Rb X alpha Synuclein, phospho Serine 129

Species Reactivity	Key Applications	Host	Format	Antibody Type
R	WB	Rb	Affinity Purified	Polyclonal Antibody

Species Reactivity

Key Applications

Host

Format

Antibody Type

Affinity Purified

Polyclonal Antibody

Description
Catalogue Number	AB9850
Replaces	04-1052
Brand Family	Chemicon®
Trade Name	Chemicon
Description	Anti-phospho-α Synuclein (Ser129) Antibody

Description

Catalogue Number

AB9850

Replaces

04-1052

Brand Family

Chemicon®

Trade Name

Chemicon

Description

Anti-phospho-α Synuclein (Ser129) Antibody

Product Information
Format	Affinity Purified
Presentation	Liquid in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug/mL BSA and 50% glycerol.

Product Information

Format

Affinity Purified

Presentation

Liquid in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug/mL BSA and 50% glycerol.

Applications
Application	This Anti-phospho-α Synuclein (Ser129) Antibody is validated for use in WB for the detection of phospho-α Synuclein (Ser129).
Key Applications	Western Blotting

Applications

Application

This Anti-phospho-α Synuclein (Ser129) Antibody is validated for use in WB for the detection of phospho-α Synuclein (Ser129).

Key Applications

Western Blotting

Biological Information
Immunogen	Synthetic peptide of amino acids surrounding the phosphoSerine 129 site of rat alpha synuclein.
Host	Rabbit
Specificity	Alpha Synuclein, phospho Serine 129. The antibody recognizes a protein of ~15 kDa corresponding to alpha synuclein, phospho Serine 129 in lysates from rat cortex. Immunolableing is blocked by preadsorption with the phospho-peptide used as the immunogen but not by the corresponding dephospho-peptide.
Species Reactivity	Rat
Species Reactivity Note	The immunogen has 100% homology with human, mouse, non-human primate, bovine and canine.
Antibody Type	Polyclonal Antibody
Entrez Gene Number	NM_000345.2 NM_007308.1
Entrez Gene Summary	Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Two alternatively spliced transcripts of SNCA have been identified. Additional splicing may be present but the full-length nature of these variants has not been determined.
Gene Symbol	SNCA MGC110988 PD1 alpha-synuclein NACP PARK1 PARK4 Alpha-synuclein
Modifications	Phosphorylation
Purification Method	ImmunoAffinity Purified
UniProt Number	P37840
UniProt Summary	FUNCTION: SwissProt: P37840 # May be involved in the regulation of dopamine release and transport. Soluble protein, normally localized primarily at the presynaptic region of axons, which can form filamentous aggregates that are the major non amyloid component of intracellular inclusions in several neurodegenerative diseases (synucleinopathies). Induces fibrillization of microtubule- associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase 3 activation. SIZE: 140 amino acids; 14460 Da SUBUNIT: Soluble monomer which can form filamentous aggregates. Interacts with UCHL1 (By similarity). Interacts with phospholipase D and histones. SUBCELLULAR LOCATION: Cytoplasm. Membrane. Nucleus. Note=Membrane- bound in dopaminergic neurons. Also found in the nucleus. TISSUE SPECIFICITY: Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals. DOMAIN: SwissProt: P37840 The NAC domain is involved in the fibril formation. The middle region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments. PTM: 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 (By similarity). DISEASE: SwissProt: P37840 # Defects in SNCA are a cause of autosomal dominant Parkinson disease 1 (PARK1) [MIM:168601, 168600]. Parkinson disease (PD) is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early-onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. & Defects in SNCA are the cause of Parkinson disease 4 (PARK4) [MIM:605543, 168600]. & Defects in SNCA are the cause of Lewy body dementia (DLB) [MIM:127750]. DLB is a neurodegenerative disorder clinically characterized by dementia and parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Presence of Lewy bodies are the only essential pathologic features. & Deposition of fibrillar amyloid proteins intraneuronally as neurofibrillary tangles is characteristic of Alzheimer disease (AD). SNCA is a minor protein found within these deposits, but a major non amyloid component. & Brain iron accumulation type 1 (NBIA1, also called Hallervorden-Spatz syndrome), a rare neuroaxonal dystrophy, is histologically characterized by axonal spheroids, iron deposition, Lewy body (LB)-like intraneuronal inclusions, glial inclusions and neurofibrillary tangles. SNCA is found in LB-like inclusions, glial inclusions and spheroids. SIMILARITY: Belongs to the synuclein family.

Biological Information

Immunogen

Synthetic peptide of amino acids surrounding the phosphoSerine 129 site of rat alpha synuclein.

Host

Rabbit

Specificity

Alpha Synuclein, phospho Serine 129. The antibody recognizes a protein of ~15 kDa corresponding to alpha synuclein, phospho Serine 129 in lysates from rat cortex. Immunolableing is blocked by preadsorption with the phospho-peptide used as the immunogen but not by the corresponding dephospho-peptide.

Species Reactivity

Species Reactivity Note

The immunogen has 100% homology with human, mouse, non-human primate, bovine and canine.

Antibody Type

Polyclonal Antibody

Entrez Gene Number

Entrez Gene Summary

Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Two alternatively spliced transcripts of SNCA have been identified. Additional splicing may be present but the full-length nature of these variants has not been determined.

Gene Symbol

SNCA
MGC110988
PD1
alpha-synuclein
NACP
PARK1
PARK4
Alpha-synuclein

Modifications

Phosphorylation

Purification Method

ImmunoAffinity Purified

UniProt Number

P37840

UniProt Summary

FUNCTION: SwissProt: P37840 # May be involved in the regulation of dopamine release and transport. Soluble protein, normally localized primarily at the presynaptic region of axons, which can form filamentous aggregates that are the major non amyloid component of intracellular inclusions in several neurodegenerative diseases (synucleinopathies). Induces fibrillization of microtubule- associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase 3 activation.
SIZE: 140 amino acids; 14460 Da
SUBUNIT: Soluble monomer which can form filamentous aggregates. Interacts with UCHL1 (By similarity). Interacts with phospholipase D and histones.
SUBCELLULAR LOCATION: Cytoplasm. Membrane. Nucleus. Note=Membrane- bound in dopaminergic neurons. Also found in the nucleus.
TISSUE SPECIFICITY: Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
DOMAIN: SwissProt: P37840 The NAC domain is involved in the fibril formation. The middle region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments.
PTM: 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 (By similarity).
DISEASE: SwissProt: P37840 # Defects in SNCA are a cause of autosomal dominant Parkinson disease 1 (PARK1) [MIM:168601, 168600]. Parkinson disease (PD) is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early-onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. & Defects in SNCA are the cause of Parkinson disease 4 (PARK4) [MIM:605543, 168600]. & Defects in SNCA are the cause of Lewy body dementia (DLB) [MIM:127750]. DLB is a neurodegenerative disorder clinically characterized by dementia and parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Presence of Lewy bodies are the only essential pathologic features. & Deposition of fibrillar amyloid proteins intraneuronally as neurofibrillary tangles is characteristic of Alzheimer disease (AD). SNCA is a minor protein found within these deposits, but a major non amyloid component. & Brain iron accumulation type 1 (NBIA1, also called Hallervorden-Spatz syndrome), a rare neuroaxonal dystrophy, is histologically characterized by axonal spheroids, iron deposition, Lewy body (LB)-like intraneuronal inclusions, glial inclusions and neurofibrillary tangles. SNCA is found in LB-like inclusions, glial inclusions and spheroids.
SIMILARITY: Belongs to the synuclein family.

Product Usage Statements
Usage Statement	Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Product Usage Statements

Usage Statement

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage and Shipping Information
Storage Conditions	Maintain at -20degC in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.

Storage and Shipping Information

Storage Conditions

Maintain at -20degC in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.

Packaging Information
Material Size	100 µL

Packaging Information

Material Size

100 µL

实验耗材

分子生物学试剂

蛋白与免疫学

生化试剂

细胞及检测试剂

色谱及层析

仪器设备

实验服务

办公用品

Rb X alpha Synuclein, phospho Serine 129

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