Vector Labs Ab04613-3.3 Anti-Oligomeric alpha-synuclein [D5 (D5E)], Mouse IgG2b, Fc Silent™, kappa (100 μg) Centrifuge Bundle Savings at Sycamore Life Sciences

Description

Product Class: Purified
Clone ID: D5 (D5E)
Heavy Chain Modification: Fc Silent™
Synonyms: SNCA; NACP; PARK1; alpha-syn; α-Synuclein; α-syn; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; oligomeric α-synuclein; oligomeric α-syn
Amount: 100 μg
Application Codes Clone: ELISA; WB; functional assay
Shipping Temperature: Wet Ice
Buffer Composition: PBS with 0.02% Proclin 300.
Original Format: scFv
Storage Temperature: Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement: This full-length, chimeric mouse antibody was made using the variable domain sequences of the original Human scFv format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement: This antibody recognizes the early-stage oligomeric morphological form of human alpha-synuclein. Alpha-synuclein is a small 140 amino acid presynaptic neuronal protein, a major component of Lewy bodies and a member of the synuclein family. Misfolding, abnormal accumulation, and secretion of α-Synuclein (α-Syn) are closely associated with synucleinopathies, including Parkinson’s disease (PD). α-syn is abundant in the brain, and smaller amounts are found in the heart, muscles, and other tissues. In the brain, α-syn is found mainly at the tips of neurons in the specialized structures known as presynaptic terminals and has been shown to comprise up to ∼1% of total proteins in the neuronal cytosol. Recent evidence suggests that α-synuclein (α-syn) can contribute to the pathogenesis of amyotrophic lateral sclerosis (ALS).
Application Notes: The binding of this antibody to oligomeric forms of alpha-synuclein was confirmed using ELISA. This antibody is not capable of recognizing monomeric and fibrillar forms of alpha-synuclein. This antibody could also recognize molecular masses of about 29 and 56 kDa corresponding to dimeric and tetrameric forms of alpha-syn form in a western blot (PMID: 17391701; 19141614). The scFv form of this antibody binds only to an oligomeric form of α-synuclein and inhibits both aggregation and toxicity of α-synuclein in vitro (PMID: 17391701). This antibody could recognize the early stage alpha-synuclein aggregates occurring during (4–10 day) time points (PMID: 19141614). Intracellular expression of scFv version of this antibody containing a non-conventional secretion signal sequence could successfully bind their cytosolic targets and secrete them from a mammalian cell. It was further demonstrated that secretion of scFv bound oligomeric alpha-syn aggregates provides complete protection from a-syn-induced toxicity (PMID: 19394405). A fusion protein comprising D5 scFv, cell penetrating peptide like penetratin were found to be effective in Lewy body disease. It specifically targeted α-syn oligomers and reduced the accumulation of α-syn and ameliorated functional deficits when delivered late in disease development (PMID: 27606342).

Product Class:	Purified
Clone ID:	D5 (D5E)
Heavy Chain Modification:	Fc Silent™
Synonyms:	SNCA; NACP; PARK1; alpha-syn; α-Synuclein; α-syn; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; oligomeric α-synuclein; oligomeric α-syn
Amount:	100 μg
Application Codes Clone:	ELISA; WB; functional assay
Shipping Temperature:	Wet Ice
Buffer Composition:	PBS with 0.02% Proclin 300.
Original Format:	scFv
Storage Temperature:	Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement:	This full-length, chimeric mouse antibody was made using the variable domain sequences of the original Human scFv format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement:	This antibody recognizes the early-stage oligomeric morphological form of human alpha-synuclein. Alpha-synuclein is a small 140 amino acid presynaptic neuronal protein, a major component of Lewy bodies and a member of the synuclein family. Misfolding, abnormal accumulation, and secretion of α-Synuclein (α-Syn) are closely associated with synucleinopathies, including Parkinson’s disease (PD). α-syn is abundant in the brain, and smaller amounts are found in the heart, muscles, and other tissues. In the brain, α-syn is found mainly at the tips of neurons in the specialized structures known as presynaptic terminals and has been shown to comprise up to ∼1% of total proteins in the neuronal cytosol. Recent evidence suggests that α-synuclein (α-syn) can contribute to the pathogenesis of amyotrophic lateral sclerosis (ALS).
Application Notes:	The binding of this antibody to oligomeric forms of alpha-synuclein was confirmed using ELISA. This antibody is not capable of recognizing monomeric and fibrillar forms of alpha-synuclein. This antibody could also recognize molecular masses of about 29 and 56 kDa corresponding to dimeric and tetrameric forms of alpha-syn form in a western blot (PMID: 17391701; 19141614). The scFv form of this antibody binds only to an oligomeric form of α-synuclein and inhibits both aggregation and toxicity of α-synuclein in vitro (PMID: 17391701). This antibody could recognize the early stage alpha-synuclein aggregates occurring during (4–10 day) time points (PMID: 19141614). Intracellular expression of scFv version of this antibody containing a non-conventional secretion signal sequence could successfully bind their cytosolic targets and secrete them from a mammalian cell. It was further demonstrated that secretion of scFv bound oligomeric alpha-syn aggregates provides complete protection from a-syn-induced toxicity (PMID: 19394405). A fusion protein comprising D5 scFv, cell penetrating peptide like penetratin were found to be effective in Lewy body disease. It specifically targeted α-syn oligomers and reduced the accumulation of α-syn and ameliorated functional deficits when delivered late in disease development (PMID: 27606342).

Specifications

More Information
Brand	Vector Labs
UNSPSC	12161500

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