9 Results for "

pVHL

" in MedChemExpress (MCE) Product Catalog:
Products (9)

9 Results for "pVHL" in MCE Product Catalog:

1
1 Cited Publications
Cat. No.: HY-111593
CAS No.: 2244684-49-7
Purity:  99.40%
Target:  

PROTACs

Research Areas:  

Cancer

Homo-PROTAC pVHL30 degrader 1 is a Homo-PROTAC autodegraders targeting the von Hippel-Lindau E3 ubiquitin ligase (VHL), with Kd values of 11 nM and 25 nM for pVHL19-EloBC​ and pVHL30-EloBC​, respectively. Homo-PROTAC pVHL30 degrader 1 induces Cullin2 depletion, promotes VHL dimerization to form a ternary complex, and drives proteasome-dependent and CRL2-VHL-like ubiquitination-dependent autodegradation. Homo-PROTAC pVHL30 degrader 1 does not trigger hypoxic responses, and only causes extremely mild stabilization of hypoxia-inducible factor α subunits. Homo-PROTAC pVHL30 degrader 1 can be used in studies related to cervical cancer and osteosarcoma .
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1
1 Cited Publications
Cat. No.: HY-P86001
Synonyms: von Hippel-Lindau disease tumor suppressor, Protein G7, pVHL, VHL

Host:  

Mouse

Application:  

IHC-P, ICC/IF, ELISA

Reactivity:  

Human

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Cat. No.: HY-136257
CAS No.: 2244684-50-0
Purity:  99.72%
Target:  

PROTACs

Research Areas:  

Others

CMP98 is a homologous PROTAC that serves as a negative control compound for CM11, a pVHL30 PROTAC degrader. CMP98 does not induce VHL protein degradation, bind to the VCB complex, or form a ternary VCB complex .
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Cat. No.: HY-RS16509
Research Areas:  

Others

Vhl Mouse Pre-designed siRNA Set A contains three designed siRNAs for Vhl gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control.

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Cat. No.: HY-RS15648
Research Areas:  

Others

VHL Human Pre-designed siRNA Set A contains three designed siRNAs for VHL gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.

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Cat. No.: HY-P76124
Purity:  ≥ 90%, as determined by reducing SDS-PAGE.
Synonyms: VHL; Von Hippel-Lindau Tumor Suppressor; Von Hippel-Lindau Disease Tumor Suppressor; VHL1; pVHL; Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase; Protein G7; Von Hippel-Lindau Tumor Suppressor, Isoform CRA_d; Von Hippel-Lindau Tumor Suppre
Species:  
Human
Source:  
E. coli
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Cat. No.: HY-117844
CAS No.: 1631137-31-9
Target:  

Ligands for E3 Ligase

Research Areas:  

Others

VHL Ligand 35 (Compound 14) is a von Hippel-Lindau protein (pVHL) E3 ubiquitin ligase ligand with a Kd of 0.291 μM. VHL Ligand 35 disrupts protein-protein interaction between pVHL and hypoxia inducible factor 1α (HIF-1α) .
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Cat. No.: HY-P80517
Synonyms: von Hippel-Lindau disease tumor suppressor, Protein G7, pVHL, VHL

Host:  

Mouse

Application:  

IHC-P

Reactivity:  

Human, Mouse, Rat

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Cat. No.: HY-L045
4,368 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 4,368 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.