SNCA (Ab-125) Antibody

Shipped with Ice Packs
In Stock

Description

Introduction to SNCA (Ab-125) Antibody

The SNCA (Ab-125) Antibody is a specialized immunological reagent designed to target alpha-synuclein proteins, specifically around the tyrosine 125 region. This antibody serves as a valuable tool for researchers investigating alpha-synuclein-related pathologies and normal physiological functions. It targets a specific epitope of the alpha-synuclein protein, allowing for precise detection in various experimental contexts .

Alpha-synuclein plays a significant role in the pathogenesis of Parkinson's disease and other neurodegenerative disorders. The protein is encoded by the SNCA gene and has been implicated in various cellular processes, including synaptic vesicle recycling and neurotransmitter release. The ability to specifically detect and quantify this protein using antibodies like SNCA (Ab-125) is fundamental to advancing our understanding of these diseases .

Physical Properties and Formulation

The SNCA (Ab-125) Antibody is supplied in a liquid formulation consisting of rabbit IgG suspended in phosphate-buffered saline (PBS) without magnesium and calcium ions. The buffer is maintained at pH 7.4 and contains 150mM NaCl, 0.02% sodium azide, and 50% glycerol to ensure stability during storage and handling .

Purification Method

The antibody undergoes affinity purification from rabbit antiserum using affinity-chromatography with an epitope-specific immunogen. This purification process ensures high specificity and minimal cross-reactivity with unrelated proteins .

Applications in Research

The SNCA (Ab-125) Antibody has demonstrated utility in several experimental techniques, particularly Western blotting and ELISA. These applications make it a versatile tool for both qualitative and quantitative studies of alpha-synuclein.

Western Blotting

In Western blotting applications, the SNCA (Ab-125) Antibody has been validated for use with rat and mouse brain samples. The recommended dilution range is 1:500 to 1:3000, allowing researchers to optimize detection sensitivity based on their specific experimental conditions and sample characteristics .

ELISA Applications

The antibody has been validated for use in ELISA (Enzyme-Linked Immunosorbent Assay) protocols. ELISA techniques provide quantitative data on alpha-synuclein levels in various biological samples. When using ELISA methods with this antibody, researchers have developed validation protocols to ensure accuracy and reproducibility .

ELISA validation studies with anti-SNCA antibodies have demonstrated good recovery rates (92-108%) and acceptable coefficients of variation for both intra-assay and inter-assay precision, indicating reliable performance in quantitative applications .

Alpha-Synuclein in Disease Context

Understanding the broader context of alpha-synuclein's role in disease provides important background for the utility of the SNCA (Ab-125) Antibody in research applications.

Relevance to Parkinson's Disease Research

Alpha-synuclein plays a major role in Parkinson's disease pathology. Circulating anti-SNCA antibodies have been detected in both Parkinson's disease patients and healthy controls, though their significance and epitope specificity have been incompletely characterized until recent research efforts .

Studies have examined the prevalence of anti-SNCA reactivity in various populations, including individuals carrying LRRK2 mutations (both symptomatic and asymptomatic), idiopathic Parkinson's disease patients, and healthy controls. Research has revealed interesting patterns of antibody presence across these groups, with some evidence suggesting genetic or familial clustering of anti-SNCA antibodies, particularly in LRRK2 mutation carriers .

Regulation of Alpha-Synuclein Expression

Research has identified interesting relationships between alpha-synuclein expression and regulatory proteins such as PARP-1 (Poly ADP Ribose Polymerase-1). Inhibition of PARP-1 has been shown to elevate SNCA mRNA levels, suggesting a role in transcriptional regulation of the SNCA gene .

Studies using the PARP-1 inhibitor 3-Aminobenzamide (3-AB) have demonstrated dose-dependent increases in SNCA mRNA levels, with up to 3.7-fold elevation over untreated cells. This relationship appears to involve interaction with specific regulatory elements in the SNCA promoter/enhancer region, particularly the NACP-Rep1 repeat sequence .

Research Findings Related to Anti-SNCA Antibodies

Studies examining anti-SNCA antibodies in human populations have yielded valuable insights relevant to the application of tools like the SNCA (Ab-125) Antibody.

Prevalence in Clinical Populations

Research has identified "clear-cut" presence of antibodies against alpha-synuclein in various populations, including:

  • 8 out of 49 non-manifesting LRRK2 carriers

  • 5 out of 55 manifesting LRRK2 carriers

  • 3 out of 59 idiopathic Parkinson's disease patients

  • 5 out of 83 healthy controls

These patterns suggest an interesting distribution of naturally occurring anti-SNCA antibodies, with potentially higher prevalence in asymptomatic LRRK2 mutation carriers compared to healthy controls .

Epitope Recognition Patterns

Individuals positive for wild-type alpha-synuclein antibodies typically also recognize various mutant forms of the protein, including A30P, E46K, and A53T missense point mutants. This broad recognition pattern suggests that naturally occurring antibodies target conserved epitopes within the protein structure .

Product Specs

Form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Lead Time
Generally, we can ship the products within 1-3 business days after receiving your orders. Delivery times may vary depending on the purchase method or location. Please consult your local distributors for specific delivery details.
Synonyms
Alpha synuclein antibody; Alpha-synuclein antibody; Alpha-synuclein; isoform NACP140 antibody; alphaSYN antibody; MGC105443 antibody; MGC110988 antibody; MGC127560 antibody; MGC64356 antibody; NACP antibody; Non A beta component of AD amyloid antibody; Non A4 component of amyloid antibody; Non A4 component of amyloid precursor antibody; Non-A beta component of AD amyloid antibody; Non-A-beta component of alzheimers disease amyloid ; precursor of antibody; Non-A4 component of amyloid precursor antibody; Non-A4 component of amyloid; precursor of antibody; OTTHUMP00000218549 antibody; OTTHUMP00000218551 antibody; OTTHUMP00000218552 antibody; OTTHUMP00000218553 antibody; OTTHUMP00000218554 antibody; PARK 1 antibody; PARK 4 antibody; PARK1 antibody; PARK4 antibody; Parkinson disease (autosomal dominant; Lewy body) 4 antibody; Parkinson disease familial 1 antibody; SNCA antibody; Snca synuclein antibody; Snca synuclein; alpha (non A4 component of amyloid precursor) antibody; SYN antibody; Synuclein alpha antibody; Synuclein alpha 140 antibody; Synuclein; alpha (non A4 component of amyloid precursor) antibody; SYUA_HUMAN antibody
Target Names
Uniprot No.

Target Background

Function
SNCA (Alpha-synuclein) is a neuronal protein that plays a significant role in synaptic activity, including the regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. It functions as a monomer in synaptic vesicle exocytosis, enhancing vesicle priming, fusion, and dilation of exocytotic fusion pores. Mechanistically, it operates by increasing local Ca(2+) release from microdomains, crucial for enhancing ATP-induced exocytosis. Furthermore, SNCA acts as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at the presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is vital for maintaining normal SNARE-complex assembly during aging. Additionally, SNCA plays a role in regulating dopamine neurotransmission by associating with the dopamine transporter (DAT1) and modulating its activity.
Gene References Into Functions
  1. Research suggests that SNCA plays a role in opiate dependence. PMID: 21309955
  2. The molecular basis and clinical relevance of statistically reduced alphaSyn pathology in schizophrenic brains compared to aged controls remain unclear and require further investigation. This understanding is crucial for its incidence and relevance in chronic affective disorders. PMID: 19198857
  3. Elevated levels of insoluble alpha-Syn are observed in the brains of patients with Parkinson's and dementia, exceeding those found in Parkinson brains for both insoluble and insoluble/soluble alpha-Syn, with a significant difference between the two groups. PMID: 20599975
  4. Findings suggest that the most effective molecular scaffold for inhibiting and destabilizing self-assembly by alphaS requires: (i) aromatic elements for binding to the alphaS monomer/oligomer and (ii) vicinal hydroxyl groups present on a single phenyl ring. PMID: 21443877
  5. [review] This review summarizes the role of alpha-syn in synaptic vesicle recycling, neurotransmitter synthesis and release, and synaptic plasticity, exploring the potential relationship between the loss of normal alpha-syn functions and disease conditions. PMID: 21167933
  6. Age-related accumulation of neuromelanin may induce alpha-synuclein overexpression, potentially rendering dopamine neurons more vulnerable to injury. PMID: 21461961
  7. The function of alpha-synuclein in promoting cell proliferation is associated with its microtubule assembly activity, with the functional domain located in its carboxyl-terminal part. PMID: 21331461
  8. The association of alpha-synuclein with Rab attachment receptor protein and soluble NSF attachment receptors (SNAREs) highlights the crucial role of membrane transport defects in alpha-synuclein-mediated pathology. PMID: 21439320
  9. Research strongly indicates that Parkinson's disease, induced by alpha-SYN mutation, is triggered by deregulation of the AKT-signaling cascade. PMID: 21474915
  10. While genetic mutations in the alpha-synuclein gene can lead to Parkinson's disease, even in these patients, age-dependent physiological changes or environmental exposures seem to play a role in disease presentation. PMID: 21238487
  11. Current evidence suggests that CSF alpha-synuclein is not suitable as a biomarker to differentiate between PD and AP. PMID: 21236518
  12. [review] This review examines genetic models of PD and implicates presynaptic function in the function/dysfunction of alpha-synuclein, the first gene identified as contributing to Parkinson's disease. PMID: 20969957
  13. In the Caucasian patient-control series examined, the risk for Parkinson disease is influenced by variation in SNCA and tau proteins but not glycogen synthase kinase (GSK)beta3. PMID: 21159074
  14. Overexpression of alpha-Syn transgene alters dopamine efflux and dopamine D2 receptor modulation of corticostriatal glutamate release at a young age in mice. PMID: 21488084
  15. An artificial microRNA-embedded human SNCA silencing vector is expressed without toxicity in rat PC12 cells where rat SNCA is not silenced. It also exhibits reduced toxicity in human SH-SY5Y cells where hSNCA is silenced. PMID: 21338582
  16. Patients with multiple system atrophy may have a cerebrospinal fluid environment particularly conducive to alpha-synuclein fibril formation. PMID: 21215793
  17. Iron up-regulates alpha-synuclein and induces aggregation through the predicted iron responsive element (IRE) in the 5'-untranslated region (UTR) of human alpha-synuclein mRNA. PMID: 20383623
  18. Research has shown an association of the two SNPs in 4q22/SNCA with the age of onset of Parkinson's disease. PMID: 21044948
  19. Findings suggest that alpha-synuclein pathology is associated with Tar DNA-binding protein-43 accumulation in Lewy body disease. PMID: 20669025
  20. Attenuation of nigral SNCA pathology and dopaminergic neurodegeneration by inhibiting NADPH oxidase and iNOS supports a causal relationship between inflammation-mediated SNCA pathologic alterations and chronic dopaminergic neurodegeneration. PMID: 21245015
  21. Research describes spontaneous accumulation of hyperphosphorylated tau in striata of a mouse model of Parkinsonism, which overexpresses human a-Synuclein under the PDGF promoter. PMID: 21453448
  22. Direct replication of single nucleotide polymorphisms (SNPs) within SNCA and BST1 confirmed these two genes to be associated with Parkinson's Disease in the Netherlands. PMID: 21248740
  23. Transgenic alpha-synuclein localizes to the mitochondrial membranes under conditions of proteasomal inhibitory stress. This localization coincides with selective age-related mitochondrial complex I inhibition. PMID: 20887775
  24. Synphilin-1 inhibits alpha-synuclein degradation by the proteasome. PMID: 21103907
  25. Based on crystal structures of fusions between maltose-binding protein and four segments of alpha-synuclein, the study traces a virtual model of the first 72 residues of alpha -synuclein. PMID: 21462277
  26. In transgenic mice, the norepinephrine systems may be more vulnerable than dopamine systems to toxic effects of aberrant alpha-synuclein. This aligns with the significant damage to the noradrenaline system observed in patients with Parkinson's disease. PMID: 19152986
  27. In patients diagnosed with dementia with Lewy bodies, lower cerebrospinal fluid alpha-synuclein levels may be associated with lower cognitive performance, compared to patients diagnosed with Alzheimer's disease. PMID: 20847452
  28. Research identifies a novel function for BAG5 as a modulator of CHIP E3 ubiquitin ligase activity, with implications for CHIP-mediated regulation of alpha-syn oligomerization. PMID: 21358815
  29. Single-nucleotide polymorphisms in SNCA (rs356219; P = 5.5 x 10(-4)) are significantly associated with Parkinson's disease. PMID: 21425343
  30. Evidence suggests that alpha-synuclein exerts a primary and direct effect on the morphology of an organelle long implicated in the pathogenesis of Parkinson disease. PMID: 21489994
  31. Research provides evidence that alpha-synuclein is a cellular ferrireductase, responsible for reducing iron (III) to bioavailable iron (II). PMID: 21249223
  32. A study found a significant association between the NACP-Rep1 length polymorphism and Beck Depression Inventory (BDI) score. However, no further association was observed between the In4 polymorphism or between the mRNA expression of SNCA and the BDI score. PMID: 21271299
  33. This research provides mechanistic insights into the role of alpha-synuclein in modulating neurodegenerative phenotypes by regulating Akt-mediated cell survival signaling in vivo. PMID: 21304957
  34. Data suggests that overexpression of alpha-syn may cause mitochondrial defects in dopaminergic neurons of the substantia nigra through an association with adenylate translocator and activation of mitochondria-dependent cell death pathways. PMID: 21310263
  35. Research demonstrates an elevated state of tauopathy in striata of the A53T alpha-Syn mutant mice, suggesting that tauopathy is a common feature of synucleinopathies. PMID: 21445308
  36. REVIEW: This review explores the role of alpha-Synuclein in Parkinson disease and other neurodegenerative disorders. PMID: 21342025
  37. Data suggests that membrane lipid modification in oligodendroglial cells containing SUMO-1 promotes the formation of alpha-synuclein inclusion bodies resembling protein aggregates in neurodegenerative disease. PMID: 20725866
  38. Research indicates that low SMN levels are associated with significantly lower alpha-synuclein expression, suggesting that alpha-synuclein may be a genetic modifier or biomarker of spinal muscular atrophy. PMID: 20640532
  39. SNCA locus duplication carriers: from genetics to Parkinson disease phenotypes. PMID: 21412942
  40. Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination. PMID: 21466165
  41. This study analyzes the mechanism of membrane permeabilization by oligomeric alpha-synuclein. PMID: 21179192
  42. The research explores the relationship between membrane physical properties and AS binding affinity and dynamics, which presumably define protein localization in vivo and, consequently, the role of AS in the physiopathology of Parkinson disease. PMID: 21330368
  43. MMP3 digestion of alpha-synuclein in DA neurons plays a pivotal role in the progression of Parkinson disease through modulation of alpha-synuclein in aggregation, Lewy body formation, and neurotoxicity. PMID: 21330369
  44. This research characterizes the coordination features and affinity of the Cu(2+) site in the alpha-synuclein protein of Parkinson's disease. PMID: 21319811
  45. This study confirms the association between PD and both SNCA SNPs and the H1 MAPT haplotype. PMID: 21391235
  46. This study exhaustively characterizes Cu(ii) coordination to peptide fragments encompassing residues 45-55 of synuclein alpha, including systems containing the inherited mutations E46K and A53T, as model peptides of the His-50 site. PMID: 21212878
  47. Results support the hypothesis that WT and A53T alpha-synuclein play a significant role in initiating and maintaining inflammation in Parkinson's disease. PMID: 21255620
  48. The combined data indicate that the A30P mutation does not cause changes in the number, location, and overall arrangement of beta-strands in amyloid fibrils of alpha-synuclein. PMID: 21280130
  49. Data suggests that mutations in alpha-synuclein may impair specific functional domains while leaving others intact. PMID: 21272100
  50. Single locus analysis revealed that G/G SNCA and H1/H1 MAPT risk genotypes were over-represented in patients with Parkinson disease compared to controls. PMID: 21054681

Show More

Hide All

Database Links

HGNC: 11138

OMIM: 127750

KEGG: hsa:6622

STRING: 9606.ENSP00000338345

UniGene: Hs.21374

Involvement In Disease
Parkinson disease 1, autosomal dominant (PARK1); Parkinson disease 4, autosomal dominant (PARK4); Dementia Lewy body (DLB)
Protein Families
Synuclein family
Subcellular Location
Cytoplasm. Membrane. Nucleus. Cell junction, synapse. Secreted.
Tissue Specificity
Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2025 TheBiotek. All Rights Reserved.