You Searched For: Acrylamide+(monomer)

Supplier: Biotium

Description: This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta-1, TGF beta-2 and TGF beta-3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF betarequires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta-3 protein has approximately 80% identity to the mature region of both TGF beta-1 and TGF beta-2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.

Supplier: Biotium

Description: This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta-1, TGF beta-2 and TGF beta-3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF betarequires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta-3 protein has approximately 80% identity to the mature region of both TGF beta-1 and TGF beta-2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.

Catalog Number: (BOSSBS-1499R-A350)

Supplier: Bioss

Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1499R-A647)

Supplier: Bioss

Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13276R-CY7)

Supplier: Bioss

Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into alpha, beta, and gamma families, and the beta and gamma-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. gamma-crystallins are structural proteins in the lens, and they exists as monomers which typically lack connecting peptides and terminal extensions. The gamma-crystallins include seven closely related gamma A, gamma B, gamma C, gamma D, gamma E, gamma F, and gamma G-crystallin, as well as the gamma N and gamma S-crystallin genes. The gamma-crystallins are differentially regulated after early development, and are involved in cataract formation as a result of either age-related protein degradation or genetic mutation.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13276R-CY3)

Supplier: Bioss

Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into alpha, beta, and gamma families, and the beta and gamma-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. gamma-crystallins are structural proteins in the lens, and they exists as monomers which typically lack connecting peptides and terminal extensions. The gamma-crystallins include seven closely related gamma A, gamma B, gamma C, gamma D, gamma E, gamma F, and gamma G-crystallin, as well as the gamma N and gamma S-crystallin genes. The gamma-crystallins are differentially regulated after early development, and are involved in cataract formation as a result of either age-related protein degradation or genetic mutation.

UOM: 1 * 100 µl

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Catalog Number: (ROTH4233.1)

Supplier: Roth Carl

Description: Methyl methacrylate stabilised

UOM: 1 * 1 L

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Catalog Number: (PRSI26-845)

Supplier: ProSci Inc.

Description: GSN binds to the 'plus' ends of actin monomers and filaments to prevent monomer exchange. It is a calcium-regulated protein, which functions in both assembly and disassembly of actin filaments. Defects in the gene encoding GSN are a cause of familial amyloidosis Finnish type (FAF).The protein encoded by this gene binds to the 'plus' ends of actin monomers and filaments to prevent monomer exchange. The encoded calcium-regulated protein functions in both assembly and disassembly of actin filaments. Defects in this gene are a cause of familial amyloidosis Finnish type (FAF). Multiple transcript variants encoding several different isoforms have been found for this gene.

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-11676R-CY3)

Supplier: Bioss

Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11676R-FITC)

Supplier: Bioss

Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-15573R-A555)

Supplier: Bioss

Description: Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13447R-CY5)

Supplier: Bioss

Description: Glycogen synthesis is initiated by the autoglucosylation of Glycogenin-1. Specifically, Glycogenin-1 glucosylates itself to begin the synthesis of glycogen in mammalian skeletal muscle. It acts as the primer to which further glucose monomers may be added. All of the Glycogenin-1 molecules contain at least one glucosyl residue before autoglucosylation begins. The first step of the glycogen synthesis occurs when a glucose molecule from UDP-glucose binds to the hydroxyl group of Tyr 194 on the Glycogenin-1 molecule. Using its glucosyltransferase activity, Glycogenin-1 adds more glucoses, each one coming from UDP-glucose. The glycosylation process reaches a plateau when five new glucose residues have been added, at which point glycogen synthase (GS) takes over and further elongates the chain. Glycogenin-1 remains covalently attached to the reducing end of the glycogen molecule.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7548R-CY5.5)

Supplier: Bioss

Description: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0474R)

Supplier: Bioss

Description: Human IgA (immunoglobulin A) is a glycosylated protein of 160 kDa and is produced as a monomer or as a J chain linked dimer. Monomeric IgA constitutes 5-15 % of the serum immunoglobulins whereas dimeric IgA is localized to mucosa surfaces such as saliva, gastrointestinal secretion, bronchial fluids and milk. Mucosal IgA plays a major role in host defence by neutralising infectious agents at mucosal surfaces. The production is usually local and antigen specific IgA producing B cells can be found in regions under the lamina propria where they mature into dimeric IgA producing plasma cells. IgA deficiency is the most common immunodeficiency that may affect both serum and mucosal produced IgA.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-5371R-CY5)

Supplier: Bioss

Description: PMVK is a 192 amino acid peroxisomal enzyme belonging to the nucleoside monophosphate (NMP) kinase family and is expressed in heart, liver, skeletal muscle, kidney, and pancreas with lower expression in brain, placenta and lung. Induced by sterol, PMVK participates in isopentenyl diphosphate biosynthesis via the mevalonate pathway. PMVK catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate in the fifth reaction of the cholesterol biosynthetic pathway. PMVK exists as a monomer and is encoded by a gene located on human chromosome 1, which houses over 3,000 genes and is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-5371R-A488)

Supplier: Bioss

Description: PMVK is a 192 amino acid peroxisomal enzyme belonging to the nucleoside monophosphate (NMP) kinase family and is expressed in heart, liver, skeletal muscle, kidney, and pancreas with lower expression in brain, placenta and lung. Induced by sterol, PMVK participates in isopentenyl diphosphate biosynthesis via the mevalonate pathway. PMVK catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate in the fifth reaction of the cholesterol biosynthetic pathway. PMVK exists as a monomer and is encoded by a gene located on human chromosome 1, which houses over 3,000 genes and is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome.

UOM: 1 * 100 µl

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