VHL sirna

VHL siRNA (Human)

Cat. Num. AAA8216232

• Gene Names: VHL; RCA1; VHL1; pVHL; HRCA1
• Reactivity: Human
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: VHL; VHL siRNA (Human); Von Hippel-Lindau disease tumor suppressor; Protein G7; pVHL; VHL sirna

• Host: Synthetic
• Reactivity: Human
• Specificity: VHL siRNA (Human) is a target-specific 19-23 nt siRNA oligo duplexes designed to knock down gene expression.
• Purity/Purification: > 97%
• Form/Format: Lyophilized powder
• Sequence Length: 160

• Applicable Applications for VHL sirna: RNA Interference (RNAi)
• Quality Control: Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
• Directions for Use: We recommends transfection with 100 nM siRNA 48 to 72 hours prior to cell lysis. Before resuspending, briefly centrifuge the tube to ensure the lyophilized siRNA is at the bottom of the tube. Resuspend the siRNA oligos to an appropriate concentration with DEPC water. For each vial, suitable for 250 transfections in 24 well plate (20 pmol for each well).
• Components: We offer pre-designed sets of 3 different target-specific siRNA oligo duplexes of human VHL gene. Each vial contains 5 nmol of lyophilized siRNA. The duplexes can be transfected individually or pooled together to achieve knockdown of the target gene, which is most commonly assessed by qPCR or western blot. Our siRNA oligos are also chemically modified (2'-OMe) at no extra charge for increased stability and enhanced knockdown in vitro and in vivo.
• Preparation and Storage: Shipped at 4 degree C. Store at -20 degree C for one year.

Related Product Information for VHL sirna

siRNA to inhibit VHL expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 4507891
• NCBI GeneID: 7428
• NCBI Accession #: NP_000542.1
• NCBI GenBank Nucleotide #: NM_000551.3
• UniProt Accession #: P40337; Q13599; Q6PDA9; B2RE45
• Molecular Weight: 18,532 Da
• NCBI Official Full Name: von Hippel-Lindau disease tumor suppressor isoform 1
• NCBI Official Synonym Full Names: von Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase
• NCBI Official Symbol: VHL
• NCBI Official Synonym Symbols: RCA1; VHL1; pVHL; HRCA1
• NCBI Protein Information: von Hippel-Lindau disease tumor suppressor
• UniProt Protein Name: Von Hippel-Lindau disease tumor suppressor
• Protein Family: Von Hippel-Lindau disease tumor suppressor
• UniProt Gene Name: VHL
• UniProt Entry Name: VHL_HUMAN

NCBI Description

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 this gene is the basis of familial inheritance of VHL syndrome. The protein encoded by this gene 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. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]

Uniprot Description

VHL: 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. Component of the VCB (VHL-Elongin BC-CUL2) complex; this complex acts as a ubiquitin-ligase E3 and directs proteasome- dependent degradation of targeted proteins. Interacts with CUL2; this interaction is dependent on the integrity of the trimeric VBC complex. Interacts (via the beta domain) with HIF1A (via the NTAD domain); this interaction mediates degradation of HIF1A in normoxia and, in hypoxia, prevents ubiqitination and degradation of HIF1A by mediating hypoxia-induced translocation to the nucleus, a process which requires a hypoxia-dependent regulatory signal. Interacts with ADRB2; the interaction, in normoxia, is dependent on hydroxylation of ADRB2 and the subsequent VCB- mediated ubiquitination and degradation of ADRB2. Under hypoxia, hydroxylation, interaction with VHL, ubiquitination and subsequent degradation of ADRB2 are dramatically decreased. Interacts with RNF139, USP33 and PHF17. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Isoform 1 and isoform 3 interact with LIMD1 (via LIM zinc-binding 2), AJUBA (via LIM domains) and WTIP (via LIM domains). Interacts with EPAS1. Expressed in the adult and fetal brain and kidney. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Tumor suppressor; Ubiquitin ligase

Chromosomal Location of Human Ortholog: 3p25.3

Cellular Component: nucleoplasm; intermediate filament cytoskeleton; mitochondrion; membrane; endoplasmic reticulum; nucleus; cytosol

Molecular Function: protein binding; enzyme binding; ubiquitin-protein ligase activity; transcription factor binding

Biological Process: negative regulation of cell proliferation; regulation of transcription, DNA-dependent; protein stabilization; positive regulation of transcription, DNA-dependent; cell morphogenesis; protein ubiquitination; negative regulation of transcription from RNA polymerase II promoter; proteolysis; positive regulation of cell differentiation; negative regulation of apoptosis

Disease: Erythrocytosis, Familial, 2; Von Hippel-lindau Syndrome; Renal Cell Carcinoma, Nonpapillary; Pheochromocytoma