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AB133104

HIF-1 alpha Transcription Factor Assay Kit

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(27 Publications)

HIF-1 alpha Transcription Factor Assay (ab133104) is a non-radioactive, sensitive method for detecting specific transcription factor DNA binding activity in nuclear extracts and whole cell lysate.

View Alternative Names

BHLHE78, MOP1, PASD8, HIF1A, Hypoxia-inducible factor 1-alpha, HIF-1-alpha, HIF1-alpha, ARNT-interacting protein, Basic-helix-loop-helix-PAS protein MOP1, Class E basic helix-loop-helix protein 78, Member of PAS protein 1, PAS domain-containing protein 8, bHLHe78

4 Images
Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)
  • FuncS

Supplier Data

Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)

Assay of nuclear extract from stimulated HeLa cells (100 µM CoCl2) and non-stimulated HeLa cells.

Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)
  • FuncS

Lab

Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)

Titration of positive control, background signal subtracted (duplicates; +/- SD).

Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)
  • FuncS

Lab

Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)

HEK293 cells were treated with 1 mM deferoxamine mesylate (DFO) for 1 or 24 hours. 40 micoliters of nuclear lysates (ab113474; corresponding to 4e6 cells) were tested in duplicates (+/- SD).

Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)
  • FuncS

Lab

Functional Studies - HIF-1 alpha Transcription Factor Assay Kit (AB133104)

Titration of positive control with different volumes of inhibitor (TA), background signal subtracted (duplicates; +/- SD).

Key facts

Detection method

Colorimetric

Sample types

Cell culture extracts, Cell Lysate

Reacts with

Mouse, Rat, Human

Results type

Semi-Quantitative

Assay Platform

Microplate reader

Product details

HIF-1 alpha Transcription Factor Assay (ab133104) is a non-radioactive, sensitive method for detecting specific transcription factor DNA binding activity in nuclear extracts and whole cell lysate.

A 96-well enzyme-linked immunosorbent assay (ELISA) replaces the cumbersome radioactive electrophoretic mobility shift assay (EMSA). A specific double stranded DNA (dsDNA) sequence containing the HIF-1 alpha response element (5'-ACGTG-3') is immobilized to the wells of a 96-well plate. HIF-1 alpha contained in a nuclear extract, binds specifically to the HIF-1 alpha response element. The HIF transcription factor complex is detected by addition of a specific primary antibody directed against HIF-1 alpha. A secondary antibody conjugated to HRP is added to provide a sensitive colorimetric readout at 450 nm.

REACH authorisation
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It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.

What's included?

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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
Multi
Appropriate long-term storage conditions
Multi
Storage information
Please refer to protocols

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

HIF-1 alpha also known as hypoxia-inducible factor 1-alpha is a transcription factor critical in cellular response to low oxygen levels. Its molecular weight usually ranges from 93 to 120 kDa. You can find HIF-1 alpha expressed in tissues throughout the body but its expression significantly increases under hypoxic conditions. Researchers often use the HIF-1a ELISA to measure its expression levels. HIF-1 alpha forms a complex with other proteins to perform its functions effectively.
Biological function summary

HIF-1 alpha regulates gene expression in response to hypoxic conditions in cells. It forms a complex with HIF-1 beta to activate transcription of various genes involved in energy metabolism angiogenesis and erythropoiesis. HIF-1 alpha enables cells to adapt to reduced oxygen availability allowing for cellular survival and function under stress. It plays an important role in promoting the expression of genes like VEGF and EPO which are important for vascular and red blood cell development respectively.

Pathways

HIF-1 alpha plays an integral role in the hypoxia signaling pathway and the glycolytic pathway. In the hypoxia signaling pathway HIF-1 alpha partners with VHL (Von Hippel-Lindau) protein that regulates its degradation under normal oxygen conditions. When oxygen levels drop HIF-1 alpha avoids degradation stabilizes and translocates into the nucleus to initiate transcription of hypoxia-responsive genes. The glycolytic pathway involvement highlights its function in adapting energy production under hypoxic conditions through collaboration with enzymes and transporters associated with glycolysis.

HIF-1 alpha has been implicated in cancer and ischemic diseases. Its role in promoting angiogenesis and metabolic adaptation makes it a contributor to tumor growth and survival collaborating with oncogenes such as c-Myc. In ischemic diseases like stroke or myocardial infarction HIF-1 alpha's ability to induce protective responses can mitigate tissue damage through regulation of survival pathways. Understanding these interactions helps in the development of therapeutic strategies targeting HIF-1 alpha in disease contexts.

Product protocols

Target data

Functions as a master transcriptional regulator of the adaptive response to hypoxia (PubMed : 11292861, PubMed : 11566883, PubMed : 15465032, PubMed : 16973622, PubMed : 17610843, PubMed : 18658046, PubMed : 20624928, PubMed : 22009797, PubMed : 30125331, PubMed : 9887100). Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia (PubMed : 11292861, PubMed : 11566883, PubMed : 15465032, PubMed : 16973622, PubMed : 17610843, PubMed : 20624928, PubMed : 22009797, PubMed : 30125331, PubMed : 9887100). Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease (PubMed : 22009797). Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300 (PubMed : 16543236, PubMed : 9887100). Activity is enhanced by interaction with NCOA1 and/or NCOA2 (PubMed : 10594042). Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP (PubMed : 10202154, PubMed : 10594042). Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (PubMed : 19528298).. (Microbial infection) Upon infection by human coronavirus SARS-CoV-2, is required for induction of glycolysis in monocytes and the consequent pro-inflammatory state (PubMed : 32697943). In monocytes, induces expression of ACE2 and cytokines such as IL1B, TNF, IL6, and interferons (PubMed : 32697943). Promotes human coronavirus SARS-CoV-2 replication and monocyte inflammatory response (PubMed : 32697943).
See full target information HIF1A

Publications (27)

Recent publications for all applications. Explore the full list and refine your search

Cell death & disease 16:149 PubMed40032849

2025

Transcription factor ONECUT3 regulates HDAC6/HIF-1α activity to promote the Warburg effect and tumor growth in colorectal cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Ruixue Huo,Weihan Li,Hao Wu,Kexin He,Hao Wang,Shan Zhang,Shu-Heng Jiang,Rongkun Li,Junli Xue

Journal of translational medicine 22:1135 PubMed39707401

2024

Ubiquitin-specific protease 7 maintains c-Myc stability to support pancreatic cancer glycolysis and tumor growth.

Applications

Unspecified application

Species

Unspecified reactive species

Jichun Gu,Xi Xiao,Caifeng Zou,Yishen Mao,Chen Jin,Deliang Fu,Rongkun Li,Hengchao Li

Nature communications 15:8624 PubMed39366973

2024

MDM2 induces pro-inflammatory and glycolytic responses in M1 macrophages by integrating iNOS-nitric oxide and HIF-1α pathways in mice.

Applications

Unspecified application

Species

Unspecified reactive species

Kelvin Ka-Lok Wu,Xiaofan Xu,Manyin Wu,Xiaomu Li,Moinul Hoque,Gloria Hoi Yee Li,Qizhou Lian,Kekao Long,Tongxi Zhou,Hailong Piao,Aimin Xu,Hannah Xiaoyan Hui,Kenneth King-Yip Cheng

International journal of biological sciences 19:2613-2629 PubMed37215979

2023

ACE2 negatively regulates the Warburg effect and suppresses hepatocellular carcinoma progression via reducing ROS-HIF1α activity.

Applications

Unspecified application

Species

Unspecified reactive species

Fangyuan Dong,Hui Li,Limin Liu,Lin-Li Yao,Jiaofeng Wang,Danni Xiang,Jianxia Ma,Gansheng Zhang,Shan Zhang,Jun Li,Shu-Heng Jiang,Xiaona Hu,Jie Chen,Zhijun Bao

Scientific reports 13:6528 PubMed37085612

2023

Contribution of HIF-1α/BNIP3-mediated autophagy to lipid accumulation during irinotecan-induced liver injury.

Applications

Unspecified application

Species

Unspecified reactive species

Congjian Shi,Zhenghong Zhang,Renfeng Xu,Yan Zhang,Zhengchao Wang

Nature communications 13:5208 PubMed36064857

2022

Adipocyte-derived lactate is a signalling metabolite that potentiates adipose macrophage inflammation via targeting PHD2.

Applications

Unspecified application

Species

Unspecified reactive species

Tianshi Feng,Xuemei Zhao,Ping Gu,Wah Yang,Cunchuan Wang,Qingyu Guo,Qiaoyun Long,Qing Liu,Ying Cheng,Jin Li,Cynthia Kwan Yui Cheung,Donghai Wu,Xinyu Kong,Yong Xu,Dewei Ye,Shuang Hua,Kerry Loomes,Aimin Xu,Xiaoyan Hui

Biomedical reports 17:79 PubMed36158318

2022

Inhibitory effect of low‑intensity pulsed ultrasound on the fibrosis of the infrapatellar fat pad through the regulation of HIF‑1α in a carrageenan‑induced knee osteoarthritis rat model.

Applications

Unspecified application

Species

Unspecified reactive species

Takashi Kitagawa,Hirohisa Kawahata,Motokuni Aoki,Shintarou Kudo

Theranostics 12:3196-3216 PubMed35547748

2022

Neuronal STAT3/HIF-1α/PTRF axis-mediated bioenergetic disturbance exacerbates cerebral ischemia-reperfusion injury via PLA2G4A.

Applications

Unspecified application

Species

Unspecified reactive species

Weili Jin,Jixing Zhao,Eryan Yang,Yunfei Wang,Qixue Wang,Ye Wu,Fei Tong,Yanli Tan,Junhu Zhou,Chunsheng Kang

Journal of the American College of Cardiology 79:632-647 PubMed35177192

2022

Splenic Marginal Zone B Lymphocytes Regulate Cardiac Remodeling After Acute Myocardial Infarction in Mice.

Applications

Unspecified application

Species

Unspecified reactive species

Yanyi Sun,Cristina Pinto,Stéphane Camus,Vincent Duval,Paul Alayrac,Ivana Zlatanova,Xavier Loyer,Jose Vilar,Mathilde Lemitre,Angélique Levoye,Meritxell Nus,Hafid Ait-Oufella,Ziad Mallat,Jean-Sébastien Silvestre

Cell reports 38:110309 PubMed35108537

2022

Macrophage IL-1β promotes arteriogenesis by autocrine STAT3- and NF-κB-mediated transcription of pro-angiogenic VEGF-A.

Applications

Unspecified application

Species

Unspecified reactive species

Chris S Mantsounga,Cadence Lee,Jade Neverson,Sheila Sharma,Abigail Healy,Joshua M Berus,Crystal Parry,Nicolle M Ceneri,Francesc López-Giráldez,Hyung J Chun,Qing Lu,Frank Sellke,Gaurav Choudhary,Alan R Morrison
View all publications
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