Analytical Data
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Gene name
SAMD13
- Application
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Alternative Names
SAMD13;Sterile alpha motif domain-containing Protein 13
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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
Q5VXD3
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Expression Region
1-122aa
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AA Sequence
MANSLLEGVF AEVKEPCSLP MLSVDMENKE NGSVGVKNSM ENGRPPDPAD WAVMDVVNYF RTVGFEEQAS AFQEQEIDGK SLLLMTRNDV LTGLQLKLGP ALKIYEYHVK PLQTKHLKNN SS
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Molecular Weight
14 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
SAMD13, or Sterile Alpha Motif Domain 13, is a relatively less-studied protein that is increasingly being recognized for its potential roles in cellular processes and disease mechanisms. Research has suggested that SAMD13 may be involved in various biological functions, including cellular signaling, stress responses, and immune regulation. Notably, some studies have indicated its potential involvement in cancer progression and neurodegenerative diseases, highlighting its importance in maintaining cellular homeostasis. The protein's unique structural features include the presence of a sterile alpha motif domain, which is typically associated with protein-protein interactions. This property makes SAMD13 a candidate for further exploration in understanding the molecular pathways that contribute to pathological states. Recent advances in recombinant protein expression and purification techniques have enabled researchers to produce SAMD13 in sufficient quantities, paving the way for in-depth functional studies. Such investigations are critical for elucidating the protein's biological roles and for exploring its potential as a therapeutic target. Overall, the functional characterization of SAMD13 is a growing area of interest in biomedical research, with implications for understanding complex diseases and developing innovative treatment strategies.
