ELISA/assay

Human Glucosylceramidase (GBA) ELISA Kit

MBS7200758

48-Strip-Wells

470 USD

ELISA Kit

Human Glucosylceramidase (GBA) ELISA Kit

Glucosylceramidase (GBA)

glucosylceramidase isoform 3; Glucosylceramidase; glucosylceramidase; beta-GC; alglucerase; imiglucerase; acid beta-glucosidase; beta-glucocerebrosidase; lysosomal glucocerebrosidase; glucosylceramidase-like protein; D-glucosyl-N-acylsphingosine glucohydrolase; glucosidase, beta, acid; Acid beta-glucosidase; Alglucerase; Beta-glucocerebrosidase; Beta-GC; D-glucosyl-N-acylsphingosine glucohydrolase; Imiglucerase

GBA

GBA; GBA; GCB; GBA1; GLUC; GC; GLUC; Beta-GC

GLCM_HUMAN

Human

This assay has high sensitivity and excellent specificity for detection of GBA. No significant cross-reactivity or interference between GBA and analogues was observed. NOTE: Limited by current skills and knowledge, it is impossible for us to complete the cross-reactivity detection between GBA and all the analogues, therefore, cross reaction may still exist in some cases.

Store all reagents at 2-8 degree C.

Samples: Serum, plasma, cell culture supernatants, body fluid and tissue homogenate. Assay Type: Competitive. Sensitivity: 0.1 ng/mL.

Intended Uses This GBA ELISA kit is a 1.5 hour solid-phase ELISA designed for the quantitative determination of HumanGBA. This ELISA kit for research use only, not for therapeutic or diagnostic applications!. Principle of the Assay: GBA ELISA kit applies the competitive enzyme immunoassay technique utilizing a monoclonal anti- GBA antibody and an GBA -HRP conjugate. The assay sample and buffer are incubated together with GBA -HRP conjugate in pre-coated plate for one hour. After the incubation period, the wells are decanted and washed five times. The wells are then incubated with a substrate for HRP enzyme. The product of the enzyme-substrate reaction forms a blue colored complex. Finally, a stop solution is added to stop the reaction, which will then turn the solution yellow. The intensity of color is measured spectrophotometrically at 450nm in a microplate reader. The intensity of the color is inversely proportional to the GBA concentration since GBA from samples and GBA -HRP conjugate compete for the anti- GBA antibody binding site. Since the number of sites is limited, as more sites are occupied by GBA from the sample, fewer sites are left to bind GBA -HRP conjugate. A standard curve is plotted relating the intensity of the color (O.D.) to the concentration of standards. The GBA concentration in each sample is interpolated from this standard curve.

284807152

NP_001165283.1

NM_001171812.1

54,471 Da

Glycosphingolipid Metabolism Pathway (530751); Lysosome Pathway (99052); Lysosome Pathway (96865); Metabolic Pathways (132956); Metabolism Pathway (477135); Metabolism Of Lipids And Lipoproteins Pathway (160976); Other Glycan Degradation Pathway (82976); Other Glycan Degradation Pathway (346); Sphingolipid Metabolism Pathway (82994); Sphingolipid Metabolism Pathway (119543)

This gene encodes a lysosomal membrane protein that cleaves the beta-glucosidic linkage of glycosylceramide, an intermediate in glycolipid metabolism. Mutations in this gene cause Gaucher disease, a lysosomal storage disease characterized by an accumulation of glucocerebrosides. A related pseudogene is approximately 12 kb downstream of this gene on chromosome 1. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2010]

GBA: Defects in GBA are the cause of Gaucher disease (GD); also known as glucocerebrosidase deficiency. GD is the most prevalent lysosomal storage disease, characterized by accumulation of glucosylceramide in the reticulo-endothelial system. Different clinical forms are recognized depending on the presence (neuronopathic forms) or absence of central nervous system involvement, severity and age of onset. Defects in GBA are the cause of Gaucher disease type 1 (GD1); also known as adult non-neuronopathic Gaucher disease. GD1 is characterized by hepatosplenomegaly with consequent anemia and thrombopenia, and bone involvement. The central nervous system is not involved. Defects in GBA are the cause of Gaucher disease type 2 (GD2); also known as acute neuronopathic Gaucher disease. GD2 is the most severe form and is universally progressive and fatal. It manifests soon after birth, with death generally occurring before patients reach two years of age. Defects in GBA are the cause of Gaucher disease type 3 (GD3); also known as subacute neuronopathic Gaucher disease. GD3 has central nervous manifestations. Defects in GBA are the cause of Gaucher disease type 3C (GD3C); also known as pseudo-Gaucher disease or Gaucher-like disease. Defects in GBA are the cause of Gaucher disease perinatal lethal (GDPL). It is a distinct form of Gaucher disease type 2, characterized by fetal onset. Hydrops fetalis, in utero fetal death and neonatal distress are prominent features. When hydrops is absent, neurologic involvement begins in the first week and leads to death within 3 months. Hepatosplenomegaly is a major sign, and is associated with ichthyosis, arthrogryposis, and facial dysmorphism. Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders. Defects in GBA contribute to susceptibility to Parkinson disease (PARK). A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. Belongs to the glycosyl hydrolase 30 family. 3 isoforms of the human protein are produced by alternative splicing. Protein type: Hydrolase; EC 3.2.1.45; Glycan Metabolism - other glycan degradation; Lipid Metabolism - sphingolipid. Chromosomal Location of Human Ortholog: 1q21. Cellular Component: lysosomal lumen; lysosomal membrane. Molecular Function: protein binding; receptor binding; glucosylceramidase activity. Biological Process: glucosylceramide catabolic process; negative regulation of MAP kinase activity; sphingolipid metabolic process; skin morphogenesis; response to glucocorticoid stimulus; response to testosterone stimulus; positive regulation of protein amino acid dephosphorylation; regulation of water loss via skin; response to estrogen stimulus; negative regulation of inflammatory response; carbohydrate metabolic process; negative regulation of interleukin-6 production; sphingosine biosynthetic process; ceramide biosynthetic process; glycosphingolipid metabolic process; response to pH. Disease: Gaucher Disease, Type Ii; Dementia, Lewy Body; Parkinson Disease, Late-onset; Gaucher Disease, Perinatal Lethal; Gaucher Disease, Type Iiic; Gaucher Disease, Type Iii; Gaucher Disease, Type I

48-Strip-Wells

470 USD

96-Strip-Wells

675