Analytical Data
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Gene name
BHLHE22
- Application
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Alternative Names
Basic helix loop helix domain containing class B 5 1 2 5; Basic helix loop helix Protein 5; Beta3
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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
Q8NFJ8
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Expression Region
1-381aa
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AA Sequence
MERGMHLGAA AAGEDDLFLH KSLSASTSKR LEAAFRSTPP GMDLSLAPPP RERPASSSSS PLGCFEPADP EGAGLLLPPP GGGGGGSAGS GGGGGGGVGV PGLLVGSAGV GGDPSLSSLP AGAALCLKYG ESASRGSVAE SSGGEQSPDD DSDGRCELVL RAGVADPRAS PGAGGGGAKA AEGCSNAHLH GGASVPPGGL GGGGGGGSSS GSSGGGGGSG SGSGGSSSSS SSSSKKSKEQ KALRLNINAR ERRRMHDLND ALDELRAVIP YAHSPSVRKL SKIATLLLAK NYILMQAQAL EEMRRLVAYL NQGQAISAAS LPSSAAAAAA AAALHPALGA YEQAAGYPFS AGLPPAASCP EKCALFNSVS SSLCKQCTEK P
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Molecular Weight
68.31 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
BHLHE22, a member of the basic helix-loop-helix (bHLH) transcription factor family, plays a critical role in various biological processes, including circadian rhythm regulation, cell differentiation, and immune responses. Recent studies have highlighted its potential involvement in the pathology of several diseases, such as cancer and metabolic disorders. Characterizing BHLHE22 and its interactions at the molecular level is essential for understanding its function. The use of recombinant protein technology has enabled researchers to produce BHLHE22 in large quantities, facilitating detailed biochemical analyses and structural studies. This approach not only helps in elucidating the transcriptional regulatory mechanisms governed by BHLHE22 but also aids in identifying potential therapeutic targets. By investigating its binding partners and downstream signaling pathways, researchers aim to uncover how BHLHE22 contributes to cellular homeostasis and pathology. Moreover, understanding its post-translational modifications could provide insights into its functional versatility in different physiological contexts. Given the emerging evidence of its role in disease progression, BHLHE22 represents a promising candidate for novel drug development, making its study increasingly pertinent in contemporary biomedical research.
