Analytical Data
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Gene name
G10
- Application
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Alternative Names
Bud31; BUD31 homolog (S. cerevisiae); BUD31_HUMAN; Cwc14; EDG 2; EDG2; fSAP17; Functional spliceosome associated protein 17; G10; G10 maternal transcript homolog; Maternal G10 transcript; Protein BUD31 homolog; Protein EDG-2; Protein G10 homolog; YCR063W
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P41223
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Expression Region
1-144aa
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AA Sequence
MPKVKRSRKAPPDGWELIEPTLDELDQKMREAETEPHEGKRKVESLWPIFRIHHQKTRYIFDLFYKRKAISRELYEYCIKEGYADKNLIAKWKKQGYENLCCLRCIQTRDTNFGTNCICRVPKSKLEVGRIIECTHCGCRGCSG
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Molecular Weight
41.47 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 research background of G10 recombinant proteins is rooted in the field of biotechnology and molecular biology, particularly focusing on the production and application of proteins for therapeutic and diagnostic purposes. G10 proteins are often derived from specific genes that encode for proteins with potential functions in cell signaling, immune response, or structural integrity. The development of recombinant DNA technology has enabled scientists to manipulate these genes, facilitating the expression of G10 proteins in host systems, such as bacteria, yeast, or mammalian cells. This capability not only allows for large-scale production but also enables the study of the protein's structure and function. As interest in personalized medicine and targeted therapies grows, G10 recombinant proteins are being explored for their potential role in disease treatment, including cancer and infectious diseases. Advanced characterization techniques, such as X-ray crystallography and mass spectrometry, are frequently employed to elucidate the functional mechanisms of these proteins, paving the way for innovative therapeutic strategies. Researchers continue to investigate the stability, efficacy, and potential applications of G10 recombinant proteins, aiming to address critical challenges in protein engineering and biopharmaceutical development. Overall, the exploration of G10 recombinant proteins highlights the synergy between genetic engineering and therapeutic advancement, underscoring their significance in modern medical research.
