Analytical Data
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Gene name
SAMD12
- Application
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Alternative Names
SAMD12; Sterile alpha motif domain-containing protein 12; SAM domain-containing protein 12
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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
Q8N8I0
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Expression Region
1-201 aa
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AA Sequence
MAVEALHCGL NPRGIDHPAH AEGIKLQIEG EGVESQSIKN KNFQKVPDQK GTPKRLQAEA ETAKSATVKL SKPVALWTQQ DVCKWLKKHC PNQYQIYSES FKQHDITGRA LLRLTDKKLE RMGIAQENLR QHILQQVLQL KVREEVRNLQ LLTQGTLLLP DGWMDGEIRR KTTLLLGQTG VRENLLLFLH RISIIENSIQ I
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Molecular Weight
22.9 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
The SAMD12 gene, which encodes the SAM domain-containing protein 12, has garnered attention in recent years due to its potential role in various biological processes, including cellular differentiation, proliferation, and stress responses. Research indicates that SAMD12 may be involved in the regulation of gene expression, influencing pathways associated with neurological disorders and metabolic diseases. Its unique structure, characterized by the presence of a SAM domain, suggests that it may participate in protein-protein interactions, which could be crucial for its function in cellular signaling. Recent studies have explored the implications of SAMD12 expression in conditions such as obesity and diabetes, highlighting its relevance in understanding the underlying mechanisms of these diseases. Furthermore, investigations into the post-translational modifications of SAMD12 could provide insights into its regulatory functions and interactions within the cellular milieu. The recombinant expression of SAMD12 protein is a vital step in elucidating its structure-function relationships, enabling researchers to dissect its roles in health and disease. As a result, SAMD12 is emerging as a promising target for therapeutic interventions, necessitating further research to explore its full potential and clarify its biological significance across various physiological contexts.
