Analytical Data
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Gene name
AKAP5
- Application
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Alternative Names
AKAP75; AKAP79; H21; A-kinase anchor protein 79 kDa; cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
D3YVF0
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Expression Region
Met1~Gln161
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Molecular Weight
63kDa
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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
AKAP5 (A-Kinase Anchoring Protein 5) is a crucial scaffold protein that plays a significant role in the compartmentalization of protein kinase A (PKA) signaling within cells. Research into AKAP5 has gained attention due to its involvement in various physiological processes, including cardiac function, cell adhesion, and spatial regulation of signaling pathways. The reorganization of AKAP5 is particularly relevant in the context of disease states, such as heart failure and cancer, where altered PKA signaling can contribute to pathophysiology. Furthermore, the ability of AKAP5 to interact with multiple signaling molecules places it at the intersection of various cellular pathways, making it a potential therapeutic target. Studies using recombinant AKAP5 proteins allow researchers to dissect its functional roles and interactions at a molecular level, facilitating the understanding of its contributions to health and disease. This research underscores the importance of spatially organized signaling in cellular biology and highlights the therapeutic potential of targeting AKAP5 in various diseases where signaling dysregulation is a key factor. As a result, the engineering and characterization of recombinant AKAP5 proteins could provide valuable insights into the mechanisms underlying its action and pave the way for novel treatment strategies.
