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Recombinant Mouse DDR2 Fc Chimera Protein, CF  50 UG图1

Recombinant Mouse DDR2 Fc Chimera Protein, CF 50 UG

2024-11-24 18:48IP属地 广东省东莞市 电信00留言

7479-DR

 

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.


Reconstitution Reconstitute at 250 μg/mL in PBS.



Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.


Stability & Storage:       Use a manual defrost freezer and avoid repeated freeze-thaw cycles.      

  • 12 months from date of receipt, -20 to -70 °C as supplied.

  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.

  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.


Background: DDR2

DDR2, also known as TYR010 and TKT, is a widely expressed 130 kDa type I transmembrane glycoprotein belonging to the discoidin‑like domain containing subfamily of receptor tyrosine kinases (1). Mature mouse DDR2 consists of a 378 amino acid (aa) extracellular domain (ECD) that includes the discoidin-like domain, a 22 aa transmembrane segment, and a 433 aa cytoplasmic domain that includes the kinase domain (2). Within the ECD, mouse DDR2 shares 50% aa sequence identity with DDR1. It shares 97% and 99% aa sequence identity with human and rat DDR2, respectively. The discoidin-like domain mediates DDR2 interactions with collagens I, III, and X (3‑5). Collagens II and V are less efficacious ligands (3). DDR2 selectively recognizes the triple helical structure of collagen compared to monomeric or denatured collagen (3, 5, 6). Within collagen II, the D2 period is required for DDR2 binding. The D1 period is additionally required to trigger DDR2 autophosphorylation (6). The ECD of DDR2 exists as a noncovalent dimer in solution, and dimerization of the receptor greatly enhances collagen binding (4, 7). DDR2 interaction with collagen I inhibits collagen fibrillogenesis and alters collagen fiber morphology (7). Ligand binding induces DDR2 autophosphorylation in the cytoplasmic domain (3, 5, 8), which promotes associations with Shc and Src (9). In addition to the above mechanism, DDR2 exhibits a distinct interaction with collagen X. A region other than the discoidin-like domain of DDR2 recognizes the non-helical NC1 domain of collagen X, and this interaction does not lead to receptor autophosphorylation (5). Activation of DDR2 by collagen induces up‑regulation of MMP-1, -2, and -13 as well as DDR2 itself (3, 8, 10). DDR2 is implicated in collagenous matrix destruction and cell invasiveness (8, 10). It promotes osteoblast and chondrocyte differentiation and supports ovulation and spermatogenesis (11‑13). DDR2 is up‑regulated in several pathological conditions, including hepatic fibrosis following injury, rheumatoid and osteoarthritis, and smooth muscle cell overgrowth diseases (8, 10, 14, 15).

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