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Description
DLL3(312-492aa) His Tag Protein, HumanProduct Specification Species Human Synonyms DLL3, Delta3, delta like 3 (Drosophila), delta like protein 3, Pudgy, SCDO1, SCDO1delta3 Accession Q9NYJ7 Amino Acid Sequence Ser312 Arg490, with C terminal His Expression System HEK293 Molecular Weight 20 24kDa Purity >95% by SDS PAGE Endotoxin <0. 1EU g Conjugation Unconjugated Tag His Tag Physical Appearance Lyophilized Powder Storage Buffer PBS, pH7. 4 Reconstitution Reconstitute at 0. 1 1 mg ml
Product Specification
| Species | Human |
| Synonyms | DLL3, Delta3, delta-like 3 (Drosophila), delta-like protein 3, Pudgy, SCDO1, SCDO1delta3 |
| Accession | Q9NYJ7 |
| Amino Acid Sequence | Ser312-Arg490, with C-terminal His |
| Expression System | HEK293 |
| Molecular Weight | 20-24kDa |
| Purity | >95% by SDS-PAGE |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, pH7.4 |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles. |
| Reference |
1、Ladi E. et al. (2005) The divergent DSL ligand DLL3 does not activate Notch signaling but cell autonomously attenuates signaling induced by other DSL ligands. J Cell Biol. 170: 983-992. 2、Xiu M X. et al. (2020) The role of DLLs in cancer: a novel therapeutic target. Onco Targets Ther. 13: 3881-3901. |
Background
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. Mature human DLL3 consists of a 466 amino acid (aa) extracellular domain (ECD) with one DSL domain and six EGF-like repeats, a 21 aa transmembrane segment, and a 105 aa cytoplasmic domain. Within the ECD, human DLL3 shares 86% aa sequence identity with mouse and rat DLL3. DLL3 is known as a divergent DSL ligand since it does not function in similar manner as the rest of DSL ligands. It does not activate Notch signaling through trans-activation, but autonomously attenuates signaling induced by other DSL ligands. A loss-of-function mutation of DLL3 is linked to axial skeletal defects in the spondylocostal dysplasia, which is linked to abnormal Notch signaling. DL-3 promotes proliferation and inhibits apoptosis of cancer cells. The proliferative effect mediated by DLL3 is thought to be due to increased Akt phosphorylation in cancer cells.
The Notch pathway is a highly conserved cell signaling pathway that is implicated in malignant transformation, cell proliferation, cycle arrest, and apoptosis, epithelial to mesenchymal transition, and suppression of neuroendocrine differentiation. The Notch signaling pathway is initiated by the binding of one of five ligands (Jagged 1 [Jag 1], Jag 2, DLL1, DLL3, DLL4) with one of four receptors (Notch 1-4). The DLL family of proteins interact with EGF repeats on Notch receptors on cell membranes, triggering Notch signaling. In canonical Notch signaling, ligand binding results in the intracellular cleavage of the receptor by metalloproteases, and the Notch intracellular domain then translocates into the nucleus and modulates transcription of Notch-responsive genes. Notch signaling can be oncogenic or tumor suppressive depending on the cellular context.DLL1 has a tumor-suppressive role in lung cancer and is poorly expressed in the bone marrow of patients with lung cancer. In contrast, DLL1 has an oncogenic role in breast cancer, and its overexpression is associated with a poorer prognosis.DLL4 has an oncogenic role in a range of cancers.DLL3 is a noncanonical inhibitory ligand of the Notch receptor that is involved in NEC/NET tumorigenesis.DLL3 is thought to inhibit Notch signaling in cis; it does not bind or activate Notch receptors when presented in trans. In normal tissues, DLL3 is generally expressed at low levels (if at all) and confined to the cytoplasm. It regulates Notch signaling by preventing the localization of Notch receptors to the cell surface and redirecting them to the endosomes for degradation.
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4.3 ★★★★★
Based on 7 reviews
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Product Reviews
★★★★★ 5
Very detailed! Beautiful world building! Strong Heroine!
Format: Kindle
Starts off a little slow and confusing with different POV’s, but starts to all come together towards the middle to make an elaborate plot line and makes it all worth it. Beautiful world building and attention to detail as well as great writing. The cliffhanger was gut wrenching! Can’t wait for the next book!
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Reviewed in the United States on March 4, 2020
★★★★★ 4
Interesting
Format: Kindle
This was a very captivating book once you got into it thoroughly. But the third person perspective was a bit hard to get used to. But as you got into it and followed the different characters, it was interesting and filled with intrigue, conflict and forbidden love.
I can’t wait to read the next one and to complete the series.
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Reviewed in the United States on November 12, 2022
★★★★★ 5
OUTSTANDING
Format: Kindle
This was very, very good. The world is vast and characters are complex. There is a good plot with a whole lot going on. This is well written. Good twists and turns and some heart breaking moments. You will love these characters, they have heart and loyalty. I am hoping that there will be several more books. We've yet to see anything from the Sea Court but only a mention of them here and there. The Wood Court was given a quick couple of scenes, and only as far as some warriors, we've yet to enter their court and the Shadow Court, I'm not sure if they will be a force for good or bad, but they definitely will play a much bigger role moving forward. This is primarily the Ice and Air Courts. Told in multiple views, which I loved, it gives you a chance to see things from different eyes. There's alot of political maneuvering and deception. I loved it and will pick up the next book as it becomes available. If you like The Fae and the courts, you should love this. I think the author has mucn in store for us.
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Reviewed in the United States on March 8, 2020
★★★★★ 4
Definitely worth the read!
Format: Kindle
After taking a deep breath and taking in that wicked twist of an ending, I have finally composed myself. My first thought when I started this book was that I love Reyna's character. I was intrigued by her connection with her familiar and the Ruin that is plaguing her land. It came as no surprise that she took her sister's place in an attempt to protect her. When they reach the Air Court everything slows down. This is where it was iffy for me. First of all, I like multiple POV's in books however 7 is a bit much. It starts to interrupt the story line. I felt like I was finally making progress connecting with one character, then it was switched to another person. I felt they all had necessary or pertinent information but not necessarily were they all POV worthy. The only other thing that annoyed me was that Reyna constantly was " trapped." She would rush off without thinking, only to need rescuing. She is brilliant in a fight, but she really doesn't think through anything. Lorcan is amazing. I know he might be on the "bad" list, but his background is so interesting. Eislyn(Reyna's sister) is really so sweet, but calculating. I enjoyed her and Thane's dialogue. The author did an amazing job with the imagery in this book. Everything was so detailed it was easy to fall into the scene. I love unexpected twists and while part of the ending I expected, I wasn't expecting how it took place. All in all, I found it very entertaining and I am very invested in continuing this series.
Favorite quotes:
"The truth may be twisted but never false."
"Who was she if she was not the enemy of the Air Court? What was her purpose of she no longer has that?"
"In a war-torn land, love was always a lie."
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Reviewed in the United States on March 4, 2020
★★★★★ 5
Great Read!!! Great story!!!
Format: Kindle
The series is long, but Ms. Wolfhart does a fantastic job of weaving this tale while bringing so much to the characters. Surprises and plot twists along the way to keep you intrigued. There is some graphic sex, but is no way the focal point. Grammar was excellent (a rare find with a lot of self publishers) with only a few noted errors. I rarely give 4 stars, let alone 5.
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Reviewed in the United States on April 30, 2021