Recombinant Human VAP-A Protein, CF

R&D Systems | Catalog # 5820-VA

R&D Systems
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Key Product Details

  • R&D Systems E. coli-derived Recombinant Human VAP-A Protein (5820-VA)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession Number

Structure / Form

Monomer

Applications

Bioactivity
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Product Specifications

Source

E. coli-derived human VAP-A protein
Met1-Met132, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ala2

Predicted Molecular Mass

15.5 kDa

SDS-PAGE

16 kDa, reducing conditions

Activity

Measured by its binding ability in a functional ELISA.
When rmEphB2/Fc Chimera (Catalog # 467-B2) is coated at 2 μg/mL (100 μL/well), the concentration of rhVAP-A that produces 50% of the optimal binding response is found to be approximately 0.8‑4 μg/mL.

Formulation, Preparation, and Storage

5820-VA
Formulation Lyophilized from a 0.2 μm filtered solution in MOPS and NaCl.
Reconstitution

Reconstitute at 100 μg/mL in PBS.


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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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: VAP-A

Vesicle-associated membrane protein (VAMP)‑associated protein A (VAP‑A; also VAMP‑A and VAP-33) is a 33 kDa, ubiquitously expressed, type IV transmembrane protein belonging to the VAP family of proteins (1). It is found in plasma and ER membranes as well as in intracellular vesicles as a homodimer and a heterodimer with VAP-B. Human VAP-A is synthesized as a 249 amino acid (aa) precursor that contains a 227 aa cytoplasmic domain and a 21 aa transmembrane region. The cytoplasmic domain contains a mobile sperm protein (MSP) domain (aa 14 ‑ 131) and a coiled-coil region (aa 169 ‑ 205). Human VAP-A is 97% aa identical to mouse and rat VAP-A. VAP-A and VAP-B recruit FFAT (two phenylalanines in an acidic tract)-motif-containing proteins to the cytosolic surface of ER membranes through a conserved region within their MSP domain, and they have been implicated in regulation of membrane transport, phospholipid biosynthesis, and the unfolded protein response (2 ‑ 3). Their role in maintaining the identities of intracellular organelles has not been demonstrated, but their ability to interact with lipid-transfer/binding proteins (LT/BPs) may affect the lipid composition of certain cellular membranes (2, 4). One study shows that VAPs play a critical role in maintaining the structural and functional properties of the Golgi complex (2). Researchers found that knockdown of VAP reduces the levels of phosphatidylinositol-4-phosphate (PI4P), diacylglycerol (DAG), and sphingomyelin (SM) in Golgi membranes and exports pleiotropic effects in Golgi-mediated transport (2). The effects of VAPs are mediated by their interacting FFAT-motif-containing proteins Nir2, OSBP, and CERT (2). VAPs provide a scaffold for these LT/BPs at the ER-Golgi membrane contact sites, thereby affecting the lipid composition of the Golgi membranes and consequently their structural and functional identities (2). Most recently, researchers found that VAP-A associates and co‑localizes with protrudin, a protein that promotes neurite formation, and found that it was an important regulator both of the subcellular localization of protrudin and of its ability to stimulate neurite outgrowth (5).

References

  1. Weir, M.L. et al. (1998) Biochem. J. 333:247.
  2. Peretti, D. et al. (2008) Mol. Biol. Cell 19:3871.
  3. Kaiser, S.E. et al. (2005) Structure 13:1035.
  4. Loewen, C.J. et al. (2003) EMBO J. 22:2025.
  5. Saita, S. et al. (2009) J. Biol. Chem. 284:13766.

    Long Name

    VAMP [Vesicle-associated Membrane Protein]-associated Protein A

    Alternate Names

    VAMP-A, VAP-33, VAPA

    Entrez Gene IDs

    9218 (Human); 30960 (Mouse); 58857 (Rat)

    Gene Symbol

    VAPA

    UniProt

    Additional VAP-A Products

    Product Documents for Recombinant Human VAP-A Protein, CF

    Certificate of Analysis

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    Product Specific Notices for Recombinant Human VAP-A Protein, CF

    For research use only

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