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Glucosidase, beta (Bile Acid) 2 Proteins (GBA2)

GBA2 encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Additionally we are shipping GBA2 Antibodies (24) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
GBA2 230101 Q69ZF3
Rat GBA2 GBA2 298399  
GBA2 57704 Q9HCG7
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Top GBA2 Proteins at antibodies-online.com

Showing 5 out of 5 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 39 to 44 Days
$9,248.02
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 39 to 44 Days
$9,248.02
Details
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
$405.71
Details
Yeast Rice His tag   1 mg Log in to see 56 to 66 Days
$3,344.00
Details
HOST_Human Human Un-conjugated   20 μg Log in to see 9 to 11 Days
$785.40
Details

GBA2 Proteins by Origin and Source

Origin Expressed in Conjugate
Mouse (Murine)

Human , ,
,

More Proteins for Glucosidase, beta (Bile Acid) 2 (GBA2) Interaction Partners

Zebrafish Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

  1. GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons.

Mouse (Murine) Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

  1. GBA2 is particularly abundant in Purkinje cells (PCs), one of the most affected neuronal populations in NPC (show NPC1 Proteins) disease.

  2. glucosylceramide accumulation in GBA2 knockout-mice alters cytoskeletal dynamics due to a more ordered lipid organization in the plasma membrane. Similar cytoskeletal defects were observed in male germ and Sertoli cells from GBA2 knockout-mice.

  3. the deletion of Gba2 significantly rescues the type 1 Gaucher disease clinical phenotype.

  4. redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin.

  5. GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling.

  6. The repression of IL-6 (show IL6 Proteins)/STAT3 (show STAT3 Proteins) signalling pathway seems to be one of the mechanisms for the delay of liver regeneration in GBA2-deficient mice.

  7. GBA1 (show GBA Proteins) and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples.

  8. The coiled-coil structure of LIMP-2 is required for its interaction wit (show SCARB2 Proteins)h beta-glucocerebrosidase.

  9. L-type calcium channel blockers have the ex vivo effects of increasing GCase (show GBA Proteins) activity and protein in mouse fibroblasts

  10. GBA2 is a glucosylceramidase (show GBA Proteins) whose loss causes accumulation of glycolipids and an endoplasmic reticulum storage disease

Human Glucosidase, beta (Bile Acid) 2 (GBA2) interaction partners

  1. Spastic paraplegia/cerebellar ataxia (show USP14 Proteins) patients have a severe deficit in GBA2 activity, because the GBA2 mutants are intrinsically inactive and/or reduced in amount.

  2. The GBA2 gene shows a low mutation frequency in a general population of complicated hereditary spastic paraparesis

  3. Whole-exome and targeted sequencing have defined the genetic basis of dizziness including new genes causing ataxia (show USP14 Proteins): GBA2, TGM6 (show TGM5 Proteins), ANO10 (show ANO10 Proteins) and SYT14 (show SYT14 Proteins)

  4. We hereby report a novel GBA2 mutation associated with spastic ataxia (show USP14 Proteins) and suggest that GBA2 mutations may be a relatively frequent cause of autosomal recessive cerebellar ataxias.

  5. observations make GBA2 a likely candidate to be involved in Gaucher disease etiology.

  6. redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin.

  7. GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons.

  8. This study suggests GBA2 mutations are a cause of recessive spastic ataxia (show USP14 Proteins) and responsible for a form of glucosylceramide storage disease in humans.

  9. GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling.

  10. GBA2 is down-regulated in melanoma; inducible expression of GBA2 affects endogenous sphingolipid metabolism by promoting glucosylceramide degradation (decrease by 78%) and ceramide generation.

GBA2 Protein Profile

Protein Summary

This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Studies to determine subcellular localization of this protein in the liver indicated that the enzyme was mainly enriched in the microsomal fraction where it appeared to be confined to the endoplasmic reticulum. This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism.

Gene names and symbols associated with GBA2

  • glucosidase, beta (bile acid) 2 (GBA2)
  • glucosidase, beta (bile acid) 2 (gba2)
  • glucosidase beta 2 (Gba2)
  • F630034E04 protein
  • SPG46 protein
  • TLN1 protein

Protein level used designations for GBA2

bile acid beta-glucosidase , talin 1 , glucosidase, beta (bile acid) 2 , non-lysosomal glucosylceramidase-like , NLGase , beta-glucocerebrosidase 2 , beta-glucosidase 2 , bile acid , glucosylceramidase 2 , non-lysosomal glucosylceramidase

GENE ID SPECIES
465082 Pan troglodytes
559240 Danio rerio
696062 Macaca mulatta
100145361 Xenopus (Silurana) tropicalis
100438148 Pongo abelii
100476888 Ailuropoda melanoleuca
230101 Mus musculus
298399 Rattus norvegicus
57704 Homo sapiens
100859407 Gallus gallus
474760 Canis lupus familiaris
100155655 Sus scrofa
100139170 Bos taurus
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