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Numéro de catalogue: (BOSSBS-13189R-FITC)
Fournisseur: Bioss
Description: Amines, including those present on proteins, spontaneously react with glucose to make fructosamines in a reaction termed glycation. Fructosamine 3-kinase (FN3K), a 309-amino acid enzyme initially identified in erythrocytes, catalyzes the ATP-dependent phosphorylation of the third carbon on both D- and L-fructosamines, leading to their destabilization and eventually, their removal from the protein. FN3K is a monomer that is ubiquitously expressed in mammalian tissue and phosphorylates both low molecular mass and protein-bound fructosamines which are formed as a result of glycation of glucose with primary amines. FN3K protects proteins from the harmful effects of nonenzymatic glycation, and may also be involved in peptide repair and cell metabolism. FN3KRP (fructosamine-3-kinase-related protein) is a 309 amino acid protein that is expressed in erythrocytes, bone marrow, spleen, brain and kidney and belongs to the fructosamine kinase family. FN3KRP functions to phosphorylate psicoamines and ribulosamines on the third carbon of their sugar moiety, thereby leading to the deglycation of the target amines.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-10414R-A488)
Fournisseur: Bioss
Description: Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3'. Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation.
UOM: 1 * 100 µl


Numéro de catalogue: (PERCN9300235)
Fournisseur: PerkinElmer
Description: Designed to contain virtually every element in the mass spectrum for concentration checks.
UOM: 1 * 1 ST


Numéro de catalogue: (LONZ50334)
Fournisseur: LONZA
Description: QuantLadders are prepared from five highly purified DNA fragments that provide visual quantitation of DNA within ±1% accuracy. The DNA QuantLadder provides each DNA fragment in perfect relative mass equivalence at 100 ng, 70 ng, 50 ng, 20 ng and 10 ng. The reverse QuantLadder simply reverses the mass equivalence order of the QuantLadder.
UOM: 1 * 50 ST


Numéro de catalogue: (BOSSBS-1879R-A750)
Fournisseur: Bioss
Description: Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilising complex with the substrates of the sphingolipid hydrolases. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12). Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalisation followed by ERK phosphorylation signaling. Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-0241R-FITC)
Fournisseur: Bioss
Description: The attachment of enveloped viruses to cells and the fusion of viral and cellular membranes are critical early events in the HIV viral infection. This process is mediated by envelope glycoproteins (gp) on the surface of the virus. The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein, gp160, is proteolytically cleaved into gp120 and gp41, which remain noncovalently associated with one another. gp120 is one of the proteins that forms the envelope of HIV. gp120 projects from the surface of HIV and binds to the CD4 molecule on helper T cells. gp120 has been a logical experimental HIV vaccine because the outer envelope is the first part of the virus that encounters antibody. gp41 is embedded in the outer envelope of HIV that anchors gp120. gp41 also plays a key role in HIV's infection of CD4+ T cells by facilitating the fusion of the viral and cell membranes. The nomenclature of the gp proteins describes their respective molecular masses (e.g., gp160, gp120, gp41).
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-13189R-HRP)
Fournisseur: Bioss
Description: Amines, including those present on proteins, spontaneously react with glucose to make fructosamines in a reaction termed glycation. Fructosamine 3-kinase (FN3K), a 309-amino acid enzyme initially identified in erythrocytes, catalyzes the ATP-dependent phosphorylation of the third carbon on both D- and L-fructosamines, leading to their destabilization and eventually, their removal from the protein. FN3K is a monomer that is ubiquitously expressed in mammalian tissue and phosphorylates both low molecular mass and protein-bound fructosamines which are formed as a result of glycation of glucose with primary amines. FN3K protects proteins from the harmful effects of nonenzymatic glycation, and may also be involved in peptide repair and cell metabolism. FN3KRP (fructosamine-3-kinase-related protein) is a 309 amino acid protein that is expressed in erythrocytes, bone marrow, spleen, brain and kidney and belongs to the fructosamine kinase family. FN3KRP functions to phosphorylate psicoamines and ribulosamines on the third carbon of their sugar moiety, thereby leading to the deglycation of the target amines.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-13189R-CY5)
Fournisseur: Bioss
Description: Amines, including those present on proteins, spontaneously react with glucose to make fructosamines in a reaction termed glycation. Fructosamine 3-kinase (FN3K), a 309-amino acid enzyme initially identified in erythrocytes, catalyzes the ATP-dependent phosphorylation of the third carbon on both D- and L-fructosamines, leading to their destabilization and eventually, their removal from the protein. FN3K is a monomer that is ubiquitously expressed in mammalian tissue and phosphorylates both low molecular mass and protein-bound fructosamines which are formed as a result of glycation of glucose with primary amines. FN3K protects proteins from the harmful effects of nonenzymatic glycation, and may also be involved in peptide repair and cell metabolism. FN3KRP (fructosamine-3-kinase-related protein) is a 309 amino acid protein that is expressed in erythrocytes, bone marrow, spleen, brain and kidney and belongs to the fructosamine kinase family. FN3KRP functions to phosphorylate psicoamines and ribulosamines on the third carbon of their sugar moiety, thereby leading to the deglycation of the target amines.
UOM: 1 * 100 µl


Numéro de catalogue: (ENZOADIOSA400E)
Fournisseur: ENZO LIFE SCIENCES
Description: Cleavage of heme b (Fe-protoporphyrin IX) at the a-methene carbon bridge to form the open tetrapyrrole, biliverdin IXa and carbon monoxide (CO) is catalyzed by heme oxygenase (HO) isozymes HO-1 and HO-2 (heme hydrogen-donor: oxygen oxidoreductase; EC 1.14.99.3). In mammalian species, biliverdin reductase (BVR; bilirubin: NAD(P)+ oxidoreductase; EC 1.3.1.24) converts the open tetrapyrrole to bilirubin. This pathway represents the only efficient way of making bilirubin and thereby deterring activation of oxygen by the heme molecule. HO-1 belongs to the heat shock protein family (Hsp32), while HO-2 takes a constitutive form expressed at exceedingly high levels in the brain and testes. The end products of the heme degradation process carry out important physiological activities. CO may act as a messenger in the brain and systemic organs stimulating cGMP-production through interactions with the heme-dependent form of guanylate cyclase. Bile pigments display potent antioxidant activity as well as effective antiviral activity against HIV and herpes virus. BVR is unique among all enzymes characterized to date in having two pH optima (6.8 and 8.7), using a different cofactor at each pH range (NADH at pH 7.0 and NADPH at pH 8.7). The enzyme displays pI and molecular mass microheterogeneity, apparently a result of post translational modifications. In rat, the enzyme also shows a tissue specific developmental pattern. BVR is not inactivated by heat shock, and its preexisting message is not sequestered from translation subsequent to thermal stress. Furthermore, reductase preserves microheterogeneity under thermal stress. BVR expression occurs not only in cells and brain regions that already display HO-1 and HO-2, but also in regions and cell types with potential to induce stress proteins. Rat cDNA for BVR has been isolated and characterized. The deduced protein contains 3 cysteine residues (Cys73, Cys281, and Cys290) involved in cofactor and substrate binding. Human BVR consists of a substantially longer polypeptide than the rat enzyme (41-42 kDa vs. 33 kDa), but also is dual cofactor and dual pH dependent, requires free SH groups for activity, and displays pI and molecular mass microheterogeneity. The human and rat BVR share some antigenic epitopes and show immunochemical cross reactivity.
UOM: 1 * 1 EA


Numéro de catalogue: (REST27196)
Fournisseur: Restek
Description: Mass spec cleaning kit replacement parts kit include lint-free nylon gloves (small, 2 pair), lint-free nylon gloves (large, 2 pair), lint-free cotton cloth, 9×9 (10 packs), micro mesh 4×6 sheet (4 packs)
UOM: 1 * 1 ST


Numéro de catalogue: (BOSSBS-1122R-A750)
Fournisseur: Bioss
Description: The semaphorins are a family of proteins that are involved in signaling. All the family members have a secretion signal, a 500-amino acid sema domain, and 16 conserved cysteine residues(Kolodkin et al., 1993 [PubMed 8269517]). Sequence comparisons have grouped the secreted semaphorins into 3 general classes, all of which also have an immunoglobulin domain. The semaphorin III family, consisting of human semaphorin III (SEMA3A; MIM 603961), chicken collapsin, and mouse semaphorins A, D, and E, all have a basic domain at the C terminus. Chicken collapsin contributes to path finding by axons during development by inhibiting extension of growth cones (Luo et al., 1993 [PubMed 8402908]) through an interaction with a collapsin response mediator protein of relative molecular mass 62K (CRMP62) (Goshima et al., 1995 [PubMed7637782]), a putative homolog of an axonal guidance associated UNC33 gene product (MIM 601168). SEMA3F is a secreted member of the semaphorin III family.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-11498R-FITC)
Fournisseur: Bioss
Description: Olfactory sensory neurons contain olfactory receptors, which are G protein-coupled receptor proteins that localize to the cilia and display affinity for and bind to a variety of odor molecules. Olfactory neurons send their axons from the olfactory epithelium to the olfactory bulb, which is covered by the CNS basal lamina. FEZF1 (Fez family zinc finger protein 1), also known as Forebrain Embryonic Zinc Finger and Zinc finger protein 312B, is a 475 amino acid nuclear protein that is expressed in the olfactory epithelium and hypothalamus of mice. In FEZF1-deficient mice, axons of olfactory neurons do not reach the olfactory bulb, suggesting that FEXF1 is required for the penetration of olfactory axons though the basal lamina before innervation of the olfactory bulb. When FEZF1 translocates to the nucleus, it induces KRAS overexpression, resulting in activation of ERK-signaling. Overexpression of FEZF1 leads to accelerated proliferation in cultured cells and increased tumor mass in mice. There are three isoforms of FEZF1 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-5523R-FITC)
Fournisseur: Bioss
Description: Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-5524R-HRP)
Fournisseur: Bioss
Description: Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-5524R-A647)
Fournisseur: Bioss
Description: Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-4141R-A555)
Fournisseur: Bioss
Description: Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
UOM: 1 * 100 µl


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