Analytical Data
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Gene name
YBX2
- Application
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Alternative Names
(Contrin)(DNA-binding Protein C)(Dbpc)(Germ cell-specific Y-box-binding Protein)(MSY2 homolog)
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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
Q9Y2T7
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Expression Region
1-364 aa
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AA Sequence
MSEVEAAAVATAVPAATVPATAAGVVAVVVPVPAGEPQKGGGAGGGGGAASGPAAGTPSAPGSRTPGNPATAVSGTPAPPARSQADKPVLAIQVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKRNNPRKFLRSVGDGETVEFDVVEGEKGAEATNVTGPGGVPVKGSRYAPNRRKSRRFIPRPPSVAPPPMVAEIPSAGTGPGSKGERAEDSGQRPRRWCPPPFFYRRRFVRGPRPPNQQQPIEGTDRVEPKETAPLEGHQQQGDERVPPPRFRPRYRRPFRPRPRQQPTTEGGDGETKPSQGPADGSRPEPQRPRNRPYFQRRRQQAPGPQQAPGPRQPAAPETSAPVNSGDPTTTILE
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Molecular Weight
65 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
YBX2, a member of the Y-box binding protein family, plays a crucial role in various cellular processes, including transcription regulation, RNA stabilization, and cellular stress response. It is involved in several key pathways, such as cell proliferation, differentiation, and apoptosis, making it a significant protein in cancer biology and other diseases. Recent studies have highlighted its potential as a therapeutic target, as aberrant expression of YBX2 is associated with poor prognosis in various cancers. Understanding the structure and function of YBX2 through recombinant protein studies can provide insights into its biological mechanisms and interactions with other cellular molecules. Moreover, the production of YBX2 recombinant protein offers a valuable tool for investigating its role in molecular biology and for developing potential therapeutic strategies. As research progresses, the YBX2 protein is emerging as an important subject for further investigation in the context of disease modeling, drug development, and understanding the molecular underpinnings of tumorigenesis.
