Analytical Data
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基因名
SYNC
- Application
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别名
SYNC；SYNC1；Syncoilin
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9H7C4
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表达区间
1-482aa
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氨基酸序列
MASPEPRRGG DGAAQAARKT RVEANSPLPK NSGSLNEAEA LNPEVTLSSE GSLNLEDILY LEDTGDLDET LYVQETEKAE EALYIEEAMQ PDEALHVEEP GNPEETVCVE ETTEPDRIQF VEGPVEPGKP TSPEHVVYEG ETVTRAEKSN PEESLRAEQS PSMEENLSIE DLELLEGRFQ QCVQAVAQLE EERDQLIHEL VLLREPALQE VQQVHQDILA AYKLHAQAEL ERDGLREEIR LVKQKLFKVT KECVAYQYQL ECRQQDVAQF ADFREVLTTR ATQLSEELAQ LRDAYQKQKE QLRQQLEAPP SQRDGHFLQE SRRLSAQFEN LMAESRQDLE EEYEPQFLRL LERKEAGTKA LQRTQAEIQE MKEALRPLQA EARQLRLQNR NLEDQIALVR QKRDEEVQQY REQLEEMEER QRQLRNGVQL QQQKNKEMEQ LRLSLAEELS TYKAMLLPKS LEQADAPTSQ AGGMETQSQG AV
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SYNC (Synapsin) proteins are a family of neuronal phosphoproteins implicated in the regulation of synaptic transmission and neurotransmitter release. The study of SYNC proteins is rooted in their essential role in the organization and clustering of synaptic vesicles at presynaptic terminals, making them critical for efficient communication between neurons. Research has shown that SYNC proteins interact with various proteins, including actin, thus participating in cytoskeletal dynamics and vesicle trafficking. Dysregulation of SYNC protein functions has been linked to several neuropsychiatric disorders, such as autism spectrum disorders, bipolar disorder, and schizophrenia, highlighting their importance in underlying neurobiological mechanisms. Additionally, the phosphorylation state of SYNC proteins is essential for their activity, suggesting that signaling pathways affecting phosphorylation can modulate synaptic function. Recent advancements in techniques like cryo-electron microscopy and super-resolution imaging have facilitated a deeper understanding of the molecular architecture of synapses and the specific roles of SYNC proteins within these complexes. Ongoing research aims to elucidate the precise mechanisms by which SYNC proteins contribute to synaptic plasticity, learning, and memory, as well as their potential as therapeutic targets for neurodevelopmental and neurodegenerative disorders. Overall, the exploration of SYNC proteins provides valuable insights into synaptic biology and holds promise for developing novel strategies for managing brain-related conditions.
