You Searched For: esd+protection

Catalog Number: (10371-072)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

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Catalog Number: (10748-598)

Supplier: Prosci

Description: Bik Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells and is caused by the activation of proteolytic enzymes termed caspases. Proteins that comprise the Bcl-2 family appear to control the activation of these enzymes. One such protein BIK was recently identified as an endoplasmic reticulum (ER)-residing pro-apoptotic member of the Bcl-2 homology domain-3 (BH3)-only group of the Bcl-2 family that stimulates mitochondrial release of cytochrome c following p53 induction of apoptosis. A significant fraction of BIK is found as an ER transmembrane protein, with most of the protein facing the cytosol. Restricting BIK to the ER membrane by replacing the transmembrane region with that of the ER-selective membrane anchor of cytochrome b resulted in a decreased cytochrome c release from mitochondria and a corresponding drop in cell death. Recent evidence suggests that BIK cooperates with NOXA, another BH3-only protein, to somehow enhance the activation of Bax to stimulate the rapid release of cytochrome c from mitochondria.

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Catalog Number: (76324-122)

Supplier: Safety & Industrial Supplies

Description: FACE SHIELD F10 34-0AP CLR 15 1/2IN CS50

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Catalog Number: (10110-568)

Supplier: Prosci

Description: PHF6 is a member of the plant homeodomain (PHD)-like finger (PHF) family. PHF6 is a protein with two PHD-type zinc finger domains, indicating a potential role in transcriptional regulation, that localizes to the nucleolus. Mutations affecting the coding region of its gene or the splicing of the transcript have been associated with Borjeson-Forssman-Lehmann syndrome (BFLS).This gene is a member of the plant homeodomain (PHD)-like finger (PHF) family. It encodes a protein with two PHD-type zinc finger domains, indicating a potential role in transcriptional regulation, that localizes to the nucleolus. Mutations affecting the coding region of this gene or the splicing of the transcript have been associated with Borjeson-Forssman-Lehmann syndrome (BFLS), a disorder characterized by mental retardation, epilepsy, hypogonadism, hypometabolism, obesity, swelling of subcutaneous tissue of the face, narrow palpebral fissures, and large ears. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

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Catalog Number: (95044-738)

Supplier: GE Healthcare - Life Sciences

Description: The key to reproducible electrophoresis results is temperature control. Gels cooled on their two faces produce slanted bands appearing as broad or double bands in stained gels. SE 600 Ruby ensures uniform heat in gels because, the gels are immersed in the lower buffer for uniform heat transfer and a standard magnetic stirrer circulates buffer around the vertically suspended heat exchanger to maintain homogeneous lower buffer temperature. The ergonomic SE 600 Ruby provides two built-in side handles, which facilitates carrying and handling. Run up to four gels (up to 112 samples) in a single run. Divider plates convert single-gel sandwiches into two-gel club sandwiches, which seal and fit into the casting stand like single gels. If gels longer than 16-cm are required, Cytiva offers the SE 660, which runs gels up to 24 cm. Except for gel lengt, the SE 660 has identical features to those of SE 600 Ruby.

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Catalog Number: (10782-546)

Supplier: Biosensis

Description: FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer composed of two large adaptins (gamma1/AP1G1 or gamma2/AP1G2 and beta1A/AP1B1 or beta1B/AP1B1), a medium adaptin (mu1A/AP1M1 or mu1B/AP1M2) and a small adaptin (sigma1A/AP1S1 or sigma1B/AP1S2 or sigma1C/AP1S3). SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle; cytoplasmic vesicle membrane; peripheral membrane protein; cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Widely expressed. DISEASE: Deletion of the AP1B1 gene may play a role in the tumorigenesis of meningiomas. SIMILARITY: Belongs to the adaptor complexes large subunit family.

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Catalog Number: (470203-832)

Supplier: Pope Scientific

Description: <B>Pope Lab Grade Dewars are rated the most efficient glass Dewars in the World!</B><BR>This superior ranking is due to rigid quality controls in manufacture and a number of outstanding design and manufacturing features.<BR>Efficiency assured by rigid bakeout and evacuation control (evacuated to 10-5 torr or better).<BR>Evacuation tip completely shielded for increased protection.<BR>Weighted bases on all models for stability<BR>No pads between walls on cylindrical Dewars eliminating this heat transfer potential<BR>Supplied stopper (polyethylene) tops off Dewars to minimize evaporation<BR>This 1000mL flask is has a full base with metal handle and a cylindrical wide mouth. The unsilvered glass of 47369-01 allows you to see what happens when you emerge an item into the liquid nitrogen. Features an aluminum housing and sturdy mesh cover to faciliate a firm grip and increased protection. All Pope Lab Grade Dewars are manufactured of borosilicate glass for liquid nitrogen service.<BR>Dimensions:<BR>-ID 7cm<BR>-Inside Depth 30.2 cm<BR>-OD 8.6 cm<BR>-Total Height 33.7 cm

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Supplier: Honeywell Safety Products

Description: Unique shape and style provide excellent eye protection in a variety of frames and lenses.

Catalog Number: (10394-964)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.

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Catalog Number: (10394-966)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.

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Catalog Number: (30624-392)

Supplier: W.S. Tyler

Description: SHIELD

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Catalog Number: (10388-024)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.

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Catalog Number: (10394-968)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.

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Catalog Number: (75934-096)

Supplier: Rockland Immunochemical

Description: PINK1 (PTEN induced putative kinase 1) is a mitochondrial serine/threonine kinase which maintains mitochondrial function/integrity, provides protection against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins, and is involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). PINK1 is synthesized as a 63 kD protein which undergoes proteolyt processing to generate at least two cleaved forms (55 kD and 42 kD). PINK1 and its substrates have been found in the cytosol as well as in different sub-mitochondrial compartments, and according to the recent reports; PINK1 may be targeted to OMM (outer mitochondrial membrane) with its kinase domain facing the cytosol, providing a possible explanation for the observed physical interaction with the cytosolic E3 ubiquitin ligase Parkin.
Defective PINK1 may cause alterations in processing, stability, localization and activity as well as binding to substrates/interaction-partners which ultimately leads to differential effects on mitochondrial function and morphology. Mutations in PINK1 are linked to autosomal recessive early onset Parkinson's disease, and are associated with loss of protective function, mitochondrial dysfunction, aggregation of alpha-synuclein, as well as proteasome dysfunction. Areas of interest and use for researchers include Neuroscience, mitochondrial function, and CDK-mediated phosphorylation pathways.

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Catalog Number: (75934-100)

Supplier: Rockland Immunochemical

Description: PINK1 (PTEN induced putative kinase 1) is a mitochondrial serine/threonine kinase which maintains mitochondrial function/integrity, provides protection against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins, and is involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). PINK1 is synthesized as a 63 kD protein which undergoes proteolyt processing to generate at least two cleaved forms (55 kD and 42 kD). PINK1 and its substrates have been found in the cytosol as well as in different sub-mitochondrial compartments, and according to the recent reports; PINK1 may be targeted to OMM (outer mitochondrial membrane) with its kinase domain facing the cytosol, providing a possible explanation for the observed physical interaction with the cytosolic E3 ubiquitin ligase Parkin.
Defective PINK1 may cause alterations in processing, stability, localization and activity as well as binding to substrates/interaction-partners which ultimately leads to differential effects on mitochondrial function and morphology. Mutations in PINK1 are linked to autosomal recessive early onset Parkinson's disease, and are associated with loss of protective function, mitochondrial dysfunction, aggregation of alpha-synuclein, as well as proteasome dysfunction. Areas of interest and use for researchers include Neuroscience, mitochondrial function, and CDK-mediated phosphorylation pathways.

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Catalog Number: (10388-036)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction.

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