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Recombinant Human Nectin-4/PVRL4 protein (His Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0415

Validation Data Gallery

  • Purity of Recombinant Human Nectin-4 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Human Nectin-4 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Human Nectin-4 protein Gly32-Ser349 (Accession# Q96NY8-1) with a His tag at the C-terminus.
GeneID 81607
Accession Q96NY8-1
PredictedSize 37.9 kDa
SDS-PAGE 40-52 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Nectin-4, also known as PVRL4, is a type-I transmembrane glycoprotein that belongs to the nectin subfamily of immunoglobulin-like adhesion molecules that participate in Ca(2+)-independent cell-cell adhesion. The extracellular domain of Nectin-4, which contains three immunoglobulin-like domains (V and two C2-type domains, VCC), can be proteolytically cleaved to release a soluble form. Nectin-4 interacts with afadin via its carboxyl-terminal cytoplasmic sequence and trans-interacts with nectin-1/PRR1 through V domain interaction. It acts as a receptor for measles virus. Nectin-4 is overexpressed in multiple human malignancies and the aberrant expression is correlated with cancer progression and poor prognostic.

References:

1. N Reymond, et al. (2001) J Biol Chem. 276(46):43205-15.
2. Stéphanie Fabre-Lafay. (2005) J Biol Chem. 280(20):19543-50.
3. Martin J Barron, et al. (2008) Hum Mol Genet. 17(22):3509-20.
4. Michael D Mühlebach, et al. (2011) Nature. 480(7378):530-3.
5. Wafa Bouleftour, et al. (2022) Mol Cancer Ther. 21(4):493-501.