Hypoxia Inducible Factor 1a (HIF-1a) (FITC)

Referencia H9807-04-FITC-100ul

embalaje : 100ul

Marca : US Biological

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H9807-04-FITC Hypoxia Inducible Factor 1a (HIF-1a) (FITC)

Clone Type
Polyclonal
Host
rabbit
Source
human
Swiss Prot
Q16665
Isotype
IgG
Grade
Affinity Purified
Applications
ChIP FLISA IC IF IHC IP WB
Crossreactivity
Bo Ca Gp Hu Mk Mo Rt Xe
Shipping Temp
Blue Ice
Storage Temp
-20°C

Hypoxia Inducible Factor 1 (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.

Applications:
Suitable for use in FLISA, Western Blot, Gel Shift Assays, Immunofluorescence/Immunocytochemistry, Immunoprecipitation and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
Optimal dilutions to be determined by the researcher.

Storage and Stability:
Store product at 4°C if to be used immediately within two weeks. For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C. Aliquots are stable at -20°C for 12 months after receipt. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer.
Caution: FITC conjugates are sensitive to light. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Applications
Product Type: Pab|Isotype: IgG|Host: rabbit|Source: human|Concentration: Not Determined |Form: Supplied as a liquid in PBS, 0.05% sodium azide. Labeled with Fluorescein isothiocyanate (FITC). |Purity: Purified by immunoaffinity chromatography.|Immunogen: Fusion protein corresponding to the internal region, aa432-528, of human HIF-1a |Specificity: Recognizes human Hypoxia Inducible Factor 1a. Species Crossreactivity: rat, primate, xenopus, mouse, bovine, canine, Guinea pig, zebrafish||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Immunogen
Fusion protein corresponding to the internal region, aa432-528, of human HIF-1a
Form
Supplied as a liquid in PBS, 0.05% sodium azide. Labeled with Fluorescein isothiocyanate (FITC).
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes human Hypoxia Inducible Factor 1a. Species Crossreactivity: rat, primate, xenopus, mouse, bovine, canine, Guinea pig, zebrafish
References
1. Raina S, et al. Anti-VEGF treatment accelerates polycystic kidney disease. Am J Physiol Renal Physiol. 2011 Jun 15.[PMID 21677148]. 2. Wang Y, et al. MicroRNA-138 modulates DNA damage response by repressing histone H2AX expression. Mol Cancer Res. 2011 Jun 21.[PMID 21693595]. 3. Belibi F, et al. Hypoxia-inducible factor 1{alpha} (HIF-1 {alpha}) and autophagy in polycystic kidney disease (PKD). Am J Physiol Renal Physiol. 2011.[PMID 21270095]. 4. Filby CE, et al. Respir Res. 2010 Apr 23;11(1):42. 5. Xia X, Kung AL. Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia (BioMed Central). Genome Biol (2009). [PMID: 19828020]. 6. Frede S, et al. J Immunol. 2009 May 15;182(10):6470-6. [PMID: 19414801]. 7. Rane S, et al. Circ Res. 2009 Apr 10;104(7):879-86. 8. Naito Y, et al. Am J Physiol Heart Circ Physiol. 2009 Mar;296(3):H585-93. 9. Botusan IR, et al. Proc Natl Acad Sci USA. 2008 Dec 9;105(49):19426-31. 10. Land SC, Wilson SM. Antioxid Redox Signal. 2005 Jan-Feb;7(1-2):92-107. 11. Westfall SD, et al. Stem Cells Dev. 2008 Oct;17(5):869-81. 12. Trollmann R, et al. Am J Physiol Regul Integr Comp Physiol. 2008 Dec;295(6):R1973-81. 13. Meyuhas R, et al. Mol Cancer Res. 2008 Sep;6(9):1397-409. 14. Nikinmaa M, et al. J Exp Biol. 2008 Jun;211(Pt 12):1999-2004. 15. Zhang H, et al. J Biol Chem. 2008 Apr 18;283(16):10892-903. 16. Piantadosi CA, Suliman HB. J Biol Chem. 2008 Apr 18;283(16):10967-77. 17. Ohtomo S, et al. Nephrol Dial Transplant. 2008 Apr;23(4):1166-72. 18. Lauzier MC, et al. Mol Pharmacol. 2008 Jul;74(1):282-8. 19. Singh RP, Gu M, Agarwal R. Cancer Res. 2008 Mar 15;68(6):2043-50. 20. Sikder D, Kodadek T. Genes Dev. 2007 Nov 15;21(22):2995-3005.