MilliporeSigma™ Beta-glucosidase 2 (GBA2), Rat, Unlabeled, Clone: 4A12,
Manufacturer: MilliporeSigma™
Select a Size
| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| Each of 1 | MABN757-Each-of-1 | In Stock | ₹ 38,958.86 |
MABN757 - Each of 1
In Stock
Quantity
1
Base Price: ₹ 38,958.86
GST (18%): ₹ 7,012.595
Total Price: ₹ 45,971.455
Antigen
Beta-glucosidase 2 (GBA2)
Classification
Monoclonal
Concentration
Please refer to lot specific datasheet.
Formulation
Purified rat IgG1 in buffer containing 0.1M Tris-Glycine (pH 7.4), 150mM NaCl with 0.05% Sodium Azide.
Gene Accession No.
Q69ZF3
Immunogen
Ovalbumin-conjugated linear peptide corresponding to a sequence from the N-terminal region of mouse beta-glucosidase 2 (GBA2).
Quantity
100 μL
Research Discipline
Neuroscience
Gene ID (Entrez)
NP_766280
Target Species
Mouse
Form
Purified
Applications
Immunohistochemistry (Paraffin), Western Blot
Clone
4A12
Conjugate
Unconjugated
Gene
Gba2, Kiaa1605
Host Species
Rat
Purification Method
Protein G Purified
Regulatory Status
RUO
Primary or Secondary
Primary
Test Specificity
Clone 4A12 detected the beta-glucosidase 2 (GBA2) target band in testis tissue sample from wild-type, but not Gba2-knock mice (Korschen, H.G., et al. (2013). J. Biol. Chem. 288(5):3381-3393).
Content And Storage
Stable for 1 year at 2°-8°C from date of receipt.
Isotype
IgG1 κ
Related Products
Description
- Non-lysosomal glucosylceramidase (EC 3.2.1.45; UniProt Q69ZF3; also known as Beta-glucocerebrosidase 2, Beta-glucosidase 2, Glucosylceramidase 2, NLGase) is encoded by the Gba2 (also known as Kiaa1605) gene (Gene ID 230101) in murine species
- Glucosidases GBA1, GBA2, and GBA3 are structurally unrelated proteins with similar hydrolase activity that mediates glucosylceramide (GlcCer) degradation
- GBA1 mediates GlcCer degradation in the lysosome lumen following its transport via the endosomal pathway
- GBA2 is localized at the cytosolic surface of the ER and Golgi, with a predominant presence at the cis-Golgi in close proximity to the site of GlcCer synthesis and sphingomyelin conversion
- GlcCer is also delivered to the ER through FAPP2-dependent transport and then flips to ER lumenal side by low specificity phospholipid flippases
- GBA2 ER localization allows it to regulate GlcCer level at the cytosolic side of the ER and limit the amount of GlcCer from entering the ER lumenal side for higher order glycosphingolipid synthesis
- Impaired GBA1 activity causes accumulation of GlcCer in lysosomes of tissue macrophages, causing liver and spleen enlargement and impairment of the central nervous system in patients with Gaucher disease
- GBA2 activity is found downregulated in fibroblasts from a patient with type II Gaucher disease and fibroblasts from Gba1-deficient mice, suggesting a cross-talk between GBA1 and GBA2 that could affect the phenotype of Gaucher disease
- GBA3 is a cytosolic Klotho-related protein whose physiological function is not yet known.