Analytical Data
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Gene name
Caspr
- Application
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Alternative Names
Caspr；CASPR；NRXN4；Contactin-associated Protein 1
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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
P78357
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Expression Region
26-356aa
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AA Sequence
DEELVGPLYARSLGASSYYSLLTAPRFARLHGISGWSPRIGDPNPWLQIDLMKKHRIRAVATQGSFNSWDWVTRYMLLYGDRVDSWTPFYQRGHNSTFFGNVNESAVVRHDLHFHFTARYIRIVPLAWNPRGKIGLRLGLYGCPYKADILYFDGDDAISYRFPRGVSRSLWDVFAFSFKTEEKDGLLLHAEGAQGDYVTLELEGAHLLLHMSLGSSPIQPRPGHTTVSAGGVLNDQHWHYVRVDRFGRDVNFTLDGYVQRFILNGDFERLNLDTEMFIGGLVGAARKNLAYRHNFRGCIENVIFNRVNIADLAVRRHSRITFEGKVAFRCL
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Molecular Weight
53.8kDa
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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
Caspr, also known as Contactin-associated protein, is a crucial component of the axonal membrane in the central and peripheral nervous systems. It plays a significant role in maintaining the integrity of myelinated axons and is essential for the formation of paranodal structures, which facilitate proper nerve conduction. Research has shown that Caspr interacts with various proteins, such as Contactin, Caspr2, and neurofascin, to form complexes that are vital for the clustering of ion channels and adhesion at the nodal regions of myelinated fibers. Mutations or dysregulation of Caspr expression have been implicated in several neurological disorders, including multiple sclerosis and inherited neuropathies. Additionally, the understanding of Caspr's molecular structure and its interactions offers potential insights into therapeutic strategies for demyelinating diseases. Recent advancements in recombinant protein technology have enabled the production of Caspr in functional forms, allowing for in-depth studies into its structural and functional properties. These studies aim to unravel the precise mechanisms through which Caspr contributes to neurodevelopment and axonal stability, highlighting its importance in both physiology and pathophysiology. Overall, the ongoing research on Caspr provides valuable insights into the molecular underpinnings of myelination and presents a promising avenue for interventions in neurological diseases.
