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Mouse Anti-EGLN3 Monoclonal Antibody (3C5) (CBMAB-1124-YC)

Provided herein is a mouse monoclonal antibody against Human EGLN3. The antibody, clone 3C5, can be used for immunoassay techniques, such as ELISA.
See all EGLN3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
3C5
Antibody Isotype
IgG2a, κ
Application
ELISA

Basic Information

Immunogen
Partial recombinant protein EGLN3 (AAH10992.2, aa 94-193) with GST tag
Specificity
Human
Antibody Isotype
IgG2a, κ
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
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
Located in aa 94-193, partial

Target

Full Name
egl nine homolog 3 (C. elegans)
Introduction
EGLN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. EGLN3 also hydroxylates PKM in hypoxia, limiting glycolysis, and regulates the stability of ADRB2 under normoxia. In cardiomyocytes, EGLN3 inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, EGLN3 has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity.
Entrez Gene ID
112399
UniProt ID
Q9H6Z9
Alternative Names
PHD3; HIFPH3; HIFP4H3
Research Area
Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A (PubMed:19584355, PubMed:21620138, PubMed:21483450, PubMed:22797300, PubMed:20978507, PubMed:21575608).

Target proteins are preferentially recognized via a LXXLAP motif. Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins (PubMed:11595184, PubMed:12181324).

Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A (PubMed:11595184, PubMed:12181324).

Also hydroxylates HIF2A (PubMed:11595184, PubMed:12181324).

Has a preference for the CODD site for both HIF1A and HIF2A (PubMed:11595184, PubMed:12181324).

Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (PubMed:11595184, PubMed:12181324).

Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (PubMed:11595184, PubMed:12181324).

Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes (PubMed:11595184, PubMed:12181324).

ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis (PubMed:21620138, PubMed:21483450).

Under normoxia, hydroxylates and regulates the stability of ADRB2 (PubMed:19584355).

Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex (PubMed:20849813).

In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity (PubMed:16098468).

Also essential for hypoxic regulation of neutrophilic inflammation (PubMed:21317538).

Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (PubMed:22797300).

Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (Probable).
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Apoptotic process Source: UniProtKB
Cellular response to DNA damage stimulus Source: UniProtKB-KW
Cellular response to hypoxia Source: GO_Central
Peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase
Protein hydroxylation Source: UniProtKB
Regulation of cell population proliferation Source: UniProtKB
Regulation of neuron apoptotic process Source: UniProtKB
Response to hypoxia Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm. Colocalizes with WDR83 in the cytoplasm.
PTM
Ubiquitinated by SIAH1 and/or SIAH2 in response to the unfolded protein response (UPR), leading to its degradation.

Jin, Y., Pan, Y., Zheng, S., Liu, Y., Xu, J., Peng, Y., ... & Fu, J. (2022). Inactivation of EGLN3 hydroxylase facilitates Erk3 degradation via autophagy and impedes lung cancer growth. Oncogene, 41(12), 1752-1766.

Chen, W., Song, J., Liu, S., Tang, B., Shen, L., Zhu, J., ... & Ji, J. (2021). USP9X promotes apoptosis in cholangiocarcinoma by modulation expression of KIF1Bβ via deubiquitinating EGLN3. Journal of biomedical science, 28(1), 1-15.

Zhang, G., Wang, J., Tan, W., Han, X., Han, B., Wang, H., ... & Li, H. (2021). Circular RNA EGLN3 silencing represses renal cell carcinoma progression through the miR-1224-3p/HMGXB3 axis. Acta Histochemica, 123(6), 151752.

Hu, G., Xia, Y., Chen, B., Zhang, J., Gong, L., Chen, Y., ... & Deng, Z. (2021). ESC-sEVs rejuvenate aging hippocampal NSCs by transferring SMADs to regulate the MYT1-Egln3-Sirt1 axis. Molecular Therapy, 29(1), 103-120.

Yue, Y., Cui, J., Zhao, Y., Liu, S., & Niu, W. (2020). Circ_101341 deteriorates the progression of clear cell renal cell carcinoma through the miR-411/EGLN3 axis. Cancer Management and Research, 12, 13513.

Lin, L., & Cai, J. (2020). Circular RNA circ‐EGLN3 promotes renal cell carcinoma proliferation and aggressiveness via miR‐1299‐mediated IRF7 activation. Journal of Cellular Biochemistry, 121(11), 4377-4385.

Wang, Y., Li, X., Liu, W., Li, B., Chen, D., Hu, F., ... & Liu, R. (2019). MicroRNA-1205, encoded on chromosome 8q24, targets EGLN3 to induce cell growth and contributes to risk of castration-resistant prostate cancer. Oncogene, 38(24), 4820-4834.

Li, S., Rodriguez, J., Li, W., Bullova, P., Fell, S. M., Surova, O., ... & Schlisio, S. (2019). EglN3 hydroxylase stabilizes BIM-EL linking VHL type 2C mutations to pheochromocytoma pathogenesis and chemotherapy resistance. Proceedings of the National Academy of Sciences, 116(34), 16997-17006.

Zhong, C., Li, S., Li, J., Li, F., Ran, M., Qiu, L., ... & Zhao, X. (2018). Polymorphisms in the Egl nine homolog 3 (EGLN3) and peroxisome proliferator activated receptor-alpha (PPARα) genes and their correlation with hypoxia adaptation in Tibetan chickens. PLoS One, 13(3), e0194156.

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

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