Neuroscience Proteins

Neuroscience is a multidisciplinary scientific discipline that investigates the development, organization, and functional mechanisms of the nervous system. When specific neural circuits or components become dysfunctional, this can manifest as clinically significant impairments in motor control, speech production, respiratory function, or cognitive processes.

Currently, neurodegenerative diseases including Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis (ALS), dementia with Lewy bodies (DLB), and frontotemporal dementia (FTD) have emerged as major global health challenges, yet remain without effective therapeutic interventions. These disorders share a common pathological hallmark characterized by abnormal protein aggregation, most notably the deposition of amyloid-β (Aβ) plaques in AD, and the accumulation of misfolded tau proteins and α-synuclein (α-syn) in PD[1].

Figure1. The misfolded proteins attach to other healthy proteins, building a template that rapidly grows, resembling a crystallisation process[2].

Recent genetic, histopathological, and mechanistic studies have demonstrated that immune dysregulation—characterized by aberrant cytokine signaling, disrupted immune cell proliferation/migration, impaired phagocytic function, and reactive gliosis—constitutes a shared pathological hallmark across neurodegenerative disorders.

Neurodegenerative diseases exhibit distinct clinicopathological profiles. For example, AD demonstrates widespread synaptic degeneration and neuronal loss, accompanied by cerebral accumulation of Aβ plaques and neurofibrillary tangles composed of hyperphosphorylated tau protein. PD primarily presents with motor dysfunction and is pathologically defined by α-syn-rich Lewy body inclusions. DLB shares pathological similarities with PD, while FTD encompasses diverse clinical and proteinopathic subtypes. Importantly, microglial dysfunction and aberrant immune signaling represent a common pathogenic mechanism across these disorders, potentially driving disease initiation and progression.

Alzheimer's Disease Research-Associated Recombinant Proteins

  • Tau Protein
    Hyperphosphorylation of tau proteins can lead to self-assembling tangles of paired helical and straight filaments, which has been implicated in the pathogenesis of AD and FTD and other tauopathies.
  • APP/Protease Nexin-II Protein
    In AD, it is involved in cell signaling, synaptic function, and neurotrophism, and its aberrant processing produces Aβ, which is one of the pathological features of AD, and its pathological amyloid aggregates are also clinicopathological markers of several neurodegenerative diseases.
  • Apolipoprotein E/APOE Protein
    ApoE is one of the major genetic risk factors for AD, and the ApoE ε4 allele in particular has been associated with an increased risk of the disease.ApoE affects lipid metabolism and neuroinflammation in the brain, regulates the aggregation and clearance of amyloid-β (Aβ), potentially compromising the integrity of the blood-brain barrier, and has been associated with Tau proteopathology, exacerbating neurodegeneration.ApoE is a potential target for AD therapy that regulating its expression and function may help prevent or slow disease progression.
  • Acetylcholinesterase/ACHE Protein
    Acetylcholine deficiency has been identified in AD and is associated with cognitive decline.
  • Butyrylcholinesterase/BCHE Protein
    Both acetylcholinesterase and butyrylcholinesterase are targets for improving cholinergic insufficiency, which is thought to be responsible for the decline in cognitive, behavioral, and overall functioning in AD.
  • BACE1 Protein
    BACE1 is an aspartic protease responsible for the protein hydrolytic processing of APP. The generation of the 40- or 42-amino-acid-long Aβ polypeptide that accumulates in the brains of AD patients requires two successive cleavages of APP.
  • TREM-2 Protein
    A rare variant of TREM2, specifically the R47H mutation, is a risk factor for AD.

Parkinson's Disease-Related Recombinant Proteins

  • SNCA Protein
    α-syn is found in Lewy bodies, a neuropathologic feature of Parkinson's disease, and the protein and its aggregation are widely associated with neurotoxic pathways that ultimately lead to neurodegeneration.
  • CNTFR alpha Protein
    The relationship with neurodegenerative diseases is reflected in the pleiotropic properties of its ligand, CNTF, which acts as a neurotrophic factor with neuroprotective effects and is capable of influencing neuronal cell survival and function by modulating multiple signaling pathways.
  • DDC Protein
    DDC levels in cerebrospinal fluid and plasma can be used as a potential biomarker for the detection of Parkinson's-like disease.
  • GFRAL Protein
    The GFRAL protein is a brainstem-restricted receptor that regulates food intake, energy expenditure, and body weight in response to metabolic and toxin-induced stress.

Huntington Disease-Related Recombinant Proteins

  • SOD2/Mn-SOD Protein
    The role of SOD2/Mn-SOD in antioxidant and neuroprotection has been recognized as a potential target for Huntington's disease therapy.
  • UBE2K Protein
    The UBE2K protein interacts with the ring finger protein to ubiquitinate Huntington's disease gene product, Huntington's protein.
  • ATG14 Protein
    ATG14-associated Vps34 activity and ULK1-mediated phosphorylation of ATG14 and Beclin 1 are impaired in the Q175 mouse model of Huntington's disease[5].

Multiple Sclerosis (MS)-Related Recombinant Proteins

  • CD20/MS4A1 Protein
    CD20 is a non-glycosylated protein expressed on the surface of B lymphocytes and belongs to the MS4A family of proteins, and in patients with progressive MS, B-cell and T-cell infiltrates are co-localized with active lesions and there are B-cell aggregates within the meninges resembling lymphoid follicular structures.
  • CD52 Protein
    Multiple sclerosis is an autoimmune disease of the central nervous system (CNS) whose pathogenesis involves an attack by the immune system on the components of its own myelin sheaths.Expression of the CD52 protein on the surface of immune cells makes it an important target for immune regulation. By targeting the CD52 protein, the immune response can be modulated and the attack of immune cells on the CNS can be reduced.
  • CTLA-4/CD152 Protein
    It plays a key role in the down-regulation of T-cell responses and is associated with susceptibility to multiple sclerosis.

Amyotrophic Lateral Sclerosis (ALS)-Related Recombinant Proteins

  • SOD1 Protein
    SOD1 was the first pathogenic gene found to be associated with ALS, and SOD1 mutant proteins aggregate abnormally in motor neurons to form amyloid fibril deposits, one of the typical pathological features of ALS. These aggregates are neurotoxic and can lead to degeneration and death of motor neurons.
  • TDP-43 Protein
    TDP-43 is one of the core pathological markers of ALS. In more than 97% of ALS cases, TDP-43 protein accumulates abnormally in the cytoplasm of motor neurons and forms phosphorylated and ubiquitinated aggregates.
  • VCP Protein
    VCP is involved in the process of Protein degradation, and mutations in its gene have been associated with ALS. Abnormal function of VCP may affect the normal degradation of proteins, leading to the accumulation of abnormal proteins in cells.

Neurotrophic factors are endogenous substances that regulate neurite growth, neuronal differentiation, and survival. They guide neuronal development and play a role in neuronal survival, synaptic plasticity, and the formation of long-term memory in the mature nervous system[5]，click to learn more about neurotrophic factors.

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Alzheimer's Disease Research-Associated Peptides

  • Product Name
    Application
  • β-Amyloid (1-42), human
    β-Amyloid (1-42), a fragment of the amyloid protein, is a primary component of senile plaques in Alzheimer's disease and is used in cell modeling and research to study the disease.
  • β-Amyloid (1-40) (TFA)
    β-Amyloid (1-40), a fragment of the amyloid protein, is a primary component of senile plaques in Alzheimer's disease and is used in cell modeling and research to study the disease.
  • β-Amyloid (25-35)
    β-Amyloid (25-35) is the shortest amyloid protein fragment capable of forming β-fibrils and can be used for Alzheimer's disease research.

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References

[1] Chao Peng, Virginia M-Y Lee, et al. Nat Rev Neurol. 2020 Apr;16(4):199-212.
[2] Balchin, D., Hayer-Hartl, M., Hartl, F. U.. Science. 353, aac4354, (2016).
[3] Hammond, T. R., Marsh, S. E., & Stevens, B. (2019). Immunity. 2019 Apr 16;50(4):955-974.
[4] Wold, M.S., Lim, J., Lachance, V. et al. Mol Neurodegener. 2016 Dec 9;11(1):76.