Analytical Data
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Gene name
RAPSN
- Application
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Alternative Names
RAPSN;RNF205;43 kDa receptor-associated Protein of the synapse
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13702
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Expression Region
2-412aa
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AA Sequence
GQDQTKQQI EKGLQLYQSN QTEKALQVWT KVLEKSSDLM GRFRVLGCLV TAHSEMGRYK EMLKFAVVQI DTARELEDAD FLLESYLNLA RSNEKLCEFH KTISYCKTCL GLPGTRAGAQ LGGQVSLSMG NAFLGLSVFQ KALESFEKAL RYAHNNDDAM LECRVCCSLG SFYAQVKDYE KALFFPCKAA ELVNNYGKGW SLKYRAMSQY HMAVAYRLLG RLGSAMECCE ESMKIALQHG DRPLQALCLL CFADIHRSRG DLETAFPRYD SAMSIMTEIG NRLGQVQALL GVAKCWVARK ALDKALDAIE RAQDLAEEVG NKLSQLKLHC LSESIYRSKG LQRELRAHVV RFHECVEETE LYCGLCGESI GEKNSRLQAL PCSHIFHLRC LQNNGTRSCP NCRRSSMKPG FV
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
Protein Description
RAPSN (Receptor-Associated Protein of the Synapse, also known as rapsyn) is a crucial scaffolding protein involved in the clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction and in the central nervous system. The study of RAPSN has gained significant attention due to its essential role in synaptic transmission and neurotransmission processes. Mutations and dysregulation of RAPSN have been implicated in congenital myasthenic syndromes, a group of inherited disorders characterized by weakness and fatigability of voluntary muscles, highlighting its importance in muscle function and neuromuscular disorders. Furthermore, RAPSN's interactions with various signaling molecules and receptors suggest that it may also play a role in synaptic plasticity, learning, and memory, thus making it a potential target for therapeutic interventions in neurodegenerative diseases and cognitive disorders. Research into the structural and functional properties of RAPSN, alongside its role in receptor clustering and signaling, could unveil new insights into synaptic integrity and the molecular mechanisms underpinning neuromuscular transmission. As a result, the recombinant expression of RAPSN in various model systems is being explored to elucidate its functional dynamics, interactions with nAChRs, and its potential role in developing targeted treatments for related disorders. These studies aim to advance our understanding of synaptic formation and maintenance, thereby paving the way for novel approaches in treating conditions associated with synaptic dysfunction.
