Recombinant Human DLL1/Delta-1 Protein (His Tag) | PKSH033699

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575-PKSH033699
€567.00
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Description

Recombinant Human DLL1/Delta-1 Protein (His Tag) | PKSH033699 | Gentaur US, UK & Europe Disrtribition

Synonyms: Delta-like protein 1; Drosophila Delta homolog 1; Delta1; H-Delta-1; DLL1;DELTA1;DL1

Active Protein: N/A

Activity: Recombinant Human Delta-like Protein 1 is produced by our Mammalian expression system and the target gene encoding Gln18-Gly540 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Human Delta-like Protein 1 is produced by our Mammalian expression system and the target gene encoding Gln18-Gly540 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-His

Species: Human

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 57.3 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Delta-like protein 1 (DLL1) is a type I transmembrane protein that belongs to the Delta/Serrate/Lag2 (DSL) family of Notch ligands. Mature human DLL1 consists of a 528 amino acid (aa) extracellular domain (ECD) with one DSL domain and eight EGF-like repeats, a 23 aa transmembrane segment, and a 155 aa cytoplasmic domain. Within the ECD, human DLL1 shares 91% aa sequence identity with mouse and rat DLL1. The residual membranebound portion of DLL1 can be cleave by presenilin-dependent γ-secretase, enabling the cytoplasmic domain to migrate to the nucleus. DLL1 localizes to adherens junctions on neuronal processes through its association with the scaffolding protein MAGI1. DLL1 is widely expressed, and it plays an important role in embryonic somite formation, cochlear hair cell differentiation, plus B and T lymphocyte differentiation. The upregulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis. DLL1 is also overexpressed in cervical carcinoma and glioma and contributes to tumor progression.

Research Area: Neuroscience, Developmental Biology, epigenetics and nuclear signal, Stem cells

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