You Searched For: Vineomycin+B2

Catalog Number: (BSENC-1698-100)

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).

UOM: 1 * 100 µl

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Supplier: Apollo Scientific

Description: Riboflavine-5'-phosphate sodium salt USP

Catalog Number: (BOSSBS-12933R-A680)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyse other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesised in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11470R-CY3)

Supplier: Bioss

Description: Plexins are a family of large, transmembrane receptors for multiple classes of semaphorins in vertebrates. They are widely expressed, and regions of their extracellular domain are homologus to both scatter factor receptors and semaphorin domains. Plexins may act as semaphorin receptors alone or in combination with neuropilins. Plexins are divided into four subfamilies designated plexin-A, -B, -C, and -D. Plexin-B1 and -B2 are both receptors for Sema4D, which stimulates axonal outgrowth of embryonic dorsal root ganglion neurons. . Plexin-B3 binds to Sema5A, which controls axon guidance and can initiate the intracellular signaling of the hepatocyte growth factor/scatter factor receptor Met.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13085R-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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11555R-A555)

Supplier: Bioss

Description: The Forkhead-box (FOX) genes comprise a superfamily of at least 43 members that encode proteins which are involved in transcriptional regulation and may be associated with the pathogenesis of various cancers. FOXB1 (forkhead box B1), also known as FKH5 or HFKH-5, and FOXB2 (forkhead box B2) are members of the FOX family and each contain one forkhead DNA-binding domain. Both FOXB1 and FOXB2 localize to the nucleus where they are thought to function as transcription factors that can bind to DNA via their forkhead domains. In mice, defects in the gene encoding FOXB1 are associated with retarded development of the central nervous system (CNS), suggesting that FOXB1 may play a role in CNS organization and function.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3167R-A555)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12880R-FITC)

Supplier: Bioss

Description: Spermatogenesis represents the intricate developmental process of mitotic and meiotic cell divisions that ultimately leads to the production of haploid spermatozoa. BOULE, a member of the human deleted in azoospermia (DAZ) family, functions as a key conserved switch that regulates the progression of germ cells through meiosis in man. BOULE is an RNA-binding protein that regulates the expression of twine, a Cdc25 phosphatase, which promotes progression through meiosis. BOULE is expressed not only in the testis, but also in the nervous system, where it may play a role in neural communication. Mutations in the BOULE gene are be associated with male infertility, and the relative proportions of the three BOULE isoforms (B1, B2 and B3) may function as predictive markers for meiotic efficiency.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3217R-A350)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3167R-A647)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10342R-CY3)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11215R)

Supplier: Bioss

Description: Plexins are a family of large, transmembrane receptors for multiple classes of semaphorins in vertebrates. They are widely expressed, and regions of their extracellular domain are homologus to both scatter factor receptors and semaphorin domains. Plexins may act as semaphorin receptors alone or in combination with neuropilins. Plexins are divided into four subfamilies designated plexin-A, -B, -C, and -D. Plexin-B1 and -B2 are both receptors for Sema4D, which stimulates axonal outgrowth of embryonic dorsal root ganglion neurons. . Plexin-B3 binds to Sema5A, which controls axon guidance and can initiate the intracellular signaling of the hepatocyte growth factor/scatter factor receptor Met.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12549R-HRP)

Supplier: Bioss

Description: Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (A–H) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12549R-A750)

Supplier: Bioss

Description: Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (AH) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11470R-CY7)

Supplier: Bioss

Description: Plexins are a family of large, transmembrane receptors for multiple classes of semaphorins in vertebrates. They are widely expressed, and regions of their extracellular domain are homologus to both scatter factor receptors and semaphorin domains. Plexins may act as semaphorin receptors alone or in combination with neuropilins. Plexins are divided into four subfamilies designated plexin-A, -B, -C, and -D. Plexin-B1 and -B2 are both receptors for Sema4D, which stimulates axonal outgrowth of embryonic dorsal root ganglion neurons. . Plexin-B3 binds to Sema5A, which controls axon guidance and can initiate the intracellular signaling of the hepatocyte growth factor/scatter factor receptor Met.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12933R-CY3)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

Sale