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Hypoxia Inducible Gene Domain

" in MedChemExpress (MCE) Product Catalog:

By Targets:	HIF/HIF Prolyl-Hydroxylase (3) Apoptosis (1) Biochemical Assay Reagents (1) Caspase (1) VEGFR (1)
By Research Areas:	Cancer (3) Metabolic Disease (1)

Inhibitors & Agonists

Screening Libraries

Biochemical Assay Reagents

Peptides

Targets Recommended: HIF/HIF Prolyl-Hydroxylase RIG-I-like receptor (RLR) Salt-inducible Kinase (SIK) Itk Discoidin Domain Receptor Epigenetic Reader Domain LAG-3 CGRP Receptor EHD Protein WDR5 MALT1 AIM2 YTHDF Dan family PASK/STK37 VISTA NEKs SHP1 PIKfyve BCL6 PNPLA3

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-139287

M1002 2 Publications Verification	HIF/HIF Prolyl-Hydroxylase	Cancer
M1002 is a hypoxia-inducible factor-2 (HIF-2) agonist, and can enhance the expression of HIF-2 target genes. M1002 shows synergy with prolyl-hydroxylase domain (PHD) inhibitors .

HY-P10426

cyclo(CLLFVY)	HIF/HIF Prolyl-Hydroxylase VEGFR	Cancer
cyclo(CLLFVY) is an inhibitor for hypoxia inducible factor-1 (HIF-1), with IC₅₀ of 19 μM (in U2OS) and 16 μM (in MCF-7). cyclo(CLLFVY) binds to the PAS-B domain of HIF-1α, inhibits HIF-1 dimerization and transcriptional activity. cyclo(CLLFVY) downregulates the expression of hypoxia response genes, such as VEGF and CAIX, exhibits antitumor against the HIF-1 associated cancers .

HY-125857B

Cytochrome C (Saccharomyces cerevisiae)	Biochemical Assay Reagents Apoptosis Caspase	Metabolic Disease
Cytochrome C (Saccharomyces cerevisiae) is a type C cytochrome located in the intermembrane space of the mitochondria. As an electron carrier, Cytochrome C (Saccharomyces cerevisiae) transfers electrons between complex III (cytochrome c reductase) and complex IV (cytochrome c oxidase, CIV) of the respiratory chain. Cytochrome C (Saccharomyces cerevisiae) can play a crucial role in triggering apoptosis by being released from the mitochondria into the cytosol .

HY-183583

HIF-2α-IN-18	HIF/HIF Prolyl-Hydroxylase	Cancer
HIF-2α-IN-18 is a selective HIF-2α inhibitor with a human IC₅₀ of 8.1 nM. HIF-2α-IN-18 binds to the HIF-2α PAS-B domain, induces conformational perturbations at the HIF-2α/ARNT dimerization interface, destabilizes the HIF-2α/ARNT heterodimer, and blocks HIF-2α-mediated transcriptional activity. HIF-2α-IN-18 inhibits hypoxia-induced expression of HIF-2α target genes EPO and SERPINE1, without inhibiting HIF-1α target genes PGK1 and PDK1. HIF-2α-IN-18 can be used for the research of clear cell renal cell carcinoma, hepatocellular carcinoma^[1].

Cat. No.	Product Name

HY-L045

Oxygen Sensing Compound Library	4,097 compounds
Oxygen homeostasis regulation is the most fundamental cellular process for adjusting physiological oxygen variations, and its irregularity leads to various human diseases, including cancer. Hypoxia is closely associated with cancer development, and hypoxia/oxygen-sensing signaling plays critical roles in the modulation of cancer progression. Hypoxia-inducible factor 1 (HIF-1) is a transcription factor that functions as a master regulator of oxygen homeostasis. A variety of HF-1 target genes have been identified thus far which encode proteins that play key roles in critical developmental and physiological processes including angiogenesis/vascular remodeling, erythropoiesis, glucose transport, glycolysis, iron transport, and cell proliferation/survival. HIF-1 is a heterodimeric transcription factor consisting of a constitutively expressed β-subunit and an oxygen-regulated α-subunit. The unique feature of HIF-1 is the regulation of HIF-1α expression and activity based upon the cellular O₂ concentration. Under normoxic conditions, hydroxylation of HIF-1α on these different proline residues is essential for HIF proteolytic degradation by promoting interaction with the von Hippel-Lindau tumor-suppressor protein (pVHL) through hydrogen bonding to the hydroxyproline-binding pocket in the pVHL β-domain. As oxygen levels decrease, hydroxylation of HIF decreases; HIF-1α then no longer binds pVHL, and becomes stabilized, allowing more of the protein to translocate to the cell’s nucleus, where it acts as a transcription factor, upregulating (often within minutes) the production of proteins that stimulate blood perfusion in tissues and thus tissue oxygenation. MCE offers a unique collection of 4,097 oxygen sensing related compounds targeting HIF/HIF Prolyl-Hydroxylase, MAPK/ERK, PI3K/AKT signaling pathways, etc. MCE Oxygen Sensing Compound Library is a useful tool to study hypoxia, oxidative stress and discover new anti-cancer drugs.

Oxygen Sensing Compound Library

4,097 compounds

Oxygen homeostasis regulation is the most fundamental cellular process for adjusting physiological oxygen variations, and its irregularity leads to various human diseases, including cancer. Hypoxia is closely associated with cancer development, and hypoxia/oxygen-sensing signaling plays critical roles in the modulation of cancer progression.

Hypoxia-inducible factor 1 (HIF-1) is a transcription factor that functions as a master regulator of oxygen homeostasis. A variety of HF-1 target genes have been identified thus far which encode proteins that play key roles in critical developmental and physiological processes including angiogenesis/vascular remodeling, erythropoiesis, glucose transport, glycolysis, iron transport, and cell proliferation/survival.

HIF-1 is a heterodimeric transcription factor consisting of a constitutively expressed β-subunit and an oxygen-regulated α-subunit. The unique feature of HIF-1 is the regulation of HIF-1α expression and activity based upon the cellular O₂ concentration. Under normoxic conditions, hydroxylation of HIF-1α on these different proline residues is essential for HIF proteolytic degradation by promoting interaction with the von Hippel-Lindau tumor-suppressor protein (pVHL) through hydrogen bonding to the hydroxyproline-binding pocket in the pVHL β-domain. As oxygen levels decrease, hydroxylation of HIF decreases; HIF-1α then no longer binds pVHL, and becomes stabilized, allowing more of the protein to translocate to the cell’s nucleus, where it acts as a transcription factor, upregulating (often within minutes) the production of proteins that stimulate blood perfusion in tissues and thus tissue oxygenation.

MCE offers a unique collection of 4,097 oxygen sensing related compounds targeting HIF/HIF Prolyl-Hydroxylase, MAPK/ERK, PI3K/AKT signaling pathways, etc. MCE Oxygen Sensing Compound Library is a useful tool to study hypoxia, oxidative stress and discover new anti-cancer drugs.

Cat. No.	Product Name	Type

HY-125857B

Cytochrome C (Saccharomyces cerevisiae)	Biochemical Assay Reagents
Cytochrome C (Saccharomyces cerevisiae) is a type C cytochrome located in the intermembrane space of the mitochondria. As an electron carrier, Cytochrome C (Saccharomyces cerevisiae) transfers electrons between complex III (cytochrome c reductase) and complex IV (cytochrome c oxidase, CIV) of the respiratory chain. Cytochrome C (Saccharomyces cerevisiae) can play a crucial role in triggering apoptosis by being released from the mitochondria into the cytosol .

Cytochrome C (Saccharomyces cerevisiae)

Biochemical Assay Reagents

Cytochrome C (Saccharomyces cerevisiae) is a type C cytochrome located in the intermembrane space of the mitochondria. As an electron carrier, Cytochrome C (Saccharomyces cerevisiae) transfers electrons between complex III (cytochrome c reductase) and complex IV (cytochrome c oxidase, CIV) of the respiratory chain. Cytochrome C (Saccharomyces cerevisiae) can play a crucial role in triggering apoptosis by being released from the mitochondria into the cytosol .

Cat. No.	Product Name	Target	Research Area

HY-P10426

cyclo(CLLFVY)	HIF/HIF Prolyl-Hydroxylase VEGFR	Cancer
cyclo(CLLFVY) is an inhibitor for hypoxia inducible factor-1 (HIF-1), with IC₅₀ of 19 μM (in U2OS) and 16 μM (in MCF-7). cyclo(CLLFVY) binds to the PAS-B domain of HIF-1α, inhibits HIF-1 dimerization and transcriptional activity. cyclo(CLLFVY) downregulates the expression of hypoxia response genes, such as VEGF and CAIX, exhibits antitumor against the HIF-1 associated cancers .

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BODIPY 493/503 purchased from MedChemExpress. Usage Cited in: Nat Commun. 2025 Feb 1;16(1):1241. [Abstract]

MedchemExpress Validation 01

Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature. Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature. Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.

BODIPY 493/503 purchased from MedChemExpress. Usage Cited in: Nat Commun. 2025 Feb 1;16(1):1241. [Abstract]

MedchemExpress Validation 01

MedchemExpress Validation 03

Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred

MedchemExpress Validation 04

MedchemExpress Validation

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