Analytical Data
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Gene name
DBNDD1
- Application
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Alternative Names
DBNDD1;Dysbindin domain-containing 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
Q9H9R9
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Expression Region
1-158aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEPPEG AGTGEIVKEA EVPQAALGVP AQGTGDNGHT PVEEEVGGIP VPAPGLLQVT ERRQPLSSVS SLEVHFDLLD LTELTDMSDQ ELAEVFADSD DENLNTESPA GLHPLPRAGY LRSPSWTRTR AEQSHEKQPL GDPERQATVL DTFLTVERPQ ED
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Molecular Weight
20 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
DBNDD1, or Dynamin Binding Protein Domain Containing 1, has emerged as a significant focus of research due to its potential roles in cellular mechanisms and disease pathology. This protein is primarily associated with the endocytosis process, facilitating the clathrin-mediated internalization of membrane proteins, which is critical for maintaining cellular homeostasis and signaling pathways. Recent studies suggest that DBNDD1 may be involved in various cellular processes, including synaptic vesicle recycling and the regulation of substrate transporters. Its dysregulation has been linked to several neurodegenerative disorders and other pathological conditions, highlighting its importance in both health and disease. Understanding the molecular mechanisms by which DBNDD1 functions could pave the way for novel therapeutic strategies, particularly in neurological diseases where endocytic trafficking is disrupted. Moreover, the development of recombinant DBNDD1 protein provides a valuable tool for elucidating its biological functions and interactions at a molecular level, which may offer insights into potential biomarkers or drug targets for diseases associated with its dysfunction. As research into DBNDD1 progresses, it holds promise not only for advancing our fundamental understanding of cell biology but also for contributing to the development of innovative approaches in treating complex diseases.
