You Searched For: Fall+Lanyards+and+Ropes

Catalog Number: (HAMI204880)

Supplier: HAMILTON BONADUZ

Description: This brushed stainless steel rack is used for clean and safe storage of syringes with plastic holder. A lip on the plastic holder protects the syringe against accidental touching and falling down. The distance of the plastic holder prevents the syringe from getting in contact with the metal plate.

UOM: 1 * 1 items

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Supplier: HONEYWELL SAFETY

Description: The anchorage connectors and karabiners are used for securing an intermediate attachment to an anchorage point.

Supplier: CAPITAL SAFETY

Description: These Protecta® Rebel™ Web self-retracting lifelines provide an economical fall protection solution without compromising on performance or safety. They are available in a range of lengths to meet the specific needs of jobsites. Lifelines are available in a super-tough nylon housing comprised of 25 mm polyester webbing, or in a durable, lightweight thermoplastic housing comprised of galvanised steel.

Supplier: 3M

Description: 3M DBI-SALA ExoFit XE200 harness with rescue loops, automatic buckles, two sizes. X-shaped chest straps with central D-ring attachment point optimised position on the body. Revolver adjuster for the torso length for a quick, secure and comfortable fit of the harness.

Catalog Number: (BOSSBS-12867R-A555)

Supplier: Bioss

Description: The steroid receptor superfamily acts through direct association with DNA sequences known as hormone response elements (HREs) and binds DNA as either homo- or heterodimers. The promiscuous mediator of heterodimerization, RXR, is the receptor for 9-cis retinoic acid, and dimerizes with VDR, TR, PPAR, and several novel receptors including LXR (also referred to as RLD-1) and FXR. FXR and LXR fall into a category of proteins termed “orphan receptors” because of their lack of a defined function, and in the case of LXR, the lack of a defined ligand. FXR has been shown to bind a class of lipid molecules called farnesoids. LXR/RXR heterodimers have highest affinity for DR-4 DNA elements while FXR/RXR heterodimers bind IR-1 elements. Both LXR/RXR and FXR/RXR heterodimers retain their responsiveness to 9-cis retinoic acid.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12260R-CY3)

Supplier: Bioss

Description: The proteasome represents a large protein complex that exists inside all eukaryotes and archaea, and in some bacteria. The main function of proteasomes is to degrade unnecessary or damaged proteins by proteolysis. The most common form of the proteasome, known as the 26S Proteasome, contains one 20S Proteasome core particle structure and two 19S regulatory caps. The 20S Proteasome core is hollow and forms an enclosed cavity, where proteins are degraded, as well as openings at the two ends to allow the target protein to enter. The 20S Proteasome core particle contains many subunits, depending on the organism. All of the subunits fall into one of two types: alpha subunits, which are structural, serve as docking domains for the regulatory particles and exterior gates blocking unregulated access to the interior cavity; or beta subunits, which are predominantly catalytic. The outer two rings in the proteasome consist of seven ?subunits each, and the inner two rings each consist of seven beta subunits.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6669R-A488)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6669R-A647)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10438R)

Supplier: Bioss

Description: This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9430R-HRP)

Supplier: Bioss

Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

UOM: 1 * 100 µl

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Catalog Number: (113-1250)

Supplier: HONEYWELL SAFETY

Description: This detachable climbers seat offers a comfortable supported position for the operator during prolonged periods suspended at height. It is made from marine ply covered with closed cell foam and abrasion resistant PVC coated nylon.

UOM: 1 * 1 items

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Catalog Number: (BOSSBS-6669R)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-12260R-A750)

Supplier: Bioss

Description: The proteasome represents a large protein complex that exists inside all eukaryotes and archaea, and in some bacteria. The main function of proteasomes is to degrade unnecessary or damaged proteins by proteolysis. The most common form of the proteasome, known as the 26S Proteasome, contains one 20S Proteasome core particle structure and two 19S regulatory caps. The 20S Proteasome core is hollow and forms an enclosed cavity, where proteins are degraded, as well as openings at the two ends to allow the target protein to enter. The 20S Proteasome core particle contains many subunits, depending on the organism. All of the subunits fall into one of two types: alpha subunits, which are structural, serve as docking domains for the regulatory particles and exterior gates blocking unregulated access to the interior cavity; or beta subunits, which are predominantly catalytic. The outer two rings in the proteasome consist of seven subunits each, and the inner two rings each consist of seven beta subunits.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-6669R-CY7)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (1–3), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerize with members of the class A and B HLH proteins (1–5). Due to the absence of the basic region, the resulting heterodimers cannot bind DNA. The Id-type proteins thus appear to negatively regulate DNA binding of bHLH proteins. Since Id1 inhibits DNA binding of E12 and Myo D, it apparently functions to inhibit muscle-specific gene expression. Under conditions that facilitate muscle cell differentiation, the Id protein levels fall, allowing E12 and/or E47 to form heterodimers with Myo D and myogenin, which in turn activate myogenic differentiation. It has been shown that expression of each of the Id proteins is strongly dependent on growth factor activation and that reduction of Id mRNA levels by antisense oligonucleotides leads to a delayed reentry of arrested cells into the cell cycle following growth factor stimulation.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-12260R-A350)

Supplier: Bioss

Description: The proteasome represents a large protein complex that exists inside all eukaryotes and archaea, and in some bacteria. The main function of proteasomes is to degrade unnecessary or damaged proteins by proteolysis. The most common form of the proteasome, known as the 26S Proteasome, contains one 20S Proteasome core particle structure and two 19S regulatory caps. The 20S Proteasome core is hollow and forms an enclosed cavity, where proteins are degraded, as well as openings at the two ends to allow the target protein to enter. The 20S Proteasome core particle contains many subunits, depending on the organism. All of the subunits fall into one of two types: alpha subunits, which are structural, serve as docking domains for the regulatory particles and exterior gates blocking unregulated access to the interior cavity; or beta subunits, which are predominantly catalytic. The outer two rings in the proteasome consist of seven ?subunits each, and the inner two rings each consist of seven beta subunits.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-10438R-CY3)

Supplier: Bioss

Description: This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

UOM: 1 * 100 µl

Sale