Analytical Data
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Gene name
DBNDD2
- Application
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Alternative Names
Casein kinase-1 binding protein ;CK1BPHSMNP1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BQY9
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Expression Region
1-161aa
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Molecular Weight
33.5 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
DBNDD2 (Dynamin Binding Domain Containing 2) is a protein that has gained attention in recent years due to its potential roles in cellular processes and signaling pathways. The characterization of DBNDD2 is particularly important as it is associated with important cellular functions such as membrane trafficking, cytoskeletal dynamics, and potentially in the pathogenesis of various diseases. Researchers have focused on the molecular mechanisms that govern its function, as understanding these could shed light on how DBNDD2 interacts with other proteins, particularly dynamins, which are vital for endocytosis and vesicle transport. The exploration of DBNDD2’s role in neurobiology is of particular interest, given its potential influence on synaptic plasticity and neuronal health. Moreover, dysregulation of proteins involved in these processes is often linked to neurodegenerative diseases, making DBNDD2 a candidate for further investigation as a therapeutic target. Recent studies utilizing recombinant protein techniques aim to elucidate its structure and functional properties. Through these investigations, scientists aim to build a comprehensive understanding of how DBNDD2 contributes to cellular homeostasis and pathology, which could open new avenues for therapeutic interventions in related disorders. Understanding the biochemistry of DBNDD2 could thus lead to significant advancements in the field of molecular biology and medicine.
