You Searched For: Fall+Lanyards+and+Ropes

Catalog Number: (BOSSBS-12867R-A488)

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-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: (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: (PRSI92-326)

Supplier: ProSci Inc.

Description: Collagen alpha-1(III) chain（Col3a1） is a secreted protein and belongs to the fibrillar collagen family.It contains 1 fibrillar collagen NC1 domain and 1 VWFC domain. Collagen alpha-1(III) chain is a fibrillar collagen that is found in extensible connective tissues such as skin, lung, and the vascular system, frequently in association with type I collagen. The COL3A1 gene produces the components of type III collagen, called pro-alpha1(III) chains. Three copies of this chain combine to make a molecule of type III procollagen. These triple-stranded, rope-like procollagen molecules must be processed by enzymes outside the cell to remove extra protein segments from their ends. Once these molecules are processed, the collagen molecules arrange themselves into long, thin fibrils. Within these fibrils, the individual collagen molecules are cross-linked to one another. These cross-links result in the formation of very strong mature type III collagen fibrils, which are found in the spaces around cells.

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-12260R-A680)

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-12260R-CY7)

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-12260R-A647)

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-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

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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

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Catalog Number: (PRSI32-143)

Supplier: ProSci Inc.

Description: Biochemically, most members of the CK family fall into one of two classes, type I (acidic polypeptides) and type II (basic polypeptides). The type II cytokeratins consist of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed during differentiation of simple and stratified epithelial tissues. Cytokeratins comprise a diverse group of intermediate filament proteins (IFPs) that are expressed as pairs in both keratinized and non-keratinized epithelial tissue. Cytokeratins play a critical role in differentiation and tissue specialization and function to maintain the overall structural integrity of epithelial cells. Cytokeratins have been found to be useful markers of tissue differentiation which is directly applicable to the characterization of malignant tumors.

UOM: 1 * 100 µl

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Catalog Number: (ICNA0859298)

Supplier: MP Biomedicals

Description: Product is alkaline phosphatase (AKP)-conjugated goat affinity purified antibody to rabbit IgG (whole molecule) and buffer salts. To ensure that the product titer falls within the required range, antibody titer is standardized by microtiter plate ELISA with rabbit IgG. The antibody is tested for purity at 10 mg/mL by immunoelectrophoresis. The antibody is goat IgG; no trace of albumin is detected.

Antibody and highly purified calf-intestine alkaline phosphatase are conjugated under defined conditions to obtain optimally labeled product. Conjugated protein is purified by gel filtration. The product is dialyzed into 0.03M TRIS, 0.14M sodium chloride, pH 8.0, with 1% bovine albumin, adjusted to standard titer, filtered through a 0.22 µm filter, and vialed

UOM: 1 * 1 mL

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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

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Catalog Number: (BOSSBS-12260R-A555)

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-10438R-FITC)

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-3812R-CY5)

Supplier: Bioss

Description: Ubiquitin like proteins fall into two classes: the first class, ubiquitin-like modifiers (UBLs) function as modifiers in a manner analogous to that of ubiquitin. Examples of UBLs are SUMO, Rub1 (also called Nedd8), Apg12 and Hub1. Proteins of the second class include Parkin, RAD23 and DSK2, are designated ubiquitin domain proteins (UDPs). These proteins contain domains that are related to ubiquitin but are otherwise unrelated to each other. In contrast to UBLs, UDPs are not proteolytically processed or conjugated to other proteins. Rub1 and the corresponding human homolog NEDD8 are activated by the E1 ubiquitin activating enzyme UBA2, that forms isopeptide linkages between thio esters. NEDD8 shows 80% homology to ubiquitin. The best known targets of Rub1 modification are members of the cullin family. Cullins are subunits of an E3 ubiquitin ligase complex called the Skp1 /Cul1/Cdc53 F box (SCF). The SCF promotes transfer of ubiquitin from a ubiquitin conjugating enzyme (E2) to the target protein. Rub1 modification may regulate SCF function or localization.

UOM: 1 * 100 µl

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