LDLRAD2
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Official Full Name
low density lipoprotein receptor class A domain containing 2 -
Synonyms
LDLRAD2;low density lipoprotein receptor class A domain containing 2;low density lipoprotein receptor A domain containing 2;low-density lipoprotein receptor class A domain-containing protein 2
Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
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LDLRAD2-4785HCL | Recombinant Human LDLRAD2 293 Cell Lysate | HEK293 | Human | Non |
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Ldlrad2-3767M | Recombinant Mouse Ldlrad2 Protein, Myc/DDK-tagged | HEK293 | Mouse | Myc&DDK |
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Involved Pathway
LDLRAD2 involved in several pathways and played different roles in them. We selected most pathways LDLRAD2 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with LDLRAD2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Protein Function
LDLRAD2 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by LDLRAD2 itself. We selected most functions LDLRAD2 had, and list some proteins which have the same functions with LDLRAD2. You can find most of the proteins on our site.
Function | Related Protein |
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Interacting Protein
LDLRAD2 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 LDLRAD2 here. Most of them are supplied by our site. Hope this information will be useful for your research of LDLRAD2.
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References
- 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).