Recombinant GBA Monoclonal Antibody (AN301962L)
For research use only.
| Verified Samples |
Verified Samples in WB: MCF-7, Saos-2, SH-SY5Y, 4T1, C6 Verified Samples in IHC: Human kidney, Human thyroid cancer |
| Dilution | WB 1:1000-1:20000, IHC 1:50 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human GBA fragment |
| Abbre | GBA |
| Synonyms | GBA, GBA1, GCB, GLUC, GC, 9-O-sialyl GD3, 7-O-sialyl GD3, ACID, acid (includes glucosylceramidase), beta, Acid beta glucosidase, Acid beta-glucosidase, Alglucerase, Beta glucocerebrosidase, BETA GLUCOSIDASE, betaGC, Beta-glucocerebrosidase, D glucosyl N acylsphingosine glucohydrolase, D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45, Gba protein, GCase, GLCM, Glucocerebrosidase, Glucocerebrosidase (alt.), GLUCOCEREBROSIDASE PSEUDOGENE, Glucosidase, Glucosidase beta, Glucosylceramidase, Imiglucerase, Lysosomal glucocerebrosidase, OTTHUMP00000033992, OTTHUMP00000033993 |
| Swissprot | |
| Calculated MW | 60 kDa |
| Observed MW |
60 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Lysosome |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Neuroscience, Signal Transduction, Cancer, Metabolism |
| Clone No. | A678 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Beta-Glucosylceramidase (β-GC) is a lysosomal enzyme that catalyzes the hydrolysis of glucocerebroside into free ceramide and glucose. Lysosomal breakdown of glucocerebroside is required for cellular metabolism of complex lipids and proper turnover of cellular membrane. In the absence of GBA, the gene that encodes β-GC, autophagic lysosome reformation is altered, suggesting that β-GC activity is critical to maintain functional lysosomes. The cellular function of lysosomes is to degrade and recycle cellular waste to maintain proper cellular energy metabolism. Mutations in human GBA cause deficiency in β-GC, resulting in the accumulation of lysosomal glucocerebroside. Macrophages are particularly sensitive to lysosomal glucocerebroside accumulation due to their role in phagocytosis-mediated breakdown of cellular debris and dying cells. Gaucher disease, a rare autosomal recessive lysosomal storage disorder that is genetically linked to GBA, is marked by engorged “Gaucher cell” macrophages in the spleen, liver, and bone marrow. GBA mutations are the most common genetic risk factor for Parkinson’s disease (PD), a neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra with formation of α-synuclein-rich Lewy bodies in surviving neurons. GBA mutations may play a direct role in accumulation of α-synuclein by mechanisms that are poorly understood, but may include mislocalization of lysosomal β-GC causing impaired lysosomal degradation of α-synuclein. |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
-
IF：{{item.impact}}
Journal：{{item.journal}} ({{item.year}})
DOI：{{item.doi}}Reactivity：{{item.species}}
Sample Type：{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}
