Analytical Data
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Gene name
HMGB2/HMG-2
- Application
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Alternative Names
HMG2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P26583
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Expression Region
Gly2~Pro187
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Molecular Weight
29kDa
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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
HMGB2 (High Mobility Group Box 2) is a non-histone chromosomal protein that plays a crucial role in various cellular processes, including transcription regulation, DNA repair, and chromatin remodeling. As a member of the high mobility group (HMG) protein family, HMGB2 is characterized by its ability to bind to DNA in a sequence-independent manner, facilitating the assembly of transcriptional machinery and enhancing gene expression. Research has demonstrated that HMGB2 is involved in numerous physiological and pathological contexts, including embryonic development, immune response, and cancer progression. Its expression levels are often dysregulated in various cancer types, making it a potential biomarker for tumorigenesis and a target for therapeutic interventions. The study of recombinant HMGB2 protein has become increasingly important in understanding its structural and functional dynamics, particularly in the context of DNA interactions. Methods to produce recombinant HMGB2, including expression systems such as E. coli or yeast, have enabled researchers to obtain purified protein necessary for in vitro assays and structural studies. These investigations aim to unveil the molecular mechanisms underlying HMGB2's role in chromatin architecture and its direct influence on gene regulation. Furthermore, characterizing the protein's binding affinity and specificity with different DNA structures can provide insights into its multifaceted functions in cellular processes. Overall, the research on recombinant HMGB2 is pivotal for elucidating its contribution to both normal cellular function and pathological conditions, ultimately guiding the development of novel therapeutic strategies targeting HMGB2-related pathways.
