Analytical Data
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Gene name
HIF-1 alpha
- Application
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Alternative Names
ARNT-interacting protein;Basic-helix-loop-helix-PAS protein MOP1Class E basic helix-loop-helix protein 78 ;bHLHe78Member of PAS protein 1;PAS domain-containing protein 8
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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 90% as determined by SDS-PAGE.
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Uniprot
Q16665
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Expression Region
579-826aa
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Molecular Weight
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
Hypoxia-inducible factor 1-alpha (HIF-1α) is a critical transcription factor that plays a pivotal role in cellular responses to low oxygen levels (hypoxia). Its importance is underscored by its involvement in various physiological processes, including angiogenesis, metabolism, and cell survival. Under normoxic conditions, HIF-1α is continuously degraded; however, in hypoxic environments, it stabilizes, translocates to the nucleus, and dimerizes with HIF-1β to activate numerous target genes essential for adapting to oxygen deficiency. Research has shown that dysregulation of HIF-1α is implicated in multiple pathological conditions, including cancer, ischemic diseases, and inflammatory disorders. Its role in promoting tumor growth and survival has made HIF-1α a prime target for therapeutic interventions, driving the interest in the development of HIF-1α recombinant proteins for both basic research and clinical applications. These recombinant proteins can be used to dissect the molecular mechanisms underlying HIF-1α function, evaluate its potential as a drug target, and explore its role in disease pathophysiology. Recent advancements in recombinant protein technology have facilitated the production and purification of functional HIF-1α proteins, enabling researchers to investigate their structure-function relationships and interactions with downstream signaling pathways. The ongoing studies on HIF-1α not only enhance our understanding of hypoxic responses but also pave the way for novel therapeutic strategies aimed at modulating its activity for disease treatment.
