Product Details

Target Names

DERL1

Uniprot No.

Q9BUN8

Alternative Names

DERL1; DER1; UNQ243/PRO276; Derlin-1; Degradation in endoplasmic reticulum protein 1; DERtrin-1; Der1-like protein 1

Species

Homo sapiens (Human)

Expression Region

1-251

Target Protein Sequence

MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPEAFLYRFQIWRPITATF YFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFMLLFNWICIVITGLAMDMQL LMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVG HLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRH NWGQGFRLGDQ

Protein Length

full length protein

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. Forms homotetramers which encircle a large channel traversing the endoplasmic reticulum (ER) membrane. This allows the retrotranslocation of misfolded proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome. The channel has a lateral gate within the membrane which provides direct access to membrane proteins with no need to reenter the ER lumen first. May mediate the interaction between VCP and the misfolded protein. 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. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.; (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.

Gene References into Functions

Overexpression of Derlin-1 is Associated with Non-small Cell Lung Cancer. PMID: 29530993
These findings for the first time revealed that miR-598, as a tumor suppressor, negatively regulate DERL1 and Epithelial-Mesenchymal Transition to suppress the invasion and migration in Non-Small Cell Lung Cancer (NSCLC), thereby putatively serving as a novel therapeutic target for NSCLC clinical treatment. PMID: 29768262
ChIP assays were used to ascertain the correlations between HNF1beta and Derlin-1 in the miR-217/HNF1beta/Derlin-1 pathway in glioma cells PMID: 28219405
The derlin-1 pathway therefore may represent a significant early checkpoint in the recognition and degradation of ENaC in mammalian cells. PMID: 28137758
Derlin-1 is overexpressed in bladder cancer and promotes malignant phenotype through ERK/MMP-2/9 and PI3K/AKT signaling pathway. PMID: 28178653
Derlin-1 was overexpressed in bladder cancer and was associated with the malignancy of bladder cancer. PMID: 27977784
insights into the interactions between other SHP-containing proteins and p97N PMID: 27714797
data suggest that miR-181d is a tumor suppressor in ESCC inversely regulating its downstream target gene of DERL1. PMID: 27572270
Results showed that Derlin-1 is overexpressed in colon cancer and promotes proliferation of colon cancer cells. PMID: 26173415
TMEM129 contains an unusual cysteine-only RING with intrinsic E3 ligase activity and is recruited to US11 via Derlin-1. PMID: 25030448
Cav-1 may be a cofactor in the interaction of Derlin-1 and N-glycosylated COX-2 and may facilitate Derlin-1- and p97 complex-mediated COX-2 ubiquitination, retrotranslocation, and degradation. PMID: 24089527
Derlin-1 is overexpressed in non-small cell lung cancer and promotes invasion by EGFR-ERK-mediated up-regulation of MMP-2 and MMP-9. PMID: 23306155
Upregulation of derlin-1 may be associated with endoplasmic reticulum stress in neuronal cells in Alzheimer's disease. PMID: 22627700
These results indicate that ApoB after lipidation is dislocated from the ER lumen to the LD surface for proteasomal degradation and that Derlin-1 and UBXD8 are engaged in the predislocation and postdislocation steps, respectively. PMID: 22238364
Derlin-1 expression levels may affect glucose-stimulated insulin secretion by altering surface expression of K(ATP) channels. PMID: 22311976
Derlin-1 is a negative regulator for both glycosylated and non-glycosylated BCRP expression and provide a novel posttranslational regulatory mechanism of BCRP by Derlin-1. PMID: 21184741
Derlin-1 is an important factor for the extraction of certain aberrantly folded proteins from the mammalian ER PMID: 15215855
Derlin-1 interacts with the N-terminal domain of PNGase via its cytosolic C-terminus. PNGase distributed in two populations; ER-associated and free in the cytosol, which suggests the deglycosylation process can proceed at either site PMID: 16055502
Derlin-1 is part of a retrotranslocation channel that is associated with both the polyubiquitination and p97-ATPase machineries at the endoplasmic reticulum membrane. PMID: 16186510
Derlin-1 recognizes misfolded, nonubiquitylated CFTR to initiate its dislocation and degradation early in the course of CFTR biogenesis, perhaps by detecting structural instability within the first transmembrane domain PMID: 16954204
The pool of active Derlin-1 in the ER membrane can be modulated in response to ER stress. PMID: 17453418
SVIP is an endogenous inhibitor of ERAD that acts through regulating the assembly of the gp78-p97/VCP-Derlin1 complex. PMID: 17872946
DERL1-containing protein mediates the endoplasmic reticulum-associated degradation of V2 vasopressin receptors. PMID: 18048502
These findings indicate that Derlin-1 facilitates the retro-translocation of Cholera toxin. PMID: 18094046
derlin-1 overexpression in breast cancer, together with its function in relieving ER stress-induced apoptosis, suggests that regulation of the ER stress response pathway may be critical in the development and progression of breast cancer. PMID: 18205950
KCa3.1 and KCa2.3 are translocated out of the endoplasmic reticulum associated with Derlin-1. PMID: 18227067
Overexpression of DERL1 is associated with neoplasms PMID: 18927294
Derlin-1 did not modify KCNQ1 expression level, and no interaction between endogenous KCNQ1 and Derlin-1 could be detected. PMID: 19114714

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Subcellular Location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Protein Families

Derlin family

Tissue Specificity

Ubiquitous.

Database Links

HGNC: 28454

OMIM: 608813

KEGG: hsa:79139

STRING: 9606.ENSP00000259512

UniGene: Hs.241576

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Code	CSB-CF887128HU
MSDS	MSDS
Size	Pls inquire
Source	in vitro E.coli expression system
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Recombinant Human Derlin-1 (DERL1)

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