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AB314423

Recombinant Human SNCA Protein

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Recombinant Human SNCA Protein is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95%, > 0.005 EU/µg endotoxin level, suitable for Mass Spec, HPLC, SDS-PAGE.

View Alternative Names

NACP, PARK1, SNCA, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor

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Mass Spectrometry - Recombinant Human SNCA Protein (AB314423)
  • Mass Spec

Lab

Mass Spectrometry - Recombinant Human SNCA Protein (AB314423)

Mass determination by ESI-TOF. Predicted MW is 14460.28 Da (+/- 10 Da by ESI-TOF). Observed MW is 14460.38.

Key facts

Purity

>95% HPLC

Endotoxin level

> 0.005 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, Mass Spec, HPLC

applications

Biologically active

No

Accession

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS, 5% Glycerol (glycerin, glycerine)

storage-buffer

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Reagents, Controls & Accessories

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Prestained Protein Ladder - Mid-range molecular weight (11-180 kDa, 4-color)

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Primary Antibodies

AB209538

Anti-Alpha-synuclein aggregate antibody [MJFR-14-6-4-2] - Conformation-Specific

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Immunocytochemistry/ Immunofluorescence - Anti-Alpha-synuclein aggregate antibody [MJFR-14-6-4-2] - Conformation-Specific (AB209538)

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Biochemicals

AB120751

Thioflavin T, Fluorescent cell-permeable amyloid binding benzothiazole salt

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Secondary Antibodies

AB150077

Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

Immunocytochemistry/ Immunofluorescence - Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (AB150077)

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Primary Antibodies

AB278054

Anti-GFAP antibody [RM1003] - Astrocyte Marker

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Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-GFAP antibody [RM1003] - Astrocyte Marker (AB278054)

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"linker":null,"sequence":"MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA","proteinLength":"Full Length","predictedMolecularWeight":"14.46 kDa","actualMolecularWeight":"14.46 kDa","aminoAcidEnd":140,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P37840","tags":[]}]
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Properties and storage information

Form
Liquid
Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Alpha-synuclein often referred to by alternate names such as SNCA is a protein of around 14 kDa mass. It mainly expresses in the brain particularly in presynaptic nerve terminals. This protein functions mechanically by stabilizing synaptic vesicles and maintaining synaptic function. It exists both in soluble monomer forms and as aggregates in protein filaments. Antibodies like 4D6 and EP1536Y target monomer forms of protein for more detailed studies.
Biological function summary

The alpha-synuclein protein plays critical roles in neuronal activity. It contributes to neurotransmitter release regulation by acting in the formation and plasticity of the presynaptic neuronal network. Alpha-synuclein doesn't usually form parts of large protein complexes but it may associate transiently with membranes and vesicular structures. The protein's monomer form has also been observed in alpha lines and related neuronal processes operating alongside various cellular functions.

Pathways

Synaptic vesicle trafficking and dopamine neurotransmitter release are significant areas involving the alpha-synuclein protein. In these pathways alpha-synuclein interacts with other proteins like synaptophysin and protein monomer monomerizations are intrinsic to these processes. Altered function or aggregation of alpha-synuclein disrupts these pathways influencing broader neurological functions.

Alterations or accumulations of alpha-synuclein are strongly linked to Parkinson's disease and Lewy body dementia. In these conditions alpha-synuclein forms abnormal protein filaments known as Lewy bodies within neurons. These formations disrupt cellular processes and neuron health. Synucleinopathies such as these show connections with proteins like parkin and DJ-1 which also have key roles in these neurodegenerative diseases.
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General info

Function

Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed : 20798282, PubMed : 26442590, PubMed : 28288128, PubMed : 30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed : 28288128, PubMed : 30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed : 30404828). Also 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 presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed : 20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed : 20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed : 26442590).

Sequence similarities

Belongs to the synuclein family.

Post-translational modifications

Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.. Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.. Ubiquitinated. The predominant conjugate is the diubiquitinated form.. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.

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Product protocols

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Target data

Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed : 20798282, PubMed : 26442590, PubMed : 28288128, PubMed : 30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed : 28288128, PubMed : 30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed : 30404828). Also 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 presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed : 20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed : 20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed : 26442590).
See full target information SNCA
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