Mouse Anti-DERL1 Recombinant Antibody (1B9) (CBMAB-D0710-YC)

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Basic Information

Host Animal
Mouse
Clone
1B9
Application
ELISA, WB
Immunogen
DERL1 (AAH02457, 134 a.a. ~ 233 a.a) partial recombinant protein with GST tag. The immunogen sequence: AQLNRDMIVS FWFGTRFKAC YLPWVILGFN YIIGGSVINE LIGNLVGHLY FFLMFRYPMD LGGRNFLSTP QFLYRWLPSR RGGVSGFGVP PASMRRAADQ
Specificity
Human
Antibody Isotype
IgG1, κ
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!]

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 134-233
More Infomation

Target

Full Name
Der1-like domain family, member 1
Introduction
DERL1 is a member of the derlin family. Members of this family participate in the ER-associated degradation response and retrotranslocate misfolded or unfolded proteins from the ER lumen to the cytosol for proteasomal degradation. This protein recognizes substrate in the ER and works in a complex to retrotranslocate it across the ER membrane into the cytosol. This protein may select cystic fibrosis transmembrane conductance regulator protein (CFTR) for degradation as well as unfolded proteins in Alzheimer's disease. Alternative splicing results in multiple transcript variants that encode different protein isoforms.
Entrez Gene ID
UniProt ID
Alternative Names
Derlin 1; Degradation In Endoplasmic Reticulum Protein 1; Der1-Like Domain Family, Member 1; DERtrin-1; DER1; Der1-Like Protein 1; Derlin-1; DER-1;
Function
Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein (PubMed:15215856).

Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908).

By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333).

(Microbial infection) In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class I heavy chains. Also participates in the degradation process of misfolded cytomegalovirus US2 protein.
Biological Process
Endoplasmic reticulum unfolded protein response Source: UniProtKB
ERAD pathway Source: ParkinsonsUK-UCL
ER-associated misfolded protein catabolic process Source: ParkinsonsUK-UCL
Establishment of protein localization Source: UniProtKB
Positive regulation of protein binding Source: ParkinsonsUK-UCL
Positive regulation of protein ubiquitination Source: ParkinsonsUK-UCL
Protein destabilization Source: UniProtKB
Protein folding Source: Reactome
Protein ubiquitination Source: Reactome
Response to unfolded protein Source: MGI
Retrograde protein transport, ER to cytosol Source: UniProtKB
Transmembrane transport Source: Reactome
Ubiquitin-dependent ERAD pathway Source: UniProtKB
Viral process Source: UniProtKB-KW
Cellular Location
Endoplasmic reticulum membrane
Topology
Cytoplasmic: 2-22
Helical: 23-43
Lumenal: 44-59
Helical: 60-80
Cytoplasmic: 81-105
Helical: 106-126
Lumenal: 127-154
Helical: 155-175
Cytoplasmic: 176-251

Jhan, J. H., Hsu, W. C., Lee, Y. C., Li, W. M., Huang, A. M., Lin, H. H., ... & Ke, H. L. (2022). MicroRNA-375-3p suppresses upper tract urothelial carcinoma cell migration and invasion via targeting Derlin-1. Cancers, 14(4), 880.

Shigeishi, H., Yokoyama, S., Murodumi, H., Sakuma, M., Fukada, S., Okuda, S., ... & Ohta, K. (2022). Melatonin enhances cisplatin‐induced cell death through inhibition of DERL1 in mesenchymal‐like CD44high OSCC cells. Journal of Oral Pathology & Medicine, 51(3), 281-289.

Sugiyama, T., Murao, N., Kadowaki, H., Takao, K., Miyakawa, T., Matsushita, Y., ... & Nishitoh, H. (2021). ERAD components Derlin-1 and Derlin-2 are essential for postnatal brain development and motor function. Iscience, 24(7), 102758.

Cai, Y., Xu, K., Aihaiti, Y., Li, Z., Yuan, Q., Xu, J., ... & Xu, P. (2021). Derlin-1, as a Potential Early Predictive Biomarker for Nonresponse to Infliximab Treatment in Rheumatoid Arthritis, Is Related to Autophagy. Frontiers in immunology, 12, 795912-795912.

Fan, J., Tian, L., Huang, S., Zhang, J., & Zhao, B. (2020). Derlin-1 promotes the progression of human hepatocellular carcinoma via the activation of AKT pathway. OncoTargets and therapy, 13, 5407.

Liu, Y., Wang, Z., Liu, H., Wang, X., Zhang, Z., Xiao, B., ... & Zhang, J. (2020). Derlin-1 functions as a growth promoter in breast cancer. Biological Chemistry, 401(3), 377-387.

Yang, F., Wei, K., Qin, Z., Liu, W., Shao, C., Wang, C., ... & Shen, H. (2018). MiR-598 suppresses invasion and migration by negative regulation of derlin-1 and epithelial-mesenchymal transition in non-small cell lung cancer. Cellular Physiology and Biochemistry, 47(1), 245-256.

Kadowaki, H., Satrimafitrah, P., Takami, Y., & Nishitoh, H. (2018). Molecular mechanism of ER stress-induced pre-emptive quality control involving association of the translocon, Derlin-1, and HRD1. Scientific reports, 8(1), 1-11.

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

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