Recombinant Human Synapsin-1 (SYN1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03360P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Synapsin-1 (SYN1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03360P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Description Recombinant Human Synapsin-1 (SYN1) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P17600
Target Symbol SYN1
Synonyms Brain protein 4.1; SYN 1; SYN 1a; SYN 1b; SYN I; SYN1; SYN1_HUMAN; SYN1a; SYN1b; Synapsin 1; Synapsin I; Synapsin-1; Synapsin1; SynapsinI; SYNI
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence SRVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMAQALPR
Expression Range 113-420aa
Protein Length Partial
Mol. Weight 61.6kDa
Research Area Neuroscience
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level.
Subcellular Location Cell junction, synapse. Golgi apparatus.
Protein Families Synapsin family
Database References

HGNC: 11494

OMIM: 300491

KEGG: hsa:6853

STRING: 9606.ENSP00000295987

UniGene: PMID: 28973667

  • These findings contribute to previous work showing dysregulation of Synapsins, particularly SYN2, in mood disorders and improve our understanding of the regulatory mechanisms that precipitate these changes likely leading to the BD or MDD phenotype. PMID: 27515700
  • Cerebral malaria causes pre-synaptic excitation and eventually activation of synapsin I, leading to increased neurotransmitter release. PMID: 26823711
  • Patterns of the immunoreactivity with antibodies to SNAP-25, synapsin-I and synaptophysin are completely appropriate to those of adult's OB on the 38-40 weeks of the prenatal development. PMID: 26204769
  • The implementation of the AlphaScreen pSYN1 assay and future development of additional primary neuronal HTS assays provides an attractive approach for discovery of novel classes of therapeutic candidates for a variety of CNS disorders. PMID: 24088370
  • these findings suggest PRICKLE1 mutations contribute to ASD by disrupting the interaction with SYN1 and regulation of synaptic vesicles. PMID: 24312498
  • Data indicate that in patients carrying the W356x mutation the function of synapsin I is markedly impaired, and support the value of Syn1(-/-) mice as an experimental model mimicking the human pathology. PMID: 23818987
  • Epileptogenic Q555X SYN1 mutant triggers imbalances in release dynamics and short-term plasticity. PMID: 23406870
  • The histone modification marks were significantly increased in major depression and this effect was correlated with significant increases in SYN1b gene expression. PMID: 22571925
  • The allelic frequencies of SYN1 are associated with Korean female schizophrenia. PMID: 22807112
  • SYN1 loss-of-function mutations in autism and partial epilepsy cause impaired synaptic function. PMID: 21441247
  • the nucleocytoplasmic shuttling of dysbindin-1 regulates synapsin I expression and thus may be involved in the pathogenesis of schizophrenia. PMID: 20921223
  • The authors propose claudin-2 and SYN1 work in concert to enhance microbial translocation across the intestinal epithelial barrier to contribute to chronic immune activation and CD4 T-cell depletion in HIV-1-infected patients. PMID: 20700059
  • The results showed that synapsin I was significantly decreased in the stratum radiatum of CA1 subfield and the molecular layer of DG in AD patients. PMID: 14673601
  • SYN1 nonsense mutation is the likely cause of epileptic and other phenotypes PMID: 14985377
  • Synapsins and S100A1 interact in nerve terminals where coexpresssed; S100A1 cannot bind SV-associated synapsin I and may function as a cytoplasmic store of monomeric synapsin I; synapsin dimerization and interaction with S100A1 are mutually exclusive PMID: 15147519
  • This study concluded that the human synapsin I gene is positively regulated by nuclear respiratory factor 1 and mediates the function of nuclear respiratory factor 1 in neurite outgrowth. PMID: 19301426
  • FAQs

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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.

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