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Catalog Number: (10356-194)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta 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. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.

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Catalog Number: (76085-012)

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: (10356-284)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta 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. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.

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Catalog Number: (75931-002)

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: (75934-978)

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: (102971-626)

Supplier: Adipogen

Description: Microtubules are key elements of the eukaryotic cytoskeleton that dynamically assemble from heterodimers of alpha- and beta-tubulin. Two different mechanisms can generate microtubule diversity: the expression of different alpha- and beta-tubulin genes, referred to as tubulin isotypes, and the generation of posttranslational modifications (PTMs) on alpha- and beta-tubulin. Tubulin PTMs include the well-known acetylation or phosphorylation, and others that have so far mostly been found on tubulin, detyrosination/tyrosination, polyglutamylation and polyglycylation. These PTMs might have evolved to specifically regulate tubulin and microtubule functions. Tubulin acetylation was discovered on K40 of flagellar alpha-tubulin in Chlamydomonas reinhardtii and is generally enriched on stable microtubules in cells. It is located on the microtubule lumenal surface. As a result of its localization at the inner face of microtubules, K40 acetylation might rather affect the binding of microtubule inner proteins, a poorly characterized family of proteins. Functional experiments in cells have further suggested that K40 acetylation regulates intracellular transport by regulating the traffic of kinesin motors probably by indirect mechanisms. Acetyltransferase alpha-Tat1 (or Mec-17) specifically acetylate alpha-tubulin K40. Acetylation of tubulin by alpha-Tat1 accumulates selectively in stable, long-lived microtubules thus explaining the link between this posttranslational modication and stable microtubules in cells. However, the direct cellular function of K40 acetylation on microtubules is still unclear.

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Catalog Number: (75934-098)

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: (75934-980)

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: (10388-034)

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: (10388-038)

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: (104086-848)

Supplier: HACH CO MS

Description: SAFETY SHIELD

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Catalog Number: (76085-014)

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: (10356-280)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta 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. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.

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Catalog Number: (10356-282)

Supplier: Bioss

Description: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta 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. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.

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Catalog Number: (MFLX00015-BN)

Supplier: AALBORG INSTRUMENTS & CONTROL

Description: FRONT SHIELD

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Catalog Number: (MSPP-T1388410)

Supplier: TARGETMOL CHEMICALS INC. MS

Description: SHIELD-1 10MG

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