R&D Systems代理3970-DL-050 Recombinant Rat DLL1 Fc Chimera Protein, CF (50 UG)

2025-06-25

货号:3970-DL-050

品牌:R&D Systems

规格:50ug

目录价:¥4490.00

市场价格:¥3592.00

会员价格:¥3592.00

  • 到货时间:3~4周

    金山科研平台,产品价格货期咨询微信:jinshanbio Source:Chinese Hamster Ovary cell line, CHO-derived Accession #:P97677 N-terminal Sequence Analysis:Ser22 Structure:Disulfide-linked homodimer Purity:>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Predicted Molecular Mass:82.6kDa (monomer) SDS-PAGE:90-95 kDa, reducing conditions Activity:Measured by its binding ability in a functional ELISA.When rrNotch-1 (Catalog # 1057-TK) is coated at 5 µg/mL, rrDLL-1 binds with an apparent KD < 5 nM. Formulation:Lyophilized from a 0.2 µm filtered solution in PBS.See Certificate of Analysis for details. Molecule Information: DLL1 Long Name: Delta-like 1 Aliases: Delta 1 Entrez Gene IDs: 28514 (Human); 13388 (Mouse); 84010 (Rat) Background: DLL1

    View DLL1 IHC images. Delta-like protein 1 (DLL1) is a 90 - 100 kDa type I transmembrane protein that belongs to the Delta/Serrate/Lag-2 (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. It shares 26%, 37%, and 54% aa sequence identity with DLL2, 3, and 4, respectively. A 60 kDa ECD fragment released by ADAM9, 12, or 17 mediated proteolysis, promotes the proliferation of hematopoietic progenitor cells. The residual membrane-bound portion of DLL1 can be cleaved by presenilin-dependent gamma-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.

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