You Searched For: Heat+Block

Catalog Number: (10257-864)

Supplier: Bioss

Description: A mutation of the DYT1 gene, which codes for TorsinA, has been identified as the cause of one form of autosomal dominantly inherited dystonia. Early-onset torsion dystonia is a movement disorder, characterized by twisting muscle contractures, that begins in childhood. Symptoms are believed to result from altered neuronal communication in the basal ganglia. TorsinA comprises 332 amino acids. TorsinA is widely expressed throughout the mouse central nervous system and is detected in the majority of neurons in nearly all regions. The proteins display cytoplasmic distribution, although in some types of neurons localization is perinuclear. TorsinA often performs chaperone-like functions that assist in the assembly, operation, or dis-assembly of protein complexes. The gene which encodes TorsinA has high homology to three additional mammalian genes and a nematode gene and distal similarity to the family of heat-shock proteins and the Clp protease family. The gene which encodes TorsinA maps to human chromosome 9q34.

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Catalog Number: (97062-538)

Supplier: VWR

Description: Offers blocking and hybridization for optimized complimentary base pairing of DNA and RNA in Southern blot, Northern blot, dot blot, colony and in situ hybridization.

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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.

Catalog Number: (89359-280)

Supplier: Genetex

Description: Heme oxygenase (HO) is a microsomal enzyme that catalyzes the oxidation of heme to the antioxidant molecules, biliverdin and carbon monoxide. HO consists of two homologous isozymes, an inducible HO1 and a constitutively expressed HO2. HO1 is induced by a wide variety of stimuli including conditions of oxidative stress, inflammatory agents, transforming growth factor beta and heat shock. The increase in expression of HO1 is thought to be a cellular defense mechanism against oxidative stress since elevated HO could eventually generate more bilirubin, an anti-oxidant.

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Catalog Number: (103278-378)

Supplier: Novus Biologicals

Description: The HspA1L Antibody from Novus Biologicals is a rabbit polyclonal antibody to HspA1L. This antibody reacts with human, mouse, rat. The HspA1L Antibody has been validated for the following applications: Western Blot, Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunohistochemistry-Paraffin.

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Catalog Number: (10364-036)

Supplier: Bioss

Description: Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK-1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1. Phosphorylates heat shock factor protein 4(HSF4) (By similarity). Highest levels within the nervous system, expressed in different tissues, mostly in intestine, placenta and lung. Increased expression during development. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

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Catalog Number: (10364-028)

Supplier: Bioss

Description: Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK-1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1. Phosphorylates heat shock factor protein 4(HSF4) (By similarity). Highest levels within the nervous system, expressed in different tissues, mostly in intestine, placenta and lung. Increased expression during development. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

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Catalog Number: (103328-584)

Supplier: Novus Biologicals

Description: The HSF1 Antibody (1A11) from Novus Biologicals is a mouse monoclonal antibody to HSF1. This antibody reacts with human. The HSF1 Antibody (1A11) has been validated for the following applications: Western Blot, ELISA, Immunocytochemistry / Immunofluorescence.

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Supplier: GE Healthcare - HyClone

Description: HyClone™ charcoal/dextran treated foetal bovine serum (FBS) is available for users requiring reduced levels of various hormones. High quality FBS is processed using a charcoal/dextran treatment that has been shown to reduce the levels of many hormones and growth factors.

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Catalog Number: (10050-188)

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.

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Catalog Number: (77395-200)

Supplier: Arlington Scientific

Description: A universal blocking reagent supplied in PBS for diagnostic and research systems.

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Supplier: G-Biosciences

Description: G-Biosciences' Protein-Free™ Blocking Buffer does not contain protein; it is a proprietary formation of non-protein agents that eliminates non-specific binding sites in ELISA, blotting, immunohistochemistry and other applications

Supplier: Foamtec International

Description: This triple-layered wipe is designed to aid decontamination procedures in pharmaceutical and medical device manufacturing facilities.Can hold 8 to 10× the volume of fluid compared to other wipes allowing for much quicker application of cleaning fluids to large areas such as glass windows, stainless steel tanks and piping.

Catalog Number: (10462-460)

Supplier: Bioss

Description: The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJB2 (DnaJ homolog subfamily B member 2), also known as HSJ1 or HSPF3, is expressed almost exclusively in the brain, with the highest levels in the frontal cortex and hippocampus. Two isoforms are produced due to alternative splicing.

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Catalog Number: (10462-466)

Supplier: Bioss

Description: The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJB2 (DnaJ homolog subfamily B member 2), also known as HSJ1 or HSPF3, is expressed almost exclusively in the brain, with the highest levels in the frontal cortex and hippocampus. Two isoforms are produced due to alternative splicing.

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Supplier: Enzo Life Sciences

Description: 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.

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