Analytical Data
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Gene name
CALCB
- Application
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Alternative Names
CALCB；CALC2；Calcitonin gene-related peptide 2
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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
P10092
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Expression Region
1-118aa
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AA Sequence
MGFRKFSPFL ALSILVLYQA GSLQAAPFRS ALESSPDPAT LSKEDARLLL AALVQDYVQM KASELKQEQE TQGSSSAAQK RACNTATCVT HRLAGLLSRS GGMVKSNFVP TNVGSKAF
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Molecular Weight
36 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
CALCB (Calcitonin Gene-Related Peptide Beta) is a neuropeptide that plays significant roles in various physiological processes, including pain modulation, cardiovascular regulation, and neurogenic inflammation. Its abundant presence in the central and peripheral nervous systems has piqued interest among researchers investigating its potential therapeutic applications, particularly in pain management and neurodegenerative diseases. The complexity of CALCB's biological functions necessitates advanced study into its structure and activity. Recombinant protein production of CALCB allows for detailed characterization of its properties and interactions with receptors and other biomolecules. This research not only enhances our understanding of CALCB's role in signaling pathways but also aids in the development of novel treatments targeting conditions linked to CALCB dysregulation, such as chronic pain syndromes and migraine. Furthermore, the recombinant CALCB can be utilized in drug discovery processes, providing a platform for high-throughput screening of potential pharmacological agents. Overall, the investigation into CALCB recombinant proteins is crucial for unlocking new therapeutic strategies and improving outcomes for patients suffering from various neurological disorders.
