|Other Names||Von Hippel-Lindau disease tumor suppressor, Protein G7, pVHL, VHL|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6549a was selected from the N-term region of human VHL. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia- inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2.|
|Cellular Location||Isoform 1: Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note=Found predominantly in the cytoplasm and with less amounts nuclear or membrane-associated Colocalizes with ADRB2 at the cell membrane|
|Tissue Location||Expressed in the adult and fetal brain and kidney|
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Von Hippel-Lindau syndrome (VHL) is a dominantly inherited familial cancer syndrome predisposing to a variety of malignant and benign tumors. A germline mutation of VHL gene is the basis of familial inheritance of VHL syndrome. The protein is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. This protein is involved in the ubiquitination and degradation of hypoxia-inducible-factor (HIF), which is a transcription factor that plays a central role in the regulation of gene expression by oxygen. RNA polymerase II subunit POLR2G/RPB7 is also reported to be a target of this protein.
Olmos,G., Cell. Mol. Life Sci. 66 (13), 2167-2180 (2009)Hatzimichael,E., Clin Lymphoma Myeloma 9 (3), 239-242 (2009)Luu,V.D., Clin. Cancer Res. 15 (10), 3297-3304 (2009)
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