Analytical Data
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Gene name
MORN4
- Application
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Alternative Names
44050 protein; C10orf83 ; Chromosome 10 open reading frame 83; MORN repeat containing 4 ; MORN repeat-containing protein 4; Morn4; MORN4_HUMAN; Protein 44050; Retinophilin
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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
Q8NDC4
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Expression Region
1-146 aa
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AA Sequence
MTLTKGSFTY SSGEEYRGEW KEGRRHGFGQ LMFADGGTYL GHFENGLFNG FGVLTFSDGS RYEGEFAQGK FNGVGVFIRY DNMTFEGEFK NGRVDGFGLL TFPDGSHGIP RNEGLFENNK LLRREKCSAI VQRAQSASKS ARNLTA
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Molecular Weight
16.2 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
MORN4, a member of the MORN (membrane occupation and recognition nexus) domain-containing proteins, has gained attention in recent years due to its potential roles in various cellular processes, including signal transduction, cytoskeletal organization, and membrane dynamics. The MORN domain is characterized by its ability to interact with membrane lipids, suggesting a key function in cellular signaling and membrane-associated processes. Research indicates that MORN4 is involved in the regulation of cell proliferation and apoptosis, making it a crucial player in cancer biology. Furthermore, MORN4 has been implicated in the pathogenesis of several diseases, including neurodegenerative disorders, where its dysregulation may contribute to disease progression. As a result, understanding the structure and function of MORN4 at the molecular level could provide insights into its biological significance and open new avenues for therapeutic intervention. Consequently, the study of MORN4 recombinant proteins is essential for elucidating its functional mechanisms, interactions with other cellular components, and potential as a biomarker or therapeutic target in various conditions.
