Analytical Data
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Gene name
CCM2
- Application
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Alternative Names
CCM2；C7orf22；Cerebral cavernous malformations 2 Protein
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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
Q9BSQ5-3
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Expression Region
66-353aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSEVKYLGQLTSIPGYLNPSSRTEILHFI DNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAV SYVRDDAAHLVVLKTDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHS KTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHE FCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITD SFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIE ALGCSMDQDSA
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Molecular Weight
34 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
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Protein Description
CCM2, or cerebral cavernous malformation 2, is a protein linked to the formation of cerebral cavernous malformations, which are vascular lesions in the brain that can lead to seizures, hemorrhage, or neurological deficits. Mutations in the CCM2 gene are known to be associated with familial and sporadic cases of these malformations. Research on CCM2 recombinant proteins has gained traction due to their potential role in elucidating the molecular mechanisms underlying the development and progression of cavernous malformations. Understanding the functional properties of CCM2 and its interactions with other cellular components is critical, as it may reveal therapeutic targets for the treatment of these conditions. Furthermore, studies involving CCM2 can provide insights into vascular development and maintenance, highlighting its significance in broader contexts such as angiogenesis and endothelial cell biology. This research area has the potential to advance our knowledge of CCM pathophysiology and inform the development of novel strategies for prevention and management of cerebrovascular diseases associated with CCM2 mutations.
