Recombinant Human VAP-A Protein, CF

Catalog # Availability Size / Price Qty
5820-VA-050
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Recombinant Human VAP-A Protein, CF Summary

Product Specifications

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.
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.
Source
E. coli-derived human VAP-A protein
Met1-Met132, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Ala2
Structure / Form
Monomer
Predicted Molecular Mass
15.5 kDa
SDS-PAGE
16 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

5820-VA

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS and NaCl.
Reconstitution Reconstitute at 100 μg/mL in 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.
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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
    Entrez Gene IDs
    9218 (Human); 30960 (Mouse); 58857 (Rat)
    Alternate Names
    hVAP-33; MGC3745,33 kDa VAMP-associated protein; VAMP (vesicle-associated membrane protein)-associated protein A, 33kDa; VAMP-A; VAP-33; VAP33VAMP (vesicle-associated membrane protein)-associated protein A (33kD); VAPA; VAP-A; VAP-AVAMP-associated protein A; vesicle-associated membrane protein-associated protein A

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