Analytical Data
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Gene name
DOC2a
- Application
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Alternative Names
DOC2a;Double C2-like domain-containing Protein alpha
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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
Q14183
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Expression Region
1-400aa
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AA Sequence
MRGRRGDRMT INIQEHMAIN VCPGPIRPIR QISDYFPRGP GPEGGGGGGG EAPAHLVPLA LAPPAALLGA TTPEDGAEVD SYDSDDATAL GTLEFDLLYD RASCTLHCSI LRAKGLKPMD FNGLADPYVK LHLLPGACKA NKLKTKTQRN TLNPVWNEDL TYSGITDDDI THKVLRIAVC DEDKLSHNEF IGEIRVPLRR LKPSQKKHFN ICLERQVPLA SPSSMSAALR GISCYLKELE QAEQGQGLLE ERGRILLSLS YSSRRRGLLV GILRCAHLAA MDVNGYSDPY VKTYLRPDVD KKSKHKTCVK KKTLNPEFNE EFFYEIELST LATKTLEVTV WDYDIGKSND FIGGVSLGPG ARGEARKHWS DCLQQPDAAL ERWHTLTSEL PPAAGALSSA
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Molecular Weight
43.9 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
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Protein Description
DOC2a, or double C2 domain-containing protein A, is an important member of the DOC2 protein family, which is implicated in various cellular processes, particularly in neuronal function and synaptic transmission. Research into DOC2a has gained momentum due to its role as a calcium sensor that modulates the release of neurotransmitters in response to calcium signaling. This protein contains two C2 domains, which are characteristic of proteins involved in calcium-dependent membrane interactions, suggesting its potential involvement in synaptic vesicle trafficking and exocytosis. Dysregulation of DOC2a has been linked to several neurological disorders, making it a target for understanding synaptic dynamics and developing therapeutic strategies. Furthermore, the study of DOC2a recombinant proteins has facilitated the elucidation of its structural and functional properties, enhancing our understanding of its mechanism of action in cellular contexts. In summary, the exploration of DOC2a recombinant proteins is crucial for unraveling the complexities of synaptic signaling and the potential impact on neurological health and disease.











