ldlrad3

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ldlrad3

Official Full Name low density lipoprotein receptor class A domain containing 3
Synonyms LDLRAD3; low density lipoprotein receptor class A domain containing 3; low-density lipoprotein receptor class A domain-containing protein 3; LRAD3
    • Species :
    • Human
    • Mouse
    • Zebrafish
    • Source :
    • HEK293
    • Mammalian Cell
    • Tag :
    • Fc
    • His
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human LDLRAD3-735H Recombinant Human LDLRAD3 Protein, Fc-tagged HEK293 Fc
    Mouse LDLRAD3-9028M Recombinant Mouse LDLRAD3 Protein Mammalian Cell His
    Zebrafish LDLRAD3-7090Z Recombinant Zebrafish LDLRAD3 Mammalian Cell His

    ldlrad3 involved in several pathways and played different roles in them. We selected most pathways ldlrad3 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ldlrad3 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    ldlrad3 has several biochemical functions, for example, beta-amyloid binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ldlrad3 itself. We selected most functions ldlrad3 had, and list some proteins which have the same functions with ldlrad3. You can find most of the proteins on our site.

    Function Related Protein
    beta-amyloid binding ACHE; APBB3; PION; HSD17B10; APOE; ITM2C; MAPK8IP2; COL25A1; CD74; CHRNA7

    ldlrad3 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ldlrad3 here. Most of them are supplied by our site. Hope this information will be useful for your research of ldlrad3.

    Campbell, LA; Puolakkainen, M; et al. Chlamydia pneumoniae binds to the lectin-like oxidized LDL receptor for infection of endothelial cells. MICROBES AND INFECTION 14:43-49(2012).
    Gaidukov, L; Nager, AR; et al. Glycine Dimerization Motif in the N-terminal Transmembrane Domain of the High Density Lipoprotein Receptor SR-BI Required for Normal Receptor Oligomerization and Lipid Transport. JOURNAL OF BIOLOGICAL CHEMISTRY 286:18452-18464(2011).

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