Recombinant Human VLDL R Protein, CF 25 UG

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Recombinant Human VLDL R Protein, CF 25 UG信息二维码

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3-Amino-5-methoxycarbonylphenylboronic acid, pinacol ester  1 g 2,3-Dichloro-6-(trifluoromethyl)benzyl bromide  1 g 1-(4-Fluorophenyl)-5-methoxycarbonyl-2(1H)-pyridinone  1 g N,N-Diethyl-cyclohexane-1,4-diamine  1 g N-Methyl-DL-leucine hydrochloride  5 g N-(2-Chloroethyl) 3-boronobenzamide  5 g

产品介绍

    基本参数

    详细说明

    • Purity
      >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
    • Endotoxin Level
      <0.10 EU per 1 μg of the protein by the LAL method.
    • Activity
      Measured by its binding ability in a functional ELISA. When Recombinant Human LRPAP is coated at 1 μg/mL (100 μL/well), the concentration of Recombinant Human VLDL R hat produces 50% of the optimal binding response is found to be approximately 5-30 ng/mL.
    • Source
      Human embryonic kidney cell, HEK293-derived Thr25-Ser797, with a C-terminal 6-His tag
    • Accession #
    • N-terminal Sequence
      Analysis
      Thr25
    • Predicted Molecular Mass
      86 kDa
    • SDS-PAGE
      116-142 kDa, reducing conditions
    8444-VL
     
    Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
    Reconstitution Reconstitute at 250 μg/mL in sterile 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.
    Data Images
    SDS-PAGE

    1 μg/lane ofRecombinant Human VLDL R (Catalog # 8444-VL)was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditionsand visualized by silver staining, showing bands at 129  and 107kDa, respectively.
    Background: VLDL R
    Very low density lipoprotein receptor (VLDL R) is a 130 kDa type I transmembrane protein that plays a significant role in lipid metabolism and in nervous system development and function (1). Mature human VLDL R consists of a 770 amino acid (aa) extracellular domain (ECD) with eight tandem LDLR class A repeats, three EGF-like domains, six tandem LDLR class B repeats, and a juxtamembrane region that is rich in O-linked glycosylation; a transmembrane segment, and a 54 aa cytoplasmic domain with one NPxY internalization motif (2). Within the ECD, human VLDLR shares 95% and 92% aa sequence identity with mouse and rat VLDL R, respectively. Alternative splicing of human VLDL R shows a deletion of the O-glycosylated region and also includes a critical determinant for ApoE binding (3, 4). VLDL R is predominantly expressed on endothelial cells lining capillaries and small arterioles (5). VLDL R participates in the tissue uptake of fatty acids from plasma by mediating the internalization of ApoE-containing lipoparticles ( i.e. VLDL, beta -VLDL, and chylomicron remnants) (6). VLDL R binds and internalizes lipoprotein lipase (LPL) and mediates its transport from the basolateral to the lumenal face of endothelial cells (7, 8). VLDL R knockout mice are characterized by reduced LPL activity and increased serum triglyceride clearance (9). VLDL R influences breast cancer cell motility by mediating the uptake of uPAR-PAI1 complexes (7, 10). Lipoprotein accumulation via macrophage VLDL R is instrumental in promoting the formation of atherosclerotic plaques (11). In the nervous system, VLDL R and ApoE R2 interactions with Reelin are critical for neuronal migration and positioning in the developing brain (12, 13). VLDL R also functions in adult hippocampal synapse maturation, synaptic plasticity, and memory formation (14).
    • References:
      1. May, P. et al. (2005) Cell. Mol. Life Sci. 62:2325.
      2. Sakai, J. et al. (1994) J. Biol. Chem. 269:2173.
      3. Iijima, H. et al. (1998) J. Biochem. 124:747.
      4. Ruiz, J. et al. (2005) J. Lipid Res. 46:1721.
      5. Wyne, K.L. et al. (1996) Arterioscler. Thromb. Vasc. Biol. 16:407.
      6. Hauser, P.S. et al. (2011) Prog. Lipid Res. 50:62.
      7. Argraves, K.M. et al. (1995) J. Biol. Chem. 270:26550.
      8. Obunike, J.C. et al. (2001) J. Biol. Chem. 276:8934.
      9. Yagyu, H. et al. (2002) J. Biol. Chem. 277:10037.
      10. Webb, D.J. et al. (1999) J. Biol. Chem. 274:7412.
      11. van Eck, M. et al. (2005) Atherosclerosis 183:230.
      12. Hiesberger, T. et al. (1999) Neuron 24:481.
      13. Trommsdorff, M. et al. (1999) Cell 97:689.
      14. Weeber, E.J. et al. (2002) J. Biol. Chem. 277:39944.
    • Long Name:
      Very Low Density Lipoprotein Receptor
    • Entrez Gene IDs:
      7436 (Human); 22359 (Mouse)
    • Alternate Names:
      CARMQ1; CHRMQ1; FLJ35024; very low density lipoprotein receptor; very low-density lipoprotein receptor; VLDL R; VLDL receptor; VLDLR; VLDL-R; VLDLRCH
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