Analytical Data
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Gene name
CAMP
- Application
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Alternative Names
CAMP；Calmodulin-regulated spectrin-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
P49913
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Expression Region
1-170aa
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AA Sequence
MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
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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
The study of CAMP (cyclic adenosine monophosphate) recombinant proteins has gained significant traction in the fields of biochemistry and molecular biology due to their crucial role in cellular signaling pathways. CAMP is a vital second messenger that mediates various physiological processes, including metabolism, cell growth, and gene expression. Research has demonstrated that alterations in CAMP signaling can lead to various diseases, including cancer and metabolic disorders. Recombinant proteins that mimic or modulate the effects of CAMP are essential for understanding the mechanisms of its action and for developing targeted therapies. Advances in genetic engineering and protein expression techniques have enabled researchers to produce CAMP-related proteins and study their interactions with other cellular components. By elucidating the structure-function relationships of these proteins, researchers aim to uncover potential therapeutic targets and design innovative drugs that can regulate CAMP pathways. The ongoing exploration of CAMP recombinant proteins is pivotal for deciphering complex cellular responses and holds promise for novel clinical applications in treating diseases linked to dysregulated cAMP signaling.
