You Searched For: Heat+Block

Catalog Number: (75793-426)

Supplier: Prosci

Description: Clusterin shares homology with the small heat shock protein family of molecular chaperones. The mature secreted form of the protein is a glycosylated, 80-kDa disulfide-linked heterodimer of alpha and beta subunits (produced by internal cleavage). Clusterin is expressed in virtually all tissues and found in all human fluids. It is involved in numerous physiological processes important for carcinogenesis and tumor growth, including apoptotic cell death, cell cycle regulation, DNA repair, cell adhesion, tissue remodeling, lipid transportation, membrane recycling, and immune system regulation. Clusterin also exists as a nuclear protein. The secreted form of Clusterin has extracellular chaperone and anti-apoptotic activities while the nuclear form acts as a proapoptotic factor.

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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.

Supplier: Heidolph NA, LLC

Description: 5 ml Flask Insert for Radleys StarFish Workstation. Adapter to accommodate 5 ml round bottom flasks. To be used with Polyblock 1 x 250ml.

Catalog Number: (47800-056)

Supplier: Heidolph NA, LLC

Description: 50 ml Flask Insert for Radleys StarFish Workstation. Adapter to accommodate 50 ml round bottom flasks. To be used with Polyblock 1 x 250ml.

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Supplier: Thermo Scientific

Description: These hot plates feature demand-type thermostat controls that will automatically reach and hold temperature to within ±3 °C (5 °F) at 100 °C (212 °F).

Catalog Number: (TWTX3213)

Supplier: Texwipe

Description: POLYSAT® wipers are made from 100% polypropylene and pre-wetted with 70% IPA.

SDS Certificates Sale

Supplier: Arlington Scientific

Description: A non-mammalian blocking reagent supplied in PBS for diagnostic systems involving membrane or other solid phase material.

Catalog Number: (76537-106)

Supplier: Corning

Description: Accessories for Corning® LSE™ Digital Dry Bath Heaters, Corning

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Supplier: Boekel

Supplier: Contec

Description: Quiltec® I Wipes offer the highest sorptive capacity of any sealed edge wipe available. They are manufactured using two layers of knitted polyester fabric that are laminated together to form a stronger, more adsorbent wipe. Additional fluid is captured within the quilted pockets between the fabric layers, increasing the sorbent capacity. Quiltec® I have more than twice the adsorbent capacity of a single-layer wipe.

Certificates

Catalog Number: (10103-142)

Supplier: Prosci

Description: HSPA4 (Hsp70) belongs to the heat shock protein 70 family. It was isolated as a putative Rictor interacting protein and interaction with membranes acts as a platform for its release into the extracellular environment during its recovery from stress. Hsp70 gene expression in Rheumatoid Arthitis-affected synovial tissue is followed by Hsp70 cell surface expression on fibroblast-like synovial cells growing from RA synovial tissue. Serum Hsp70 levels were increased in Systemic sclerosis patients, and associated with pulmonary fibrosis, skin sclerosis, renal vascular damage, oxidative stress, and inflammation.

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Catalog Number: (77440-670)

Supplier: Bioss

Description: Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Axonemal Dynein motors contain one to three non-identical heavy chains and cause a sliding of microtubules in the axonemes of cilia and flagella in a mechanism necessary for cilia to beat and propel the cell. DNAH1 (dynein heavy chain 1, axonemal), also known as heat shock regulated protein 1 or ciliary dynein heavy chain 1, is a 4,330 amino acid protein consisting of at least two heavy chains and several intermediate and light chains. Mutations in the gene encoding DNAH1 may be a cause of primary ciliary dyskinesia, also known as Kartagener Syndrome, which is characterized by chronic recurrent respiratory infections due to defective cilia action in the respiratory tract. There are three isoforms of DNAH1 that exist as a result of alternative splicing events.

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Supplier: Biotium

Description: This antibody recognizes a 24-27 kDa estrogen-regulated protein, identified as heat shock protein 27 (hsp27). Hsp27 was recently found to be identical to the estrogen-induced p29 and 24K protein. About 50% of breast carcinomas are positive for hsp27 especially those that are also positive for estrogen and/or progesterone receptor. HSP27 has also been implicated in drug resistance in cancer cells.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®488A is a green fluorescent dye (Ex/Em 490/515 nm) with excellent brightness and photostability. The dye is minimally charged for less non-specific binding. CF®488A also is compatible with super-resolution imaging by TIRF.

Catalog Number: (10285-494)

Supplier: Bioss

Description: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008].

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Catalog Number: (10323-524)

Supplier: Bioss

Description: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

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Catalog Number: (76078-996)

Supplier: Bioss

Description: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

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