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Recombinant Human HIF-1 alpha/HIF1A protein (His Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

N-His

Activity

not tested

Cat no : Eg0939

Validation Data Gallery

  • Purity of Recombinant Human HIF-1 alpha was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) stained using Coomassie blue.

    Purity of Recombinant Human HIF-1 alpha was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Human HIF-1 alpha protein Arg575-Asn826 (Accession# Q16665-1) with a His tag at the N-terminus.
GeneID 3091
Accession Q16665-1
PredictedSize 28.3 kDa
SDS-PAGE 34-60 kDa, reducing (R) condition
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

HIF1a, the major regulator of the cellular responses to hypoxia, consists of an oxygen-sensitive subunit, HIF1 alpha (HIF1A), and an oxygen-insensitive subunit, HIF1 beta (arylhydrocarbon receptor nuclear transporter [ARNT]). Under normal oxygen conditions, HIF1a is continuously produced and destroyed, in a process involving hydroxylation, interaction with von Hippel-Lindau (VHL) protein, polyubiquitylation and subsequent proteasomal degradation. Under hypoxic conditions, hydroxylation is impaired and HIF1a is stabilized. HIF1a localizes in cytoplasm in normoxia, but it can translocate into nuclear in response to hypoxia.

References:

1.J E Albina, et al. (2001) Am J Physiol Cell Physiol. 281 (6):C1971-7.
2.Wang GL, et al. (1995) Proc Natl Acad Sci U S A.92 (12):5510-4.
3.Kubis HP, et al. (2005) Biochim Biophys Acta. 1745 (2):187-95.