Recombinant Human Membrane-associated phosphatidylinositol transfer protein 1 (PITPNM1), partial

CAT:
399-CSB-RP019954h-01
Size:
20 µg
  • Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
  • Dry Ice Shipment: No
Recombinant Human Membrane-associated phosphatidylinositol transfer protein 1 (PITPNM1), partial - image 1

Recombinant Human Membrane-associated phosphatidylinositol transfer protein 1 (PITPNM1), partial

  • Product Name Alternative:

    Drosophila retinal degeneration B homologPhosphatidylinositol transfer protein, membrane-associated 1 ; PITPnm 1; Pyk2 N-terminal domain-interacting receptor 2 ; NIR-2
  • Abbreviation:

    Recombinant Human PITPNM1 protein, partial
  • Gene Name:

    PITPNM1
  • UniProt:

    O00562
  • Expression Region:

    1-238aa
  • Organism:

    Homo sapiens (Human)
  • Target Sequence:

    MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSM
  • Tag:

    N-terminal GST-tagged
  • Type:

    Developed Protein
  • Source:

    E.coli
  • Field of Research:

    Transport
  • Relevance:

    Regulates RHOA activity, and plays a role in cytoskeleton rodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro) . May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between mbranes . Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions.4 Publications
  • Endotoxin:

    Not test
  • Purity:

    Greater than 90% as determined by SDS-PAGE.
  • Activity:

    Not Test
  • Form:

    Liquid or Lyophilized powder
  • Buffer:

    If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
  • Reconstitution:

    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • Function:

    Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro) . May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes (By similarity) . Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions.
  • Molecular Weight:

    54.5 kDa
  • References & Citations:

    Human chromosome 11 DNA sequence and analysis including novel gene identification.Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.Nature 440:497-500 (2006)
  • Storage Conditions:

    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • Protein Length:

    Partial