|Tested species reactivity||Bovine, Dog, Human, Mouse, Rat|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Human HIF-1 alpha amino acids 329-530.|
|Storage buffer||sodium borate|
|Storage Conditions||4° C, store in dark|
|Tested Applications||Dilution *|
|Immunocytochemistry (ICC)||10 µg/ml|
|Immunofluorescence (IF)||10 µg/ml|
|Immunohistochemistry (Frozen) (IHC (F))||1:100-1:5000|
|Immunohistochemistry (Paraffin) (IHC (P))||1:100-1:5000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Suggested positive control: Cos7 CoCl2-treated nuclear extract.
Hypoxia contributes significantly to the pathophysiology of major categories of human disease, including myocardial and cerebral ischemia, cancer, pulmonary hypertension, congenital heart disease and chronic obstructive pulmonary disease.
HIF-1 is a nuclear protein involved in mammalian oxygen homeostasis. This occurs as a posttranslational modification by prolyl hydroxylation. HIF-1 is a heterodimer composed of HIF-1 alpha and HIF-1 beta subunits. Both subunits are constantly translated. However, under normoxic conditions, human HIF-1 alpha is hydroxylated at Pro402 or Pro564 by a set of HIF prolyl hydroxylases, is polyubiquinated, and eventually degraded in proteosomes. Under hypoxic conditions, the lack of hydroxylation prevents HIF degradation and increases transcriptional activity. Therefore, the concentration of HIF-1 alpha increases in the cell. In contrast, HIF-1 beta remains stable under either condition. HIF hydroxylases provide insight into hypoxic cell responses, which may be used to help isolate therapeutic targets.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.