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Mouse Anti-HIF3A (AA 355-669) Recombinant Antibody (CBFYH-1104) (CBMAB-H2055-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-1104
Antibody Isotype
IgG1
Application
WB, IHC

Basic Information

Immunogen
Human recombinant protein fragment corresponding to amino acids 355-669 of human HIF3A produced in E.coli
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, PH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% Sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 355-669

Target

Full Name
HIF3A
Introduction
The protein encoded by this gene is the alpha-3 subunit of one of several alpha/beta-subunit heterodimeric transcription factors that regulate many adaptive responses to low oxygen tension (hypoxia). The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. Multiple alternatively spliced transcript variants have been found for this gene.
Entrez Gene ID
64344
UniProt ID
Q9Y2N7
Alternative Names
Hypoxia Inducible Factor 3 Alpha Subunit; Class E Basic Helix-Loop-Helix Protein 17; Basic-Helix-Loop-Helix-PAS Protein MOP7; PAS Domain-Containing Protein 7; Inhibitory PAS Domain Protein; Member Of PAS Protein 7; HIF3-Alpha-1; BHLHe17
Function
Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression (PubMed:11573933, PubMed:16126907, PubMed:19694616, PubMed:20416395, PubMed:21069422).

Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis (By similarity).

Isoform 2:
Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. Also inhibits hypoxia-inducible ARNT-mediated gene expression.

Isoform 3:
Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.

Isoform 4:
Attenuates the ability of transcription factor HIF1A and EPAS1/HIF2A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation (PubMed:16126907, PubMed:17998805, PubMed:19694616, PubMed:20416395).

May act as a tumor suppressor and inhibits malignant cell transformation (PubMed:17998805).

Isoform 5:
Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.
Biological Process
Angiogenesis Source: UniProtKB-KW
Apoptotic process Source: UniProtKB-KW
Regulation of transcription by RNA polymerase II Source: UniProtKB
Response to hypoxia Source: Ensembl
Transcription by RNA polymerase II Source: Ensembl
Cellular Location
Nucleus; Nucleus speckle; Cytoplasm; Mitochondrion. In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Colocalizes with BAD in the cytoplasm. Colocalizes with EPAS1 and HIF1A in the nucleus and speckles (By similarity). Localized in the cytoplasm and nuclei under normoxia, but increased in the nucleus under hypoxic conditions (PubMed:19694616). Colocalized with HIF1A in kidney tumors (PubMed:19694616).
PTM
In normoxia, hydroxylated on Pro-492 in the oxygen-dependent degradation domain (ODD) by prolyl hydroxylase(s) (PHD). The hydroxylated proline promotes interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation.
Ubiquitinated; ubiquitination occurs in a VHL- and oxygen-dependent pathway and subsequently targeted for proteasomal degradation.
More Infomation

Xu, Y., Hu, T., Ding, H., Yuan, Y., & Chen, R. (2023). miR-485-5p alleviates obstructive sleep apnea syndrome with hypertension by inhibiting PI3K/AKT signaling pathway via downregulating HIF3A expression. Sleep and Breathing, 27(1), 109-119.

Gu, W., Wang, L., Deng, G., Gu, X., Tang, Z., Li, S., ... & Li, Q. (2022). Knockdown of long noncoding RNA MIAT attenuates cigarette smoke-induced airway remodeling by downregulating miR-29c-3p–HIF3A axis. Toxicology Letters, 357, 11-19.

Mikec, Š., Šimon, M., Morton, N. M., Atanur, S. S., Konc, J., Dovč, P., ... & Kunej, T. (2022). Genetic variants of the hypoxia‐inducible factor 3 alpha subunit (Hif3a) gene in the Fat and Lean mouse selection lines. Molecular Biology Reports, 49(6), 4619-4631.

Chen, Q., Cao, M., & Ge, H. (2021). Knockdown of MALAT1 inhibits the progression of chronic periodontitis via targeting miR-769-5p/HIF3A axis. BioMed Research International, 2021.

Lu, Y., Yang, C., Zhang, L., & Ding, J. (2021). Ropivacaine retards the viability, migration, and invasion of choriocarcinoma cells by regulating the long noncoding RNA OGFRP1/microRNA-4731-5p/HIF3A axis. Molecular Biotechnology, 1-11.

Sun, D. G., Tian, S., Zhang, L., Hu, Y., Guan, C. Y., Ma, X., & Xia, H. F. (2020). The miRNA-29b is downregulated in placenta during gestational diabetes mellitus and may alter placenta development by regulating trophoblast migration and invasion through a HIF3A-dependent mechanism. Frontiers in endocrinology, 11, 169.

Shen, J., Song, R., Ye, Y., Wu, X., Chow, W. H., & Zhao, H. (2020). HIF3A DNA methylation, obesity and weight gain, and breast cancer risk among Mexican American women. Obesity Research & Clinical Practice, 14(6), 548-553.

Bjerre, M. T., Strand, S. H., Nørgaard, M., Kristensen, H., Rasmussen, A. K., Mortensen, M. M., ... & Sørensen, K. D. (2019). Aberrant DOCK2, GRASP, HIF3A and PKFP hypermethylation has potential as a prognostic biomarker for prostate cancer. International journal of molecular sciences, 20(5), 1173.

Zhang, Y., Chen, Y., Qu, H., & Wang, Y. (2019). Methylation of HIF3A promoter CpG islands contributes to insulin resistance in gestational diabetes mellitus. Molecular genetics & genomic medicine, 7(4), e00583.

Mansell, T., Ponsonby, A. L., Januar, V., Novakovic, B., Collier, F., Burgner, D., ... & Barwon Infant Study Investigator Team Peter Vuillermin Anne-Louise Ponsonby John Carlin Katie Allen Mimi Tang Richard Saffery Sarath Ranganathan David Burgner Terry Dwyer Kim Jachno Peter Sly. (2019). Early-life determinants of hypoxia-inducible factor 3A gene (HIF3A) methylation: a birth cohort study. Clinical Epigenetics, 11, 1-12.

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For research use only. Not intended for any clinical use.

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