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Mass+Spectrometry
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Mass+Spectrometry
Numéro de catalogue:
(BOSSBS-13596R-A488)
Fournisseur:
Bioss
Description:
ECAT1 (ES cell-associated transcript 1 protein) is a 217 amino acid protein that belongs to the KHDC1 family. The ECAT1 protein contains an atypical KH domain with amino acid changes at critical sites, suggesting that it may not bind RNA. Expression of ECAT1 appears to be maximal in germinal vesicle oocytes, it tails off through metaphase II oocytes and is undetectable following the completion of the oocyte to embryo transition. Specifically expressed in the oocytes, recent studies suggest that ECAT1 may function as a regulator of genomic imprinting in the oocyte. Defects in ECAT1 are the cause of hydatidiform mole recurrent type 2 (HYDM2), a disorder characterized by excessive trophoblast development that produces a growing mass of tissue inside the uterus at the beginning of a pregnancy. HYDM2 leads to abnormal pregnancies with no embryo, and cystic degeneration of the chorionic villi.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13596R-A555)
Fournisseur:
Bioss
Description:
ECAT1 (ES cell-associated transcript 1 protein) is a 217 amino acid protein that belongs to the KHDC1 family. The ECAT1 protein contains an atypical KH domain with amino acid changes at critical sites, suggesting that it may not bind RNA. Expression of ECAT1 appears to be maximal in germinal vesicle oocytes, it tails off through metaphase II oocytes and is undetectable following the completion of the oocyte to embryo transition. Specifically expressed in the oocytes, recent studies suggest that ECAT1 may function as a regulator of genomic imprinting in the oocyte. Defects in ECAT1 are the cause of hydatidiform mole recurrent type 2 (HYDM2), a disorder characterized by excessive trophoblast development that produces a growing mass of tissue inside the uterus at the beginning of a pregnancy. HYDM2 leads to abnormal pregnancies with no embryo, and cystic degeneration of the chorionic villi.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11498R-A680)
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-Signalling. Overexpression of FEZF1 leads to accelerated proliferation in cultured cells and increased tumour 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-11498R-A750)
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-Signalling. Overexpression of FEZF1 leads to accelerated proliferation in cultured cells and increased tumour 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-4141R-CY5.5)
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-5522R-CY3)
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-CY7)
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-CY5)
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-1967R-CY5.5)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1967R-A750)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localisation. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1967R-A350)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1967R-FITC)
Fournisseur:
Bioss
Description:
Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1913R-FITC)
Fournisseur:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1879R)
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 solubilizing 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 internalization 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-CY5)
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-1879R-CY3)
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 solubilizing 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 internalization 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
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