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Catalog Number: (BOSSBS-8497R-CY5)

Supplier: Bioss

Description: RENBP is a 427 amino acid protein that is a proteinaceous renin inhibitor. In inhibiting renin, RENBP forms a complex with it; a high molecular weight renin. RENBP contains a leucine zipper domain, which is essential for its dimerization with renin. RENBP can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Sequences of porcine, human and rat renin-binding proteins are highly homologous. The RENBP gene is conserved in dog, mouse, rat and zebrafish, and maps to human chromosome Xq28 between DXS52 and G6PD. Rat Renbp is located on chromosome X at Xq37 close to marker DXWox3 and falls outside the BP QTL regions on chromosome X.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-8497R-CY3)

Supplier: Bioss

Description: RENBP is a 427 amino acid protein that is a proteinaceous renin inhibitor. In inhibiting renin, RENBP forms a complex with it; a high molecular weight renin. RENBP contains a leucine zipper domain, which is essential for its dimerization with renin. RENBP can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Sequences of porcine, human and rat renin-binding proteins are highly homologous. The RENBP gene is conserved in dog, mouse, rat and zebrafish, and maps to human chromosome Xq28 between DXS52 and G6PD. Rat Renbp is located on chromosome X at Xq37 close to marker DXWox3 and falls outside the BP QTL regions on chromosome X.

UOM: 1 * 100 µl

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Catalog Number: (CPSD8566691)

Supplier: CAPITAL SAFETY

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: (BOSSBS-8497R-A647)

Supplier: Bioss

Description: RENBP is a 427 amino acid protein that is a proteinaceous renin inhibitor. In inhibiting renin, RENBP forms a complex with it; a high molecular weight renin. RENBP contains a leucine zipper domain, which is essential for its dimerization with renin. RENBP can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Sequences of porcine, human and rat renin-binding proteins are highly homologous. The RENBP gene is conserved in dog, mouse, rat and zebrafish, and maps to human chromosome Xq28 between DXS52 and G6PD. Rat Renbp is located on chromosome X at Xq37 close to marker DXWox3 and falls outside the BP QTL regions on chromosome X.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-8497R-A350)

Supplier: Bioss

Description: RENBP is a 427 amino acid protein that is a proteinaceous renin inhibitor. In inhibiting renin, RENBP forms a complex with it; a high molecular weight renin. RENBP contains a leucine zipper domain, which is essential for its dimerization with renin. RENBP can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Sequences of porcine, human and rat renin-binding proteins are highly homologous. The RENBP gene is conserved in dog, mouse, rat and zebrafish, and maps to human chromosome Xq28 between DXS52 and G6PD. Rat Renbp is located on chromosome X at Xq37 close to marker DXWox3 and falls outside the BP QTL regions on chromosome X.

UOM: 1 * 100 µl

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Supplier: CAPITAL SAFETY

Description: Protecta® Cabloc® Vertical Lifeline System consists of an 8 mm cable which is terminated at the top by a cable ferrule and cable clamps at the bottom.

Catalog Number: (PERCPER191010)

Supplier: PerkinElmer

Description: Reduce incidence of sample carry-over when cleaning with the Spolett Falling Number tube cleaner.

UOM: 1 * 1 items

New Product Sale

Supplier: CAPITAL SAFETY

Description: The Rollgliss R350 system provides efficient hauling, but more importantly, very controlled lowering (a finger and thumb are all that is required to hold a load). This system also allows to change the hauling ratios on the fly with quick release pulleys, allowing custom rigging for different applications and jobsites.

Catalog Number: (BOSSBS-8497R-CY5.5)

Supplier: Bioss

Description: RENBP is a 427 amino acid protein that is a proteinaceous renin inhibitor. In inhibiting renin, RENBP forms a complex with it; a high molecular weight renin. RENBP contains a leucine zipper domain, which is essential for its dimerization with renin. RENBP can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Sequences of porcine, human and rat renin-binding proteins are highly homologous. The RENBP gene is conserved in dog, mouse, rat and zebrafish, and maps to human chromosome Xq28 between DXS52 and G6PD. Rat Renbp is located on chromosome X at Xq37 close to marker DXWox3 and falls outside the BP QTL regions on chromosome X.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-8497R-FITC)

Supplier: Bioss

Description: RENBP is a 427 amino acid protein that is a proteinaceous renin inhibitor. In inhibiting renin, RENBP forms a complex with it; a high molecular weight renin. RENBP contains a leucine zipper domain, which is essential for its dimerization with renin. RENBP can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Sequences of porcine, human and rat renin-binding proteins are highly homologous. The RENBP gene is conserved in dog, mouse, rat and zebrafish, and maps to human chromosome Xq28 between DXS52 and G6PD. Rat Renbp is located on chromosome X at Xq37 close to marker DXWox3 and falls outside the BP QTL regions on chromosome X.

UOM: 1 * 100 µl

Sale

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

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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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Catalog Number: (BOSSBS-12260R-FITC)

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: (CPSD8000118)

Supplier: CAPITAL SAFETY

Description: The DBI-SALA® Confined space HC (high capacity) short reach davit system is constructed of powder-coated aluminium, and features a modular design for easy transport and storage. The system is adjustable, providing flexibility during installation.

UOM: 1 * 1 SET

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Catalog Number: (PRTWFP13RER)

Supplier: Portwest

Description: Fall Protection is put in place to prevent the risks associated with falling from heights, reducing impact force, restricting obstacle/ground collision and restricting users from fall hazard areas.

UOM: 1 * 1 items

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Catalog Number: (BOSSBS-12260R)

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