Hypoxia Inducible Factor 1 Alpha (HIF1a) Recombinant Protein | HIF1a recombinant protein

Recombinant Hypoxia Inducible Factor 1 Alpha (HIF1a)

Cat. Num. AAA2009383

• Gene Names: Hif1a; MOP1
• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: > 95%
• Synonyms: Hypoxia Inducible Factor 1 Alpha (HIF1a); Recombinant Hypoxia Inducible Factor 1 Alpha (HIF1a); HIF1a recombinant protein

• Host: E Coli
• Purity/Purification: > 95%
• Form/Format: Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
• Sequence: The target protein is fused with N-terminal His-Tag, its sequence is listed below.; MGHHHHHHSGSEF-PPMTCLVLIC EPIPHPSNIE IPLDSKTFLS RHSLDMKFSY CDERITELMG YEPEELLGRS IYEYYHALDS DHLTKTHHDM FTKGQVTTGQ YRMLAKRGGY VWVETQATVI YNTKNSQPQC IV
• Sequence Length: 823

• Applicable Applications for HIF1a recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Organism: Rattus norvegicus (Rat)
• Expression System: Prokaryotic expression
• Residues: Pro216~Val337 (Accession # O35800) with N-terminal His-Tag
• Endotoxin Level: <1.0EU per 1ug (determined by the LAL method)
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

Sequence Information

SDS-Page

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
• Molecular Weight: 15.6kDa
• 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; HIF1 alpha; HIF1-alpha; HIF-1 alpha; HIF-1-alpha; hypoxia-inducible factor 1 alpha; hypoxia inducible factor 1, alpha subunit
• 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: DNA-binding; Autophagy; Transcription factor

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

Molecular Function: RNA polymerase II transcription factor activity, enhancer binding; histone deacetylase binding; Hsp90 protein binding; transcription factor binding; protein kinase binding; histone acetyltransferase binding; signal transducer activity; protein binding; enzyme binding; DNA binding; protein heterodimerization activity; sequence-specific DNA binding; 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; connective tissue replacement during inflammatory response; elastin metabolic process; axon transport of mitochondrion; regulation of glycolysis; response to glucose stimulus; negative regulation of neuron apoptosis; neural crest cell migration; response to X-ray; negative regulation of growth; response to drug; hemoglobin biosynthetic process; positive regulation of neuroblast proliferation; transcription, DNA-dependent; collagen metabolic process; embryonic hemopoiesis; digestive tract morphogenesis; regulation of transcription from RNA polymerase II promoter; cellular response to insulin stimulus; neural fold elevation formation; response to mechanical stimulus; response to estrogen stimulus; regulation of gene expression; blood vessel morphogenesis; positive regulation of transcription from RNA polymerase II promoter; response to activity; cerebral cortex development; negative regulation of apoptosis; transcription from RNA polymerase II promoter; response to alkaloid; lactation; 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 salt stress; response to estradiol stimulus; vasculature development; regulation of transcription, DNA-dependent; regulation of catalytic activity; positive regulation of cell proliferation; visual learning; angiogenesis; heart looping; cell differentiation; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; blood vessel development; negative regulation of TOR signaling pathway; regulation of transforming growth factor-beta2 production; 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 cobalt ion; response to hypoxia; epithelial to mesenchymal transition