Mouse Anti-HERC2 (AA 1781-1974) Recombinant Antibody (17/HERC2) (CBMAB-H1865-FY)

Name: Mouse Anti-HERC2 (AA 1781-1974) Recombinant Antibody (17/HERC2)
SKU: CBMAB-H1865-FY
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

17/HERC2

Application

Immunogen

Mouse HERC2 aa. 1781-1974

Specificity

Mouse, Human, Rat

Antibody Isotype

IgG1

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

Concentration

0.25 mg/mL

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 1781-1974

More Infomation

Target

Full Name

HECT And RLD Domain Containing E3 Ubiquitin Protein Ligase 2

Introduction

This gene belongs to the HERC gene family that encodes a group of unusually large proteins, which contain multiple structural domains. All members have at least 1 copy of an N-terminal region showing homology to the cell cycle regulator RCC1 and a C-terminal HECT (homologous to E6-AP C terminus) domain found in a number of E3 ubiquitin protein ligases. Genetic variations in this gene are associated with skin/hair/eye pigmentation variability. Multiple pseudogenes of this gene are located on chromosomes 15 and 16.

Entrez Gene ID

Human	8924
Mouse	15204
Rat	308669

UniProt ID

Human	O95714
Mouse	Q4U2R1
Rat	D4ACN3

Alternative Names

HECT And RLD Domain Containing E3 Ubiquitin Protein Ligase 2; HECT-Type E3 Ubiquitin Transferase HERC2; Hect Domain And RLD 2; Hect Domain And RCC1-Like Domain-Containing Protein 2; HECT Domain And RCC1-Like Domain-Containing Protein 2; Probable E3 Ubiquitin-Protein Ligase HERC2; E3 Ubiquitin-Protein Ligase HERC2; EC 2.3.2.26

Function

E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333).

Biological Process

Cellular response to DNA damage stimulus Source: UniProtKB
DNA repair Source: UniProtKB-KW
Intracellular protein transport Source: UniProtKB
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
Protein ubiquitination Source: UniProtKB
Spermatogenesis Source: Ensembl

Cellular Location

Centriole; Nucleus; Cytoplasm. Recruited to sites of DNA damage in response to ionizing radiation (IR) via its interaction with RNF8. May loose association with centrosomes during mitosis.

Involvement in disease

Mental retardation, autosomal recessive 38 (MRT38):
A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT38 is characterized by global developmental delay affecting motor, speech, adaptive, and social development. Patients manifest autistic features, aggression, self-injury, impulsivity, and distractibility.

PTM

Phosphorylation at Thr-4827 is required for interaction with RNF8.
Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs), promoting the interaction with RNF8.

Anandhan, A., Dodson, M., Shakya, A., Chen, J., Liu, P., Wei, Y., ... & Zhang, D. D. (2023). NRF2 controls iron homeostasis and ferroptosis through HERC2 and VAMP8. Science Advances, 9(5), eade9585.

Liu, Y., Xu, Q., Deng, F., Zheng, Z., Luo, J., Wang, P., ... & Zuo, D. (2023). HERC2 promotes inflammation-driven cancer stemness and immune evasion in hepatocellular carcinoma by activating STAT3 pathway. Journal of Experimental & Clinical Cancer Research, 42(1), 1-20.

Tencer, A. H., Liu, J., Zhu, J., Burkholder, N. T., Zhang, Y., Wu, W., ... & Kutateladze, T. G. (2022). The ZZ domain of HERC2 is a receptor of arginylated substrates. Scientific Reports, 12(1), 6063.

Salvo, N. M., Mathisen, M. G., Janssen, K., Berg, T., & Olsen, G. H. (2022). Experimental long-distance haplotyping of OCA2-HERC2 variants. Forensic Science International: Genetics Supplement Series, 8, 188-190.

Mathieu, N. A., Levin, R. H., & Spratt, D. E. (2021). Exploring the roles of HERC2 and the NEDD4L HECT E3 ubiquitin ligase subfamily in p53 signaling and the DNA damage response. Frontiers in Oncology, 11, 659049.

García‐Cano, J., Sánchez‐Tena, S., Sala‐Gaston, J., Figueras, A., Viñals, F., Bartrons, R., ... & Rosa, J. L. (2020). Regulation of the MDM2‐p53 pathway by the ubiquitin ligase HERC2. Molecular Oncology, 14(1), 69-86.

Lai, Y., Zhu, M., Wu, W., Rokutanda, N., Togashi, Y., Liang, W., & Ohta, T. (2019). HERC2 regulates RPA2 by mediating ATR-induced Ser33 phosphorylation and ubiquitin-dependent degradation. Scientific reports, 9(1), 14257.

Abraham, J. R., Barnard, J., Wang, H., Noritz, G. H., Yeganeh, M., Buhas, D., & Natowicz, M. R. (2019). Proteomic investigations of human HERC2 mutants: Insights into the pathobiology of a neurodevelopmental disorder. Biochemical and biophysical research communications, 512(2), 421-427.

Wu, W., Rokutanda, N., Takeuchi, J., Lai, Y., Maruyama, R., Togashi, Y., ... & Ohta, T. (2018). HERC2 facilitates BLM and WRN helicase complex interaction with RPA to suppress G-quadruplex DNA. Cancer Research, 78(22), 6371-6385.

Wang, L. Q., Zheng, Y. Y., Zhou, H. J., Zhang, X. X., Wu, P., & Zhu, S. M. (2021). LncRNA-Fendrr protects against the ubiquitination and degradation of NLRC4 protein through HERC2 to regulate the pyroptosis of microglia. Molecular Medicine, 27(1), 1-10.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
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For research use only. Not intended for any clinical use.

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