You Searched For: Fall+Arresters

Catalog Number: (1002871.)

Supplier: HONEYWELL SAFETY

Description: Extremely light personal fall arrester comes with with a compact plastic housing and a rectractable webbing lifeline.

UOM: 1 * 1 items

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Supplier: Portwest

Description: Kit includes two-point harness, carabiner, 12 mm detachable rope grab, 10 m kernmantle static rope, and nylon drawstring bag.

Catalog Number: (BOSSBS-6669R-CY3)

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-CY5)

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-A350)

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-6669R-A555)

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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Supplier: CAPITAL SAFETY DEUTSCHLAND

Description: Tripod with adjustable locking legs, safety chains, top pulley and winch bracket.

Catalog Number: (1005330.)

Supplier: HONEYWELL SAFETY

Description: Brackets for fixing the fall arrest blocks to the tripod.

UOM: 1 * 1 items

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Catalog Number: (CPSD8566691)

Supplier: CAPITAL SAFETY DEUTSCHLAND

Description: The portable fall arrest post is a durable aluminium construction and specifically designed for use on top of transformers or other types of vertical platforms with potential fall hazards.

UOM: 1 * 1 items

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Catalog Number: (CPSD1500104)

Supplier: CAPITAL SAFETY DEUTSCHLAND

Description: Single tool harness holster with retractor.

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-6669R-A680)

Supplier: Bioss

Description: Members of the Id family of basic helix-loop-helix (bHLH) proteins include Id1 (13), Id2 (4), Id3 and Id4 (5). They are ubiquitously expressed and dimerise with members of the class A and B HLH proteins (15). 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-6669R-CY5.5)

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: (CPSD1500003)

Supplier: CAPITAL SAFETY DEUTSCHLAND

Description: D-rings can be attached to virtually any tool under 2,3 kg (5 lbs.) or 0,9 kg (2 lbs.) by using Quick-Wrap Tape.

UOM: 1 * 1 items

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Supplier: CAPITAL SAFETY DEUTSCHLAND

Description: Sealed-Blok™ family has the most comprehensive line of sealed SRLs in the industry and decades of proven field service in the toughest environments.

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

Sale