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Mouse Anti-HERPUD1 Recombinant Antibody (CBFYH-0935) (CBMAB-H1868-FY)

This product is mouse antibody that recognizes HERPUD1. The antibody CBFYH-0935 can be used for immunoassay techniques such as: IF, IHC-P, WB.
See all HERPUD1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-0935
Antibody Isotype
IgG2a
Application
IF, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a
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
Concentration
1 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.

Target

Full Name
Homocysteine Inducible ER Protein With Ubiquitin Like Domain 1
Introduction
The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the ER stress response. This response includes the inhibition of translation to prevent further accumulation of unfolded proteins, the increased expression of proteins involved in polypeptide folding, known as the unfolded protein response (UPR), and the destruction of misfolded proteins by the ER-associated protein degradation (ERAD) system. This gene may play a role in both UPR and ERAD. Its expression is induced by UPR and it has an ER stress response element in its promoter region while the encoded protein has an N-terminal ubiquitin-like domain which may interact with the ERAD system. This protein has been shown to interact with presenilin proteins and to increase the level of amyloid-beta protein following its overexpression. Alternative splicing of this gene produces multiple transcript variants encoding different isoforms. The full-length nature of all transcript variants has not been determined.
Entrez Gene ID
9709
UniProt ID
Q15011
Alternative Names
Homocysteine Inducible ER Protein With Ubiquitin Like Domain 1; Homocysteine-Inducible, Endoplasmic Reticulum Stress-Inducible, Ubiquitin-Like Domain Member 1; Methyl Methanesulfonate (MMF)-Inducible Fragment Protein 1; Mif1; HERP; Homocysteine-Inducible Endoplasmic Reticulum Stress-Inducible Ubiquitin-Like Domain Member 1 Protein
Function
Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:16289116, PubMed:28827405).

Could enhance presenilin-mediated amyloid-beta protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway (PubMed:18307982).
Biological Process
Endoplasmic reticulum calcium ion homeostasis Source: ParkinsonsUK-UCL
Endoplasmic reticulum unfolded protein response Source: GO_Central
Negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
Negative regulation of intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
Positive regulation of ER-associated ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
Protein targeting to ER Source: Ensembl
Regulation of ER-associated ubiquitin-dependent protein catabolic process Source: GO_Central
Regulation of protein ubiquitination Source: Ensembl
Response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Response to unfolded protein Source: UniProtKB
Retrograde protein transport, ER to cytosol Source: ParkinsonsUK-UCL
Ubiquitin-dependent ERAD pathway Source: UniProtKB
Ubiquitin-dependent protein catabolic process Source: GO_Central
Cellular Location
Endoplasmic reticulum membrane
Topology
Cytoplasmic: 1-263
Helical: 264-284
Lumenal: 285-289
Helical: 290-310
Cytoplasmic: 311-391

Xie, W., Shan, Y., Wu, Z., Liu, N., Yang, J., Zhang, H., ... & Guo, H. (2023). Herpud1 deficiency alleviates homocysteine-induced aortic valve calcification. Cell Biology and Toxicology, 1-20.

Alagappan, L. P., Ramaswamy, Y., Sundaramoorthy, D. K., Bhaskar, J., Sarangapani, S., Sen, P., ... & Mathavan, S. (2023). Association of HERPUD1 genetic variant rs2217332 with age-related macular degeneration and polypoidal choroidal vasculopathy in an Indian cohort. Graefe's Archive for Clinical and Experimental Ophthalmology, 261(4), 1205-1212.

Peng, Y., Li, N., Tang, F., Qian, C., Jia, T., Liu, J., & Xu, Y. (2022). Corosolic acid sensitizes ferroptosis by upregulating HERPUD1 in liver cancer cells. Cell Death Discovery, 8(1), 376.

Nie, X., Liu, D., Zheng, M., Li, X., Liu, O., Guo, Q., ... & Lin, B. (2022). HERPUD1 promotes ovarian cancer cell survival by sustaining autophagy and inhibit apoptosis via PI3K/AKT/mTOR and p38 MAPK signaling pathways. BMC cancer, 22(1), 1338.

Mikawa, M., Sakai, C., Yamamoto, T., Nakamura, Y., Tanaka, S., Tominaga, N., ... & Yano, M. (2022). Herpud1 suppress angiotensin II induced hypertrophy in cardiomyocytes. Biochemistry and Biophysics Reports, 30, 101248.

Li, W., Wang, Y., Zhu, L., Du, S., Mao, J., Wang, Y., ... & Yi, Q. (2021). The P300/XBP1s/Herpud1 axis promotes macrophage M2 polarization and the development of choroidal neovascularization. Journal of Cellular and Molecular Medicine, 25(14), 6709-6720.

Liu, C., Xu, X., Huang, C., Zhang, L., Shang, D., Cai, W., & Wang, Y. (2020). Circ_002664/miR-182–5p/Herpud1 pathway importantly contributes to OGD/R-induced neuronal cell apoptosis. Molecular and cellular probes, 53, 101585.

Li, Y., Xie, Y., Hao, J., Liu, J., Ning, Y., Tang, Q., ... & Lv, X. (2018). ER-localized protein-Herpud1 is a new mediator of IL-4-induced macrophage polarization and migration. Experimental Cell Research, 368(2), 167-173.

Navarro-Marquez, M., Torrealba, N., Troncoso, R., Vásquez-Trincado, C., Rodriguez, M., Morales, P. E., ... & Lavandero, S. (2018). Herpud1 impacts insulin-dependent glucose uptake in skeletal muscle cells by controlling the Ca2+-calcineurin-Akt axis. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1864(5), 1653-1662.

Américo-Da-Silva, L., Diaz, J., Bustamante, M., Mancilla, G., Oyarzun, I., Verdejo, H. E., & Quiroga, C. (2018). A new role for HERPUD1 and ERAD activation in osteoblast differentiation and mineralization. The FASEB Journal, 32(9), 4681-4695.

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

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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