Heliothis viescens belongs to a highly conserved family of molecular chaperones from several species, including plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60, and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix, and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria share a common ancestry (>1 billion years), and this coupled with the high degree of homology between the divergent Hsp60s suggests that these proteins perform a primitive but vital function similar to all the different species. The common characteristics shared by the Hsp60s from the divergent species include high abundance; induction with environmental stress such as heat shock; homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP; ATPase activity; and a role in folding and assembly of oligomeric protein structures. Studies support these similarities, showing expression of the single-ring human mitochondrial homolog Hsp60 with its co-chaperonin Hsp10, in a E. coli strain engineered so that the groE operon remained under strict regulatory control. The findings demonstrate that expression of Hsp60-Hsp10 enabled successful performance of all essential in vivo functions of GroEL and its co-chaperonin, GroES. Consistent with their functions as chaperones, Hsp60 and Hsp10 may act as docking molecules with a passive role in the maturation of caspase processing. Data incidates that recombinant Hsp60 and Hsp10 accelerate the activation of procaspase-3 by cytochrome c and dATP in an ATP-dependent manner. Hsps are intracellular proteins thought to serve protective functions against infection and cellular stress; however, several studies reveal a possible link between members of the Hsp60 and a number of autoimmune diseases, atherosclerosis, and chlamydial disease.

Supplier: Enzo Life Sciences

Calreticulin (CRT) is a multifunctional, multi-compartmental protein most abundant in the ER lumen. CRT contains the ER-retrieval sequence, KDEL, and has been best characterized as a soluble molecular chaperone of new or misfolded proteins and a Ca2+- binding protein. Both CRT and its membrane bound homolog, Calnexin (CNX) interact with proteins and glycoproteins that have monoglucosylated N-glycans. The CRT/CNX cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligimerization, regulates ER degradation, and provides quality control by preventing incompletely folded glycoproteins from exiting to the Golgi complex.

Supplier: Enzo Life Sciences

Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.

Supplier: Enzo Life Sciences

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

Hip (Hsc70-interacting protein) is a cytosolic protein that exists as a homo-oligomer and participates in the regulation of Hsc70 in eukaryotic cells. Hip interacts with the ATPase domain of Hsc70 molecules through its tetratricopeptide repeats and flanking charged alpha-helices. Upon binding to Hsc70, Hip stabilizes the ADP-bound state of Hsc70, a conformation that has a high affinity for unfolded substrate proteins. Together with Hsp40 and BAG-1, Hip may regulate the chaperone activity of Hsc70 by stabilizing the chaperone-substrate complex.

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Produced in E. coli.

Supplier: Enzo Life Sciences

HSFs (Heat Shock family of transcription factors), which consists of HSF 1-4, bind to highly conserved Heat shock elements (HSEs) in the promoter regions of heat shock genes, ultimately regulating the expression of Heat shock proteins (Hsps). On exposure to heat shock and other stresses, HSF1 localizes within seconds to discrete nuclear granules and on recovery from stress, HSF1 rapidly dissipates from the stress granules to a diffuse nucleoplasmic distribution.

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Produced in E. coli.

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Enzo Life Sciences

Hsp40/Hdj1 is a cytosolic co-chaperone belonging to the class DnaJ, named after its homolog in E. coli. Hsp40 functions in protein folding by binding nascent peptides and unfolded substrates and facilitating substrate interaction with Hsp70.

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 Hsp90α and Hsp90β, encoded by separate genes. The amino acid sequences of human and yeast Hsp90-alpha are 85% and 90% homologous to those of Hsp90β , 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 to 2% of all cellular proteins in most cells. Hsp90 functions as part of the cell’s powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control. In this context, researchers identified key regulatory proteins as substrates of Hsp90, including steroid receptors, cell cycle kinases involved in signal transduction, and p53. Hsp90 may act as a capacitor for morphological evolution by buffering widespread variation, potentially affecting morphogenic pathways. When temperature and other stress factors compromise Drosophila Hsp90 buffering, cryptic variant expression occurs, and selection can lead to the continued expression of these traits even after Hsp90 function is restored.

Supplier: Enzo Life Sciences

Produced in E.coli.

Supplier: Enzo Life Sciences

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.

Supplier: Enzo Life Sciences

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.

Supplier: Enzo Life Sciences

Disrupts Wnt signaling

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Catenin blocker

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SignaSure® Wash Buffer is formulated for use with alkaline phosphatase-linked detection reagent assay systems.

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Host: Mouse, Isotype: IgG1

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PATHO-GENE® HPV type 16/18/31/33/51 probe is a mixture of biotin-labeled HPV-16, HPV- 18, HPV-31, HPV-33 and HPV-51 specific probes in buffered formamide and hybridisation enhancers.

Supplier: Enzo Life Sciences

In situ hybridisation buffer for HPV probes (ready-to use) provides a high quality hybridisation medium for In situ hybridisation analyses using either DNA or oligonucleotide probes labeled with biotin-, or fluorescein-modified nucleotides.

Supplier: Enzo Life Sciences

The PATHO-GENE® Human papillomavirus (HPV) in situ screening assay for tissue sections provides reagents and materials for (a) preparation and pretreatment and (b) hybridization/ detection and typing of HPV DNA (using alkaline phosphatase-NBT/BCIP for signal generation) in 20 tissue biopsy specimens. This product is for research use only and is not to be used for diagnostic procedures.

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Amine reactive dye

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Cyanine 3-UTP (Enhanced) can replace UTP as a substrate for T7 RNA polymerase in labeling systems that generate labeled probes through in vitro transcription. Probes generated by these methods are suitable for multicolor fluorescence analysis, specifically dual-color expression arrays in conjunction with cyanine 3-UTP .

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Cyanine 5-dUTP can replace TTP in reactions in which it serves as a substrate for E. coli DNA polymerase (holoenzyme and Klenow fragment), T4 and Taq DNA polymerases, reverse transcriptase (from AMV and M-MuLV) and terminal transferase. Fluorescently labeled probes can be prepared with this fluorescent nucleotide by a variety of methods including nick translation, cDNA labeling and 3’-end labeling. Probes generated by these methods are suitable for use for the identification of specific sequences by in situ hybridization procedures on fixed cells and tissues by direct fluorescence detection. Cyanine 5-dUTP can also be used for multicolor fluorescence labeling.

Supplier: Enzo Life Sciences

Mixture of fluorescent dyes for detection of lysosomes, mitochondria and nucleic acids