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Mass+Spectrometry
Numéro de catalogue:
(BOSSBS-1879R-CY7)
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-CY5.5)
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-A680)
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 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-1967R)
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-2537R-A680)
Fournisseur:
Bioss
Description:
Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and SKT4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2537R-CY3)
Fournisseur:
Bioss
Description:
Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and SKT4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2537R-A555)
Fournisseur:
Bioss
Description:
Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and SKT4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1913R-CY5)
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-1913R-CY5.5)
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-1913R-A488)
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-1967R-CY5)
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-6505R-A680)
Fournisseur:
Bioss
Description:
Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerisation which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2537R-A750)
Fournisseur:
Bioss
Description:
Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and SKT4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1913R-A750)
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-1122R-A488)
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-13189R-A488)
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
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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