Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human ARH aa 250 to the C-terminus (Cysteine residue). The exact sequence is proprietary.Database link: Q5SW96
Conjugate
Unconjugated
Applications
Application Notes
WB: 1/10000 - 1/50000;
Target
Alternative Names
LDLRAP1; low density lipoprotein receptor adaptor protein 1; low density lipoprotein receptor adapter protein 1; ARH; ARH2; DKFZp586D0624; FHCB1; FHCB2; MGC34705; LDL receptor adaptor protein; autosomal recessive hypercholesterolemia protein; ARH1;
Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface.
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More
Citations
Have you cited DCABH-6641 in a publication? Let us know and earn a reward for your research.
Jossin, Y; Ignatova, N; et al. The central fragment of reelin, generated by proteolytic processing in vivo, is critical to its function during cortical plate development. JOURNAL OF NEUROSCIENCE 24:514-521(2004).
Hiesberger, T; Trommsdorff, M; et al. Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation. NEURON 24:481-489(1999).
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COA
Certificate of Analysis
