You Searched For: Acrylamide+(monomer)

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.

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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.

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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.

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Catalog Number: (BOSSBS-15458R-HRP)

Supplier: Bioss

Description: Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.

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Catalog Number: (BOSSBS-15458R-FITC)

Supplier: Bioss

Description: Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2015R-A750)

Supplier: Bioss

Description: Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localisation. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2015R-A680)

Supplier: Bioss

Description: Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localisation. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2015R-A647)

Supplier: Bioss

Description: Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.

UOM: 1 * 100 µl

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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.

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-13300R-HRP)

Supplier: Bioss

Description: GBE1 is a 702 amino acid protein that is expressed at high levels in muscle and liver and is involved in glycogen biosynthesis. Existing as a monomer, GBE1 catalyzes the transfer of alpha-1,4-linked glucosyl units from the outer end of a glycogen chain to an alpha-1,6 position on a neighboring glycogen chain and, via this catalytic activity, plays an essential role in glycogen accumulation. Defects in the gene encoding GBE1 are the cause of glycogen storage disease type 4 (GSD4) and adult polyglucosan body disease (APBD), the first of which is a metabolic disorder that is associated with the accumulation of polysaccharides and is characterized by liver disease during childhood. Unlike GSD4, APBD is a late-onset disorder that affects the central and peripheral nervous systems and is characterized by cognitive impairment, pyramidal tetraparesis and peripheral neuropathy.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13300R-A350)

Supplier: Bioss

Description: GBE1 is a 702 amino acid protein that is expressed at high levels in muscle and liver and is involved in glycogen biosynthesis. Existing as a monomer, GBE1 catalyzes the transfer of alpha-1,4-linked glucosyl units from the outer end of a glycogen chain to an alpha-1,6 position on a neighboring glycogen chain and, via this catalytic activity, plays an essential role in glycogen accumulation. Defects in the gene encoding GBE1 are the cause of glycogen storage disease type 4 (GSD4) and adult polyglucosan body disease (APBD), the first of which is a metabolic disorder that is associated with the accumulation of polysaccharides and is characterized by liver disease during childhood. Unlike GSD4, APBD is a late-onset disorder that affects the central and peripheral nervous systems and is characterized by cognitive impairment, pyramidal tetraparesis and peripheral neuropathy.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11390R-A750)

Supplier: Bioss

Description: AASDHPPT (aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase), also known as LYS2, LYS5 or CGI-80, is a 309 amino acid protein that localizes to the cytoplasm and belongs to the P-Pant transferase superfamily. Expressed in testis, liver, kidney, heart, brain, placenta and skeletal muscle, AASDHPPT exists as a monomer that functions to catalyse the phosphopantetheine-dependent post-translational modification of target proteins, effectively transferring a 4'-phosphopantetheine moiety from coenzyme A (CoA) to a serine residue of an acceptor protein. AASDHPPT is subject to DNA damage-dependent phosphorylation, probably by ATM or ATR. The gene encoding AASDHPPT maps to human chromosome 11, which houses over 1,400 genes and comprises nearly 4% of the human genome.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3303R-A488)

Supplier: Bioss

Description: This gene encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. This gene is flanked on chromosome 5 by the genes for granulocyte-macrophage colony-stimulating factor and macrophage-colony stimulating factor receptor; all three genes may be implicated in the 5-q syndrome. A translocation between chromosomes 5 and 12, that fuses this gene to that of the translocation, ETV6, leukemia gene, results in chronic myeloproliferative disorder with eosinophilia. [provided by RefSeq].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11390R-A555)

Supplier: Bioss

Description: AASDHPPT (aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase), also known as LYS2, LYS5 or CGI-80, is a 309 amino acid protein that localizes to the cytoplasm and belongs to the P-Pant transferase superfamily. Expressed in testis, liver, kidney, heart, brain, placenta and skeletal muscle, AASDHPPT exists as a monomer that functions to catalyze the phosphopantetheine-dependent post-translational modification of target proteins, effectively transferring a 4'-phosphopantetheine moiety from coenzyme A (CoA) to a serine residue of an acceptor protein. AASDHPPT is subject to DNA damage-dependent phosphorylation, probably by ATM or ATR. The gene encoding AASDHPPT maps to human chromosome 11, which houses over 1,400 genes and comprises nearly 4% of the human genome.

UOM: 1 * 100 µl

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