You Searched For: Heat+Block

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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Catalog Number: (10084-596)

Supplier: Proteintech

Description: CIRBP, also named as A18HNRNP and CIRP, is a cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP is also involved in cap-independent translation upon moderate cold-shock. It acts as a translational activator. CIRBP is a suppressive rather stimulatory effect on proliferation. CIRBP can translocate from nucleus to cytoplasm under stresses such as UV irradation or heat shock. Suppression of CIRBP increased the apoptotic cell population of neural stem cells at moderate low temperature. This antibody (Catalog# 10209-2-AP) is a rabbit polyclonal antibody raised against the full-length CIRBP of human origin.

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Supplier: Biotium

Description: The TrueBlack® WB blocking buffer kit is a ready-to-use buffer system that provides optimal specificity, sensitivity, and background signal suppression for fluorescence-based western blotting (WB).

Catalog Number: (89360-924)

Supplier: Genetex

Description: Mycobacterium tuberculosis is the most common cause of tuberculosis. Primary infection begins with inhalation of 1 to 10 aerosolised bacilli. The pathogenicity of the organism is determined by its ability to escape host immune responses as well as eliciting delayed hypersensitivity. Alveolar macrophages engulf the invading cells but are unable to mount an effective defense. Several virulence factors are responsible for this apparent failure; most notably in the mycobacterial cell wall are the cord factor, lipoarabinomannan, and the 65 kd heat shock protein or HSP65. The emergence of new strains of resistant Mycobacterium tuberculosis has created new interest in clinical diagnosis. Studies have shown immunohistochemical techniques to be superior to conventional special stains. Thus the demonstration of mycobacterial antigens are not only useful in establishing mycobacterial aetiology, but can also be used as an alternative method to the conventional Ziehl-Neelsen method.

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Supplier: Thermo Scientific Chemicals

Description: Liquid

SDS Certificates

Catalog Number: (10287-492)

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. DnaJA2 (DnaJ homolog subfamily A member 2), also known as HIRA-interacting protein 4 or cell cycle progression restoration gene 3 protein, contains one CR-type zinc finger and is a co-chaperone of HSC 70.

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Catalog Number: (10423-418)

Supplier: Bioss

Description: BAG5 is a member of the BAG1 related protein family. BAG1 is an anti apoptotic protein that functions through interactions with a variety of cell apoptosis and growth related proteins including BCL 2, Raf protein kinase, steroid hormone receptors, growth factor receptors and members of the heat shock protein 70 kDa family. A BAG domain near the C terminus, may bind and inhibit the chaperone activity of Hsc70/Hsp70. It has been hypothesized that the BAG5 protein will induce the death of nigral neurons through its predicted interaction with hsp70, which will cause increased protein aggregation and cell death by disinhibition of hsp70’s anti apoptotic function. It is believed that BAG5 will play an important role in the mechanisms of neuronal death. BAG5 may also be of interest due to its possible role as a modulator of the hsp70/hsp40 chaperone axis or its possible interaction and coordination of localization/modulation of other BAG containing proteins via BAG-BAGheterodimerization.

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Catalog Number: (10423-438)

Supplier: Bioss

Description: BAG5 is a member of the BAG1 related protein family. BAG1 is an anti apoptotic protein that functions through interactions with a variety of cell apoptosis and growth related proteins including BCL 2, Raf protein kinase, steroid hormone receptors, growth factor receptors and members of the heat shock protein 70 kDa family. A BAG domain near the C terminus, may bind and inhibit the chaperone activity of Hsc70/Hsp70. It has been hypothesized that the BAG5 protein will induce the death of nigral neurons through its predicted interaction with hsp70, which will cause increased protein aggregation and cell death by disinhibition of hsp70’s anti apoptotic function. It is believed that BAG5 will play an important role in the mechanisms of neuronal death. BAG5 may also be of interest due to its possible role as a modulator of the hsp70/hsp40 chaperone axis or its possible interaction and coordination of localization/modulation of other BAG containing proteins via BAG-BAGheterodimerization.

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Supplier: Rockland Immunochemical

Description: This blocking buffer is specifically formulated to achieve superior reproducible western blotting images using fluorescent systems.

Catalog Number: (100243-742)

Supplier: Southern Biotechnology

Description: The immunoglobulin heavy chain binding protein BiP is a member of the hsp70 family of heat shock proteins and is identical to the glucose regulated protein GRP78. While BiP was originally described for its function in B cells, it is now known to be distributed in a variety of tissues, if not ubiquitous. The highly conserved hsp70 proteins have an essential physiological role in stress responses and as “molecular chaperones” which are responsible for a variety of functions such as protein transport, prevention of protein toxicity and direction of protein folding. With regard to its immunological role, BiP is a component of the endoplasmic reticulum and binds free intracellular heavy chains in nonsecreting pre-B cell lines (μ+,L-) or incompletely assembled Ig precursors in H+L+ secreting hybridomas and myelomas. In the absence of light chain synthesis, heavy chains remain associated with BiP and are not secreted. BiP is an ATP binding protein and the dissociation of the BiP-heavy chain complex is probably driven by the ATPase activity attributed to BiP. The monoclonal antibody 76-E6 recognizes a conserved epitope localized within the region of amino acids 497 to 581 of BiP.

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Catalog Number: (10480-998)

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 in-volved in the regulation of protein degradation, exocytsis and endocytosis. DnaJC7 (DnaJ homolog subfamily C member 7), also known as TPR2, TTC2 or DANJC7, is ubiquitously expressed, with highest expression in testis, liver, heart and brain.

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Catalog Number: (76108-858)

Supplier: Bioss

Description: Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been shown to be involved in many different cellular functions, such as neuron channel activation, apoptosis, cardioprotection from ischemia, heat shock response, as well as insulin exocytosis. Knockout studies in mice suggest that this kinase is important for lipopolysaccharide (LPS)-mediated signaling in activated macrophages and may also play a role in controlling anxiety-like behavior.

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Catalog Number: (10663-886)

Supplier: Bioss

Description: Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been shown to be involved in many different cellular functions, such as neuron channel activation, apoptosis, cardioprotection from ischemia, heat shock response, as well as insulin exocytosis. Knockout studies in mice suggest that this kinase is important for lipopolysaccharide (LPS)-mediated signaling in activated macrophages and may also play a role in controlling anxiety-like behavior. [provided by RefSeq, Jul 2008].

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Catalog Number: (10330-436)

Supplier: Bioss

Description: Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been shown to be involved in many different cellular functions, such as neuron channel activation, apoptosis, cardioprotection from ischemia, heat shock response, as well as insulin exocytosis. Knockout studies in mice suggest that this kinase is important for lipopolysaccharide (LPS)-mediated signaling in activated macrophages and may also play a role in controlling anxiety-like behavior. [provided by RefSeq, Jul 2008]

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