SPAST Antibodies

Structure of SPAST

The molecular weight of the spastin protein encoded by the SPAST gene is approximately 80 kDa, and its size is highly conserved among different mammals. The main differences are reflected in the specific functional domains that affect the binding ability of microtubules.

This protein is composed of 616 amino acids, and its core structural feature is an AAA ATPase functional domain, which drives conformational changes by hydrolyzing ATP to recognize and cut microtubules. The N-terminal of the protein contains a microtubule binding domain (MTBD), which is responsible for targeting the cytoskeleton. The AAA domain at the C-end forms a typical hexameric ring structure, functioning as a molecular motor. Its activity strictly depends on key residues such as glutamic acid at position 518, which jointly coordinate the mechanochemical cycle of ATP hydrolysis and microtubule cleavage.

Fig. 1 The homodimeric crystal structure of SpAST.¹

Key structural properties of SPAST:

• AAA ATPase hexameric ring structure
• Microtubule binding domain (MTBD)
• Microtubule recognition loop (M-loop)
• Hydrolyzed domain (Walker B motif)

Functions of SPAST

The main function of the spastin protein encoded by the SPAST gene is to cut and reshape the microtubule network of cells. However, it is also involved in a variety of key cellular physiological processes, including vesicle transport, organelle localization and cell division.

Unlike motor proteins such as kinesin that "walk along the microtubules", spastin acts as a "microtubule cutter" by hydrolyzing ATP at specific points to directly break the microtubule precursor, which enables it to play a unique regulatory role in maintaining the plasticity of the cytoskeleton.

Applications of SPAST and SPAST Antibody in Literature

1. Jeong, Soo Yeon, Hyeonseok Jin, and Jeong Ho Chang. "Crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe." PLoS One 14.8 (2019): e0221975. https://doi.org/10.1371/journal.pone.0221975

In this paper, by determining the crystal structure of Schizoyeast L-aspartate aminotransferase 2.1A, it was found that it regulates the catalytic mechanism through conformational changes in the N-terminal arm. Based on the characteristics of the N-terminal arm, the related enzymes were classified into eight subcategories, revealing the structural evolution relationship of pyridoxal phosphate dependent enzymes.

2. Mohan, Neha, et al. "Therapeutic strategies for mutant SPAST-based hereditary spastic paraplegia." Brain sciences 11.8 (2021): 1081. https://doi.org/10.3390/brainsci11081081

The article indicates that SPAST gene mutation is the main cause of hereditary spastic paraplegia, which leads to the loss of spastin protein function and the acquisition of toxic functions. This article explores therapeutic strategies targeting these two pathogenic mechanisms to alleviate the symptoms of patients with SPG4-type HSP.

3. Elert-Dobkowska, Ewelina, et al. "SPAST intragenic CNVs lead to hereditary spastic paraplegia via a haploinsufficiency mechanism." International journal of molecular sciences 25.9 (2024): 5008. https://doi.org/10.3390/ijms25095008

The article indicates that through the analysis of 69 SPG4 patients, it was found that the repeated Alu sequences within the SPAST gene are highly prone to cause micro-rearrangement mutations. The research successfully located multiple gene breakpoints and revealed that non-allelic homologous recombination is its formation mechanism.

4. Nan, Haitian, et al. "A p. Arg499His mutation in SPAST is associated with infantile-onset complicated spastic paraplegia: a case report and review of the literature." BMC neurology 21.1 (2021): 439. https://doi.org/10.1186/s12883-021-02478-0

The article indicates that the p.Arg499His mutation in the SPAST gene is closely related to the complex hereditary spastic paraplegia that occurs in infancy. The literature review concludes that this mutant phenotype can be classified into three categories, and the new mutation rate is high. This discovery expands its clinical spectrum.

5. Verriello, Lorenzo, et al. "Amplifying the spectrum of SPAST gene mutations." Acta Bio Medica: Atenei Parmensis 92.Suppl 1 (2021): e2021220. https://doi.org/10.23750/abm.v92iS1.11608

The article indicates that a novel variation of the SPAST gene was discovered in a pure-phenotypic HSP family in Italy. The 3T microdeletion in exon 13 leads to the deletion of leucine at position 508 of the AAA domain, which is highly conserved. It is speculated that this will disrupt protein function and cause disease.

Creative Biolabs: SPAST Antibodies for Research

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

• Custom SPAST 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 SPAST antibodies, custom preparations, or technical support, contact us at email.