Recombinant Human Hypoxia-Inducible Factor 1-Alpha (HIF1A) Protein (His)

Name: Recombinant Human Hypoxia-Inducible Factor 1-Alpha (HIF1A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03562P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Hypoxia-Inducible Factor 1-Alpha (HIF1A) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q16665
Target Symbol	HIF1A
Synonyms	ARNT interacting protein; ARNT-interacting protein; Basic helix loop helix PAS protein MOP1; Basic-helix-loop-helix-PAS protein MOP1; bHLHe78; Class E basic helix-loop-helix protein 78; HIF 1A; HIF 1alpha; HIF-1-alpha; HIF-1alpha; HIF-alpha; HIF1 A; HIF1 Alpha; HIF1; HIF1-alpha; HIF1A; HIF1A_HUMAN; hifla; Hypoxia inducible factor 1 alpha; Hypoxia inducible factor 1 alpha isoform I.3 ; Hypoxia inducible factor 1 alpha subunit; Hypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor; Hypoxia inducible factor 1; alpha subunit (basic helix loop helix transcription factor); Hypoxia inducible factor1alpha; Hypoxia-inducible factor 1-alpha; Member of PAS protein 1; Member of PAS superfamily 1; Member of the PAS Superfamily 1; MOP 1; MOP1; PAS domain-containing protein 8; PASD 8; PASD8
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	QLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
Expression Range	579-826aa
Protein Length	Partial
Mol. Weight	31.0kDa
Research Area	Transcription
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Functions as 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. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with NCOA1 and/or NCOA2. Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.; (Microbial infection) Upon infection by human coronavirus SARS-CoV-2, is required for induction of glycolysis in monocytes and the consequent proinflammatory state. In monocytes, induces expression of ACE2 and cytokines such as IL1B, TNF, IL6, and interferons. Promotes human coronavirus SARS-CoV-2 replication and monocyte inflammatory response.
Subcellular Location	Cytoplasm. Nucleus. Nucleus speckle.
Database References	HGNC: 4910 OMIM: 603348 KEGG: hsa:3091 STRING: 9606.ENSP00000338018 UniGene: PMID: 30226584 Since the FIH-1 dependent hydroxylation of NAA10 occurs oxygen-dependently, NAA10 acetylates HIF-1alpha under normoxia but does not under hypoxia. PMID: 30237125 HIF1A is upregulated in breast and bladder tumors with high NRF2 activity. NRF2 targets a functional antioxidant response element at the HIF1A locus, which reveals a direct regulatory connection between two important oxygen responsive transcription factors. PMID: 30241031 CPT1A is repressed by HIF1 and HIF2, reducing fatty acid transport into the mitochondria, and forcing fatty acids to lipid droplets for storage. PMID: 29176561 MiR-497 approximately 195 cluster regulates angiogenesis during coupling with osteogenesis by maintaining endothelial Notch1 and HIF1A activity. PMID: 28685750 Study revealed that HIF1alpha was significantly upregulated in gallbladder cancer (GBC) tissues. HIF1alpha overexpression was closely associated with lymph node metastasis and TNM stage. HIF1alpha was able to promote cell migration in a hypoxic microenvironment by overexpressing VEGF in GBC cell line. PMID: 30272364 HIF-1alpha "positive" had decreased overall survival compared to HIF-1alpha "negative" patients and this was an independent adverse prognostic factor for HCC patients with cirrhosis, but not for cirrhosis-free patients. PMID: 30274686 genetic polymorphisms in HIF1A were not associated with persistent apical periodontitis PMID: 29898065 Hypoxia-induced angiogenesis is a complex process that involves distinct but also overlapping functions of HIF-1alpha and HIF- 2alpha in regard to angiogenesis, bioenergetic adaption and the redundant transcriptional induction of MIF. PMID: 28993199 High HIF1A expression is associated with high Collagen I Fibers in Triple Negative Breast Cancer. PMID: 29247885 Cathepsin B (CTSB) is a novel target gene of hypoxia-inducible factor-1-alpha (HIF-1alpha). CTSB mRNA and protein levels can be up-regulated in a HIF-1alpha-dependent manner. PMID: 29935187 this is the first case-control study uncovering that the HIF1A gene rs10873142 polymorphism increases the risk of COPD in a Chinese Han population. PMID: 29339421 ST6Gal-I activity augmented HIF-1alpha accumulation in cells grown in a hypoxic environment or treated with two chemical hypoxia mimetics, deferoxamine and dimethyloxalylglycine. PMID: 29475939 mRNA expression levels of both HIF1A and LACC1 were upregulated in the skin lesions of individuals with leprosy. PMID: 29706348 data suggest an important role of miR-210 in sustaining HIF-1alpha activity via the suppression of HIF-3alpha, regulating cell growth and chemotherapeutic drug resistance in cholangiocarcinoma. PMID: 29953500 HOXA9 inhibits HIF1A-mediated glycolysis through interacting with CRIP2 to repress cutaneous squamous cell carcinoma development. PMID: 29662084 HIF-1alpha inhibits NCR1/NKp46 pathway through up-regulating miR-224, which affects the killing capability of NK cells on prostate cancer, thus inducing immune escape of tumor cells. PMID: 29885835 The findings demonstrate that AGPAT2, which is mutated in patients with congenital generalized lipodystrophy and over-expressed in different types of cancer, is a direct transcriptional target of HIF-1, suggesting that upregulation of lipid storage by HIF-1 plays an important role in adaptation and survival of cancer cells under low oxygen conditions. PMID: 29908837 Overexpression of HIF1A leads to radioresistance of cervical cancer. PMID: 30355300 Knockdown of DEC2 resulted in a significant (26.7%) reduction of VEGF expression in MIO-M1 cells under hypoxia-mimicking conditions induced by DFO (P < .05). Levels of HIF1alpha protein were also reduced significantly, by 60.2%, in MIO-M1 cells treated with siRNA against the DEC2 gene (P < .05). Moreover, HIF1alpha levels showed a significant (2.5-fold) increase in MIO-M1 cells overexpressing DEC2 (P < .05). PMID: 30250985 High HIF1A expression is associated with salivary adenoid cystic carcinoma. PMID: 30015895 we found that Hif-1alpha directly promoted H19 expression through binding to the H19 promoter and indirectly through SP1-mediated H19 transcriptional activation under hypoxia in glioblastoma cells. PMID: 28327666 The IRIS-driven metastatic mechanism results from IRIS-dependent suppression of phosphatase and tensin homolog (PTEN) transcription, which in turn perturbs the PI3K/AKT/GSK-3beta pathway leading to prolyl hydroxylase-independent HIF-1alpha stabilization and activation in a normoxic environment. PMID: 30254159 Data show that von Hippel-Lindau-binding protein 1 (VBP1) enhances the stability of von Hippel-Lindau tumor suppressor protein (pVHL) and facilitates pVHL-mediated ubiquitination of hypoxia-inducible factor 1, alpha subunit (HIF-1alpha). PMID: 29121446 Multifunctional proteins epigenetically modulating HIF1A stability and activity have been described. (Review) PMID: 29032501 Studies have shown that both HIF1alpha and HIF2alpha may contribute to the regulation of cellular adaptation to hypoxia and resistance to cancer therapies with their potential to exert significant effects on the maintenance and evolution of cancer stem cells. Also, HIF1alpha and HIF2alpha seemed to have significant prognostic and predictive value. [review] PMID: 29845228 HIF-1 was overexpressed in osteosarcoma tissues and cell lines, which promoted cell proliferation, clone formation, migration, invasion and inhibited cell apoptosis. PMID: 29807229 hypoxiainduced expression of CXCR4 promoted trophoblast cell migration and invasion via the activation of HIF1alpha, which is crucial during placentation. PMID: 29786753 Data suggest that NRF2/NFE2L2 promotes breast cancer progression by enhancing glycolysis through co-activation of HIF1A; NRF2 and HIF1A mRNA and protein levels are significantly up-regulated in breast cancer cells as compared to benign breast epithelial cells. (NRF2/NFE2L2 = nuclear factor erythroid 2-related factor 2; HIF1A = hypoxia inducible factor 1 subunit alpha) PMID: 29275212 the expression of MMIF, HIF-1alpha, and VEGF in the serum and endometrial tissues may be used to assess the stage of endometriosis and the severity of dysmenorrhea. PMID: 30074218 Findings revealed an HIF-1alpha/IL-1beta signaling loop between cancer cells and tumor-associated macrophages in a hypoxic microenvironment, resulting in cancer cell epithelial-mesenchymal transition and metastasis; more importantly, our results suggest a potential role of an anti-inflammatory strategy in hepatocellular carcinoma treatment PMID: 29171040 Overexpression of HIF-1alpha and P4HB is associated with poor prognosis in patients with gastric cancer. PMID: 29904245 hypoxic stress in the hepatocellular carcinoma (HCC)cells promoted YAP binding to HIF-1a in the nucleus and sustained HIF-1a protein stability to bind to PKM2 gene and directly activates PKM2 transcription to accelerate glycolysis PMID: 30180863 Overexpression of VHL was more successful at inhibiting fibrosis compared with silencing HIF-1a plus HIF-2a. Normoxia-active HIF-1a or HIF-2a prevented the inhibitory effect of VHL on liver fibrosis, indicating that attenuating fibrosis via VHL is HIF-1a- and HIF-2a-dependent to some extent. PMID: 28112200 Results find that knockdown of HIF-1alpha reduced hypoxia-induced SENP1 expression, suggesting that induction of SENP1 expression is mediated by hypoxia-inducible factor HIF-1alpha. PMID: 28796315 ADM was an upstream molecule of HIF-1alpha/VEGF and it promoted angiogenesis through upregulating HIF-1alpha/VEGF in epithelial ovarian cancer. PMID: 28091613 HIF-1alpha expression correlates with the expression level of IL- 8, as evidenced by the down regulation of IL-8 in response to silencing of HIF-1alpha in HCC cell lines under hypoxic conditions. PMID: 29881400 MOLP8/R cells display a very high overexpression of LCP1 gene (l-Plastin) controlled by HIF1&alpha. PMID: 29882856 the role of FTH1 in the FIH control of HIF-1 activity, is reported. PMID: 29580991 The findings of the current study demonstrate presence of the IDH1 R132H mutation in primary human glioblastoma cell lines with upregulated HIF-1alpha expression, downregulating c-MYC activity and resulting in a consequential decrease in miR-20a, which is responsible for cell proliferation and resistance to standard temozolomide treatment. PMID: 29625108 The cross-talk between HIF1A, NRF2 and NF-kappaB is required to adapt to changes in oxygen availability. (Review) PMID: 29485192 PKD1 not only regulates the hypoxic glycolytic metabolism of cancer cells via regulation of the expression of HIF-1alpha and glycolytic enzymes. PMID: 29901206 Results provide evidence that HIF1alpha overexpression promotes the radioresistance of prostate cancer cells through enhanced betacatenin nuclear translocation. PMID: 29658569 Collectively, the present study demonstrated mitochondrial fission as a tumor suppression process that is regulated by the HIF/miR125a/Mfn2 pathways, acting to restrict PANC1 cell survival, energy metabolism and migration, with potential implications for novel approaches for PC therapy. PMID: 29749475 the results of the present study demonstrated that hypoxia-induced cytoprotective autophagy counteracted gemcitabine-induced apoptosis through increasing HIF1alpha expression PMID: 29693166 CD40 is a key molecule for the upregulation of HIF-1alpha and PTEN underlying the severity of microangiopathy. PMID: 29549140 Enhanced expression of HIF-1alpha may be related to autophagy activation in SH-SY5Y cells, thus contributing to ischemic/hypoxic brain damage. PMID: 29724989 Data show that deletion of hypoxia inducible factor 1 subunit alpha (HIF-1alpha) in NK cells inhibited tumour growth despite impaired tumour cell killing. PMID: 29150606 AEG-1 was found to be significantly associated with hypoxia in ovarian cancer by regulating the HIF-1alpha/NF-kappaB/VEGF pathway. PMID: 29770329 no significant differences in the serum levels between early-onset pre-eclampsia, late-onset pre-eclampsia, and controls PMID: 28574293

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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