Analytical Data
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Gene name
VAPB
- Application
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Alternative Names
VAPB；Vesicle-associated membrane Protein-associated Protein B/C
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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
O95292
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Expression Region
1-222aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAKVEQVLSL EPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGI IDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAK PEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPIVSKSLSSS LDDTEVKKVMEECKRLQGEVQRLREENKQFKEEDGLRMRKTVQSNSPISA LAPTGKEEGLST
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Molecular Weight
27 kDa
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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
VAPB (Vesicle-Associated Membrane Protein B) is a type II membrane protein that plays crucial roles in various cellular processes, including membrane trafficking, lipid metabolism, and the regulation of neuronal survival. Mutations in the VAPB gene have been associated with neurological disorders, particularly amyotrophic lateral sclerosis (ALS) and familial cases of spinal muscular atrophy. Given its pivotal role in cellular homeostasis and disease pathology, there has been a growing interest in studying VAPB recombinant proteins. These studies aim to elucidate the protein's structure-function relationships, its interaction with other cellular components, and how mutations affect these interactions. Using recombinant VAPB allows researchers to investigate its oligomerization, membrane association, and potential pathogenic mechanisms in a controlled environment. Moreover, understanding VAPB’s role in stress response pathways can provide insights into neuroprotective strategies and therapeutic approaches for ALS and related disorders. The research of VAPB recombinant proteins thus serves as a fundamental step towards dissecting the molecular underpinnings of neurodegenerative diseases and could pave the way for the development of targeted treatments.
