You Searched For: Riboflavine+(Vitamin+B2)

Catalog Number: (BOSSBS-3167R-HRP)

Supplier: Bioss

Description: Ephrin B proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development. Ephrin B molecules expressed at the membrane surface bind to the Ephrin B family receptors on target cells during cell to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing Ephrin B on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of Ephrin B is thought to be a critical component of this reverse signaling event. Recent work demonstrated that Tyr331 of Ephrin B was phosphorylated in HEK293 cells after stimulation by the soluble Ephrin B2 receptor tyrosine kinase.

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Catalog Number: (BOSSBS-3167R-A750)

Supplier: Bioss

Description: Ephrin B proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development. Ephrin B molecules expressed at the membrane surface bind to the Ephrin B family receptors on target cells during cell to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing Ephrin B on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of Ephrin B is thought to be a critical component of this reverse signaling event. Recent work demonstrated that Tyr331 of Ephrin B was phosphorylated in HEK293 cells after stimulation by the soluble Ephrin B2 receptor tyrosine kinase.

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Catalog Number: (BOSSBS-9844R-A750)

Supplier: Bioss

Description: Cleavage of the serine proteinase plasminogen to form plasmin is the central event in the dissolution of blood clots by the fibrinolytic system.Plasminogen related protein B is encoded by the PLGLB1 and PLGLB2 genes. It may bind to lysine binding sites present in the kringle structures of plasminogen interfering with the binding of fibrin or alpha-2-antiplasmin to plasminogen. Within the fibrinolytic cascade, the serine proteinases urokinase-type plasminogen activator (uPA) and tissue-type plasminogen activator (tPA) activate the proenzyme plasminogen by cleaving plasminogen to form the fibrinolytically active enzyme plasmin. PLGLB2 (plasminogen-like B2), also known as PLGP1, is a 96 amino acid protein that resembles the N-terminal plasminogen activation peptide, which is released from plasminogen during conversion to plasmin.

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Catalog Number: (BOSSBS-2802R-A488)

Supplier: Bioss

Description: Retinoids are metabolites of vitamin A (retinal) and are believed to represent important signaling molecules during vertebrate development and tissue differentiation. Two families of retinoid receptors have been identified. Retinoic acid receptors (RARs) include RAR alpha, RAR beta and RAR gamma, each of which has a high affinity for all trans retinoic acids and belongs to the same class of nuclear transcription factors as thyroid hormone receptors, vitamin D3 receptor and ecdysone receptor. The ligand binding domains of the RARs are highly conserved and RAR isoforms are expressed in distinct patterns through out development and in the mature organism. Members of the retinoid X receptor (RXR) family, RXR alpha, RXR beta and RXR gamma, are activated by 9 cis retinoic acid, a stereo and photoisomer of all trans RA that is expressed in vivo in both liver and kidney and may represent a widely used hormone.

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Catalog Number: (BOSSBS-2802R-A350)

Supplier: Bioss

Description: Retinoids are metabolites of vitamin A (retinal) and are believed to represent important signaling molecules during vertebrate development and tissue differentiation. Two families of retinoid receptors have been identified. Retinoic acid receptors (RARs) include RAR alpha, RAR beta and RAR gamma, each of which has a high affinity for all trans retinoic acids and belongs to the same class of nuclear transcription factors as thyroid hormone receptors, vitamin D3 receptor and ecdysone receptor. The ligand binding domains of the RARs are highly conserved and RAR isoforms are expressed in distinct patterns through out development and in the mature organism. Members of the retinoid X receptor (RXR) family, RXR alpha, RXR beta and RXR gamma, are activated by 9 cis retinoic acid, a stereo and photoisomer of all trans RA that is expressed in vivo in both liver and kidney and may represent a widely used hormone.

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Catalog Number: (BOSSBS-5049R-A488)

Supplier: Bioss

Description: Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3-25-hydroxylase activity.

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Catalog Number: (BOSSBS-10342R-A680)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

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Supplier: Apollo Scientific

Description: L(+)-Ascorbic acid ≥99.5%

Catalog Number: (BOSSBS-11333R)

Supplier: Bioss

Description: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

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Catalog Number: (BOSSBS-9035R-A488)

Supplier: Bioss

Description: Pyridoxal kinase belongs to the pyridoxine kinase family and phosphorylates vitamin B6, a step necessary for the conversion of vitamin B6 to pyridoxal 5’ phosphate (PLP), the active form of vitamin B6. PLP acts as a coenzyme and functions to maintain homeostasis. Pyridoxal kinase is a 312-amino acid cytoplasmic protein that may act as a homodimer and is expressed ubiquitously. There are three known isoforms of pyridoxal kinase, and isoform 3 expression is observed in adult testis and spermatozoa. The optimum pH for pyridoxal kinase is between 5.5 and 6.0. PDXK, the gene that encodes the pyridoxal kinase protein, maps to chromosome 21q22.3 and may be a candidate gene for autoimmune polyglandular disease type 1, a genetic disorder that has been mapped to the same region on chromosome 21.

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Catalog Number: (BOSSBS-9035R-CY7)

Supplier: Bioss

Description: Pyridoxal kinase belongs to the pyridoxine kinase family and phosphorylates vitamin B6, a step necessary for the conversion of vitamin B6 to pyridoxal 5’ phosphate (PLP), the active form of vitamin B6. PLP acts as a coenzyme and functions to maintain homeostasis. Pyridoxal kinase is a 312-amino acid cytoplasmic protein that may act as a homodimer and is expressed ubiquitously. There are three known isoforms of pyridoxal kinase, and isoform 3 expression is observed in adult testis and spermatozoa. The optimum pH for pyridoxal kinase is between 5.5 and 6.0. PDXK, the gene that encodes the pyridoxal kinase protein, maps to chromosome 21q22.3 and may be a candidate gene for autoimmune polyglandular disease type 1, a genetic disorder that has been mapped to the same region on chromosome 21.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9035R)

Supplier: Bioss

Description: Pyridoxal kinase belongs to the pyridoxine kinase family and phosphorylates vitamin B6, a step necessary for the conversion of vitamin B6 to pyridoxal 5’ phosphate (PLP), the active form of vitamin B6. PLP acts as a coenzyme and functions to maintain homeostasis. Pyridoxal kinase is a 312-amino acid cytoplasmic protein that may act as a homodimer and is expressed ubiquitously. There are three known isoforms of pyridoxal kinase, and isoform 3 expression is observed in adult testis and spermatozoa. The optimum pH for pyridoxal kinase is between 5.5 and 6.0. PDXK, the gene that encodes the pyridoxal kinase protein, maps to chromosome 21q22.3 and may be a candidate gene for autoimmune polyglandular disease type 1, a genetic disorder that has been mapped to the same region on chromosome 21.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11281R-A488)

Supplier: Bioss

Description: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).

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Catalog Number: (BOSSBS-11281R-A555)

Supplier: Bioss

Description: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).

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Catalog Number: (BSENR-1697-100)

Supplier: Biosensis

Description: The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).

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Supplier: Apollo Scientific

Description: Contains macro/micronutrients, vitamins and plantgrowth regulators required for orchid culturePlant tissue culture testedFull specification given in appendix.