Analytical Data
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Gene name
HIF1A
- Application
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Alternative Names
HIF1A;BHLHE78;MOP1;PASD8;Hypoxia-inducible factor 1-alpha
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Species
Human
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Source
E. coli
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Tag
N-terminal His-Tag
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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
575-826aa
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AA Sequence
RSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTAS PNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSE QNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
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Molecular Weight
28.7kDa
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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
Related Products
Identification
Protein Description
Hypoxia-inducible factor 1 alpha (HIF1A) is a crucial transcription factor that plays a significant role in cellular responses to oxygen deficiency, or hypoxia. Its importance emerged from studies linking HIF1A to various physiological and pathological processes, including metabolism, angiogenesis, and tumor progression. Under hypoxic conditions, HIF1A is stabilized and translocates to the nucleus, where it binds to hypoxia-responsive elements (HREs) in target genes, facilitating adaptive responses to low oxygen levels. Recent research has highlighted its potential as a therapeutic target in cancer treatment, where tumors exploit hypoxia to promote growth and resistance to therapies. Additionally, HIF1A's involvement in chronic diseases, such as cardiovascular diseases and metabolic disorders, has spurred interest in understanding its mechanisms and pathways. The study of HIF1A recombination protein focuses on deciphering its structure, function, and interaction with other cellular components, providing insights into its regulatory roles in various contexts. Advances in recombinant DNA technology have enabled the production of HIF1A fusion proteins, facilitating the investigation of its biological activities and the development of potential HIF1A-modulating drugs. This research is crucial for harnessing the therapeutic potential of targeting HIF1A in different diseases, aiming to improve clinical outcomes and pave the way for innovative treatment strategies.
