Recombinant Human Beta-synuclein Protein

Name: Recombinant Human Beta-synuclein Protein
Brand: Beta LifeScience
SKU: BL-1375SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NM_003085
Synonym	(None)
Background	Beta-synuclein is a member of the synuclein family of proteins which are believed to be involved in the pathogenesis of neurodegenerative diseases. Beta-synuclein is highly homologous to alpha-synuclein which is abundantly expressed in the brain and putatively inhibits phospholipase D2 selectively. Beta-synuclein may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer disease. Beta-synuclein is shown to be highly expressed in the substantia nigra of the brain, a region of neuronal degeneration in patients with Parkinson disease but no direct relation to Parkinson disease has been established (1). An alteration in Beta-synuclein may impair its normal inhibitory action on the formation of toxic alpha-synuclein fibrils, thereby indirectly contributing to disease pathogenesis (2).
Description	Recombinant full length human Beta-synuclein was produced in E. coli system, fused with a His tag at N-terminus. This protein is purified with our unique purification methods.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	~19 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human Beta-synuclein Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Non-amyloid component of senile plaques found in Alzheimer disease. Could act as a regulator of SNCA aggregation process. Protects neurons from staurosporine and 6-hydroxy dopamine (6OHDA)-stimulated caspase activation in a p53/TP53-dependent manner. Contributes to restore the SNCA anti-apoptotic function abolished by 6OHDA. Not found in the Lewy bodies associated with Parkinson disease.
Subcellular Location	Cytoplasm.
Protein Families	Synuclein family
Database References	HGNC: 11140 OMIM: 602569 KEGG: hsa:6620 STRING: 9606.ENSP00000308057 UniGene: PMID: 29054856 alterations in the plasma alpha-synuclein and beta-synuclein levels might be implicated in the association between synaptic abnormalities and autism spectrum disorder pathogenesis. PMID: 29850516 Study suggests that beta-synuclein changes in Dementia with Lewy bodies may exacerbate neuronal dysfunction caused by accumulation of alpha-synuclein by influencing protein degradation. PMID: 29278715 Data suggest that pH serves as an on/off switch for beta- synuclein to form aggregates/fibrils (as seem in Parkinson disease); hydrogen bonding between glutamate residues appears to be involved in fibril formation. PMID: 28710275 Cellular pathways affected by bSyn are similar to those affected by aSyn, including impairment of vesicular trafficking and induction of oxidative stress. PMID: 26586132 loss of inhibitory C-terminal conformations in disease associated P123H beta-synuclein PMID: 26332674 beta-Synuclein expression was locally concentrated and rather modest, but nevertheless changed its effect on amyloid precursor protein expression and plaque load in a time- and concentration-dependent manner. PMID: 26111745 The differing aggregation propensities of alpha-synuclein and beta-synuclein are associated with differences in the degree of residual structure in the C-terminus coupled to the shorter separation between the N- and C-termini in beta-synuclein. PMID: 25389903 Beta-synuclein protects against isoaspartate accumulation in alpha-synuclein. PMID: 23630590 both alphaS- and P123H betaS-globules were formed through similar but distinct pathogenic mechanisms. PMID: 23013868 In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells PMID: 23319586 Thermodynamic studies in conjunction with EPR confirm that alpha-synuclein, beta-synuclein, and gamma-synuclein bind copper(II) in a high affinity 1:1 stoichiometry. PMID: 21117662 Data provide evidence for the role of beta-synuclein minor transcript variants in the development of complex diseases and provide new insights into the pathogenesis of Lewy body diseases. PMID: 22205345 This study suggested that the pathogenesis of dementia in Parkinson disease, indicating that differential sncb expression in the caudate nucleus may represent one of the molecular mechanisms involved in these complex diseases. PMID: 21683963 Despite both synucleins sharing considerable sequence homology, the level of carboxy-terminal Src kinase-homologous kinase (CHK) phosphorylation of beta-synuclein is significantly higher than that of alpha-synuclein. PMID: 21699177 Transcriptional regulation of the beta-synuclein 5'-promoter metal response element by metal transcription factor-1. PMID: 21386983 Synuclein-alpha, -beta, and -gamma are important in regulating neurotransmitter release from specific populations of midbrain dopamine neurons through mechanisms that differ from those reported in other neurons. PMID: 21593311 Studies identified molecular interaction domains within the beta-synuclein polypeptide that specifically binds alpha-synuclein. PMID: 21085664 beta-Synuclein mRNA expression in the control group was significantly higher than that in the schizophrenic group. PMID: 20854101 A drastic diminution of beta-synuclein expression was observed in cortical areas of all samples that presented neuropathological features corresponding to pure diffuse Lewy body pathology PMID: 20959308 Human beta-synuclein rendered fibrillogenic by designed mutations. PMID: 20833719 Data show that alpha-synuclein, beta-synuclein, and apolipoprotein A-1 have the conserved functional ability to induce membrane curvature and to convert large vesicles into highly curved membrane tubules and vesicles. PMID: 20693280 members of the synuclein gene family, particularly SNCA and SNCG, affect the risk of developing diffuse lewy body disease. PMID: 20697047 Gamma-synuclein protein is valuable for evaluation of progression of colorectal carcinoma; it is more sensitive to predict advanced stage and lymph node invasion when combined with either alpha- or beta-synuclein protein. PMID: 20043104 Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins PMID: 11812782 Of medulloblastomas, 76% have immunoreactivity for either alpha- or beta-synuclein or both; no immunoreactivity for gamma-synuclein is seen in medulloblastomas. PMID: 12783249 Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: cross-talk with alpha-synuclein and implication for Parkinson's disease. PMID: 12867415 2 new AA changes were found in unrelated Lewy body dementia index cases: V70M & P123H, at conserved residues in highly conserved regions of the beta-synuclein protein. Mutations in the beta-synuclein gene may predispose to DLB. PMID: 15365127 the alpha- and gamma-synucleins regulate proteasomal function and beta-synuclein acts as a negative regulator of alpha-synuclein PMID: 15591046 An 11-residue deletion in the lipid-binding domain of beta-synuclein leads to the destabilization of an entire segment of the micelle-bound helical structure containing the deletion site. PMID: 16597821 findings indicate that increased expression of beta-synuclein protein results in a reduction of alpha-synuclein protein expression PMID: 16959793 The accumulation of beta-synuclein was detectable only in the pons of Sandhoff disease cases. This differential accumulation of alpha- and beta-synucleins in human lipidoses may be related to functional differences between these two proteins. PMID: 17653558 A comparison of the structural and dynamic properties of the free states of all three synucleins, is reported in order to shed light on differences that may help to explain their different propensities to aggregate. PMID: 17681534 Our data confirm the fatty acid binding properties of alpha-syn, and to a lesser extent beta-syn, but suggest that gamma-syn does not share this same characteristic. PMID: 17692832 structural and functional properties of beta-synuclein were characterized using biochemical and bio-physical methods including: a functional assay, mass spectrometry, size exclusion chromatography, circular dichroism (CD), and fluorescence spectroscopy PMID: 18221001 The aggregation behavior of alpha- and beta-synuclein as well as a series of chimeric variants were compared by exploring the structural transitions that occur in the presence of a widely used lipid mimetic, sodium dodecyl sulfate (SDS). PMID: 18436957

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.