HIF1A sirna

HIF1A siRNA (Rat)

Cat. Num. AAA8226858

• Gene Names: Hif1a; MOP1
• Reactivity: Rat
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: HIF1A; HIF1A siRNA (Rat); Hypoxia-inducible factor 1-alpha; HIF-1-alpha; HIF1-alpha; HIF1A sirna

• Host: Synthetic
• Reactivity: Rat
• Specificity: HIF1A siRNA (Rat) 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: 825

• Applicable Applications for HIF1A 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 rat HIF1A 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°C. Store at -20°C for one year.

Related Product Information for HIF1A sirna

siRNA to inhibit HIF1A expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 13242249
• NCBI GeneID: 29560
• NCBI Accession #: NP_077335.1
• NCBI GenBank Nucleotide #: NM_024359.1
• UniProt Accession #: O35800; Q9WTU9
• NCBI Official Full Name: hypoxia-inducible factor 1-alpha
• NCBI Official Synonym Full Names: hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
• NCBI Official Symbol: Hif1a
• NCBI Official Synonym Symbols: MOP1
• NCBI Protein Information: hypoxia-inducible factor 1-alpha
• UniProt Protein Name: Hypoxia-inducible factor 1-alpha
• Protein Family: Hypoxia-inducible factor
• UniProt Gene Name: Hif1a
• UniProt Synonym Gene Names: HIF-1-alpha; HIF1-alpha
• UniProt Entry Name: HIF1A_RAT

NCBI Description

regulates transcription in response to low oxygen; may play a role in vascular biology [RGD, Feb 2006]

Uniprot Description

HIF1A: a master transcriptional regulator of the adaptive response to hypoxia. 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. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia. Interacts with the HIF1A beta/ARNT subunit; heterodimerization is required for DNA binding. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability. Interacts with EP300 (via TAZ-type 1 domains); the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts with CREBBP (via TAZ-type 1 domains). Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation. During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A. Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription. Interacts (Via the ODD domain) with ARD1A; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia. Interacts with RWDD3; the interaction enhances HIF1A sumoylation. Interacts with TSGA10. Interacts with RORA (via the DNA binding domain); the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interaction with PSMA7 inhibits the transactivation activity of HIF1A under both normoxic and hypoxia- mimicking conditions. Interacts with USP20. Interacts with RACK1; promotes HIF1A ubiquitination and proteasome- mediated degradation. Interacts (via N-terminus) with USP19. Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF, FGF2, IGF2, TGFB1, HGF, TNF, IL1B, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia. Repressed by HIPK2 and LIMD1. Expressed in most tissues with highest levels in kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Transcription factor; DNA-binding; Autophagy

Cellular Component: transcription factor complex; cell; cytoplasm; nucleolus; nuclear speck; cytosol; nucleus

Molecular Function: RNA polymerase II transcription factor activity, enhancer binding; histone deacetylase binding; Hsp90 protein binding; protein kinase binding; transcription factor binding; histone acetyltransferase binding; protein binding; signal transducer activity; enzyme binding; DNA binding; sequence-specific DNA binding; protein heterodimerization activity; ubiquitin protein ligase binding; double-stranded DNA binding; protein complex binding; transcription factor activity; nuclear hormone receptor binding

Biological Process: response to purine; maternal process involved in pregnancy; positive regulation of apoptosis; cellular iron ion homeostasis; positive regulation of transcription, DNA-dependent; response to glucocorticoid stimulus; glucose homeostasis; muscle maintenance; negative regulation of bone mineralization; elastin metabolic process; connective tissue replacement during inflammatory response; axon transport of mitochondrion; regulation of glycolysis; response to glucose stimulus; negative regulation of neuron apoptosis; neural crest cell migration; negative regulation of growth; response to X-ray; response to drug; hemoglobin biosynthetic process; positive regulation of neuroblast proliferation; collagen metabolic process; transcription, DNA-dependent; embryonic hemopoiesis; digestive tract morphogenesis; regulation of transcription from RNA polymerase II promoter; cellular response to insulin stimulus; neural fold elevation formation; response to estrogen stimulus; regulation of gene expression; response to mechanical stimulus; blood vessel morphogenesis; positive regulation of transcription from RNA polymerase II promoter; response to activity; cerebral cortex development; negative regulation of apoptosis; lactation; response to alkaloid; transcription from RNA polymerase II promoter; oxygen homeostasis; response to muscle activity; embryonic placenta development; positive regulation of cell size; positive regulation of smooth muscle cell proliferation; signal transduction; positive regulation of vascular endothelial growth factor receptor signaling pathway; response to estradiol stimulus; response to salt stress; vasculature development; regulation of transcription, DNA-dependent; regulation of catalytic activity; positive regulation of cell proliferation; visual learning; heart looping; angiogenesis; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; cell differentiation; blood vessel development; regulation of transforming growth factor-beta2 production; negative regulation of TOR signaling pathway; positive regulation of erythrocyte differentiation; B-1 B cell homeostasis; negative regulation of vasoconstriction; regulation of cell proliferation; positive regulation of hormone biosynthetic process; cartilage development; lactate metabolic process; response to hypoxia; response to cobalt ion; epithelial to mesenchymal transition