GALC Antibodies

Background

The GALC gene encodes galactoceramidase, a lysosomal hydrolase, which is mainly expressed in oligodendrocytes and Schwann cells of the central nervous system. This enzyme is responsible for catalyzing the key steps in sphingolipid metabolism, specifically hydrolyzing substrates such as galactoceramide and psychonin to maintain myelin homeostasis. Mutations in the GALC gene can lead to lysosomal storage disease - Claber's disease, which is characterized by myelin formation disorders and neurofunctional degeneration. This gene was successfully cloned in 1993. The research on its molecular mechanism not only revealed the important pathways of sphingolipid metabolism but also provided a molecular basis for the targeted treatment of related neurodegenerative diseases. The research on the function of this gene has greatly advanced people's understanding of lysosomal function, myelin biology and the mechanism of neurodegeneration.

Structure Function Application Advantage Our Products

Structure of GALC

GALC is a hydrolase with a molecular weight of approximately 80 kDa. Its precise molecular weight varies slightly among different species, mainly due to minor changes in amino acid sequences.

Species	Human	Mouse	Rat	Bovine
Molecular Weight (kDa)	80.2	79.8	80.1	80.3
Primary Structural Differences	With signal peptide and the structure of catalytic domain	Have high homology with human	The catalytic key residues are conserved	Glycosylation sites differences

This protein is composed of long-chain polypeptides containing multiple domains, and its active center has key catalytic residues, which can specifically hydrolyze galactose lipid substrates. The tertiary structure of GALC forms a typical (α/β) ₈TIM barrel-shaped catalytic core, surrounded by multiple helical domains that together constitute its substrate-binding pockets. Its active site contains a pair of conserved aspartic acid residues, which are responsible for catalyzing the cleavage of galactosidic bonds. This mechanism is highly conserved among species.

Fig. 1:The GALC–SapA complex forms a pseudo-symmetric heterotetramer. Fig. 1 The GALC–SapA complex forms a pseudo-symmetric heterotetramer.¹

Key structural properties of GALC:

Has typical hydrolase (α/β)₈ TIM barrel catalytic core structure
Hydrophobic active pockets are responsible for recognizing and binding to galactose lipid substrates
Conserved aspartic acid diides are directly involved in glycosidic bond breaking as catalytic residues

Functions of GALC

The main function of the GALC gene-encoded protein is to hydrolyze specific lipids to maintain the homeostasis of the nervous system. In addition, it is also involved in key physiological processes such as myelin metabolism and cell signal regulation.

Function	Description
Galactolipid hydrolysis	Specifically hydrolyze substrates such as galactoceramide to prevent their abnormal accumulation in lysosomes.
Maintenance of myelin homeostasis	Participating in the balance between the synthesis and degradation of myelin sheath is crucial for the structural and functional integrity of white matter.
Neuroprotective function	Eliminate potential neurotoxic metabolites and delay the occurrence and progression of demyelinating diseases.
Regulation of apoptosis	Influence of oligodendrocytes path, survival and death involved in neurodegenerative process adjustment.
Enzyme replacement therapy targets	As a molecular therapeutic target for lysosomal storage diseases such as Claber's disease, it is used for the development of exogenous enzyme replacement therapy.

The optimal pH of this enzyme is within the acidic range (approximately pH 4.0-5.0), which is adapted to the environment in which it functions in lysosomes. Its catalytic efficiency depends on the substrate aggregation state and the presence of lysosomal activators.

Applications of GALC and GALC Antibody in Literature

1. Yang, Mengdi, et al. "GALC triggers tumorigenicity of colorectal cancer via senescent fibroblasts." Frontiers in Oncology 10 (2020): 380. https://doi.org/10.3389/fonc.2020.00380

The article indicates that among colorectal cancer patients treated with XELOX, senescent fibroblasts with high GALC expression promote tumor cell proliferation, migration and invasion by regulating factors such as ATF3 and KIAA0907, thereby influencing the prognosis of patients.

2. Herdt, Aimee R., et al. "Brain targeted AAV1-GALC gene therapy reduces psychosine and extends lifespan in a mouse model of Krabbe disease." Genes 14.8 (2023): 1517. https://doi.org/10.3390/genes14081517

The article indicates that delivering the GALC gene to the central nervous system of Krabbe disease model mice through the AAV1 vector significantly reduces the level of psychotoxins, prolongs survival and improves weight gain, confirming that intraventricular gene therapy has a significant intervention effect on this disease.

3. Feo, Federica, et al. "High Prevalence of GALC Gene Variants in Adults With Neurodegenerative Conditions." European Journal of Neurology 32.5 (2025): e70206. https://doi.org/10.1111/ene.70206

Research has found that heterozygous variations in the GALC gene may be associated with neurodegenerative diseases such as Parkinson's disease and ataxia. Among the 110 patients, the heterozygous carrier rate of GALC was significantly higher than that of the general population. Some patients were also accompanied by other lysosome-related gene mutations, with phenotypes including atypical Parkinson's symptoms, white matter lesions and inflammatory abnormalities.

4. Tian, Guoshuai, et al. "rAAV2-mediated restoration of GALC in neural stem cells from Krabbe patient-derived iPSCs." Pharmaceuticals 16.4 (2023): 624. https://doi.org/10.3390/ph16040624

In this study, neural stem cells (K-NSCs) derived from iPSCs of patients with Krabbe disease were used to construct a disease model. It was found that the rAAV2 vector can efficiently infect K-NSCs, and the GALC gene delivery it mediates can effectively restore the activity of galactocephalase in cells, providing a new strategy for gene therapy of this disease.

5. Zhuang, Shunzhi, et al. "GALC mutations in Chinese patients with late-onset Krabbe disease: a case report." BMC neurology 19.1 (2019): 122. https://doi.org/10.1186/s12883-019-1345-z

This study reports a case of late-onset Krabbe disease caused by a GALC gene mutation (c.865G> c/c.136G>T). The patient presented with progressive spastic gait disorder and vision loss. MRI showed lesions in the white matter and corticospinal tract, and the diagnosis was confirmed by enzyme activity detection and gene sequencing.

Creative Biolabs: GALC Antibodies for Research

Creative Biolabs specializes in the production of high-quality GALC antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom GALC Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our GALC antibodies, custom preparations, or technical support, contact us at email.

Reference

Hill, Chris H., et al. "The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure." Nature communications 9.1 (2018): 151. https://doi.org/10.1038/s41467-017-02361-y