Analytical Data
-
Gene name
Nectin-4
-
简介
The Nectin-4 Protein IgV domain is pivotal in cell adhesion, participating in trans-homophilic and -heterophilic interactions, notably with NECTIN1. While it doesn't serve as an alpha-herpesvirus entry receptor, it functions as a receptor for measles virus, enabling virus entry into host cells. This dual role underscores the importance of Nectin-4 in cell adhesion and its specific role as a measles virus infection receptor. Nectin-4 Protein, Human (HEK293, His) is the recombinant human-derived Nectin-4 protein, expressed by HEK293 , with C-6*His labeled tag.
- Application
-
Biological Activity
1.Immobilized Anti-Human Nectin-4 mAb-mFc at 2 μg/mL (100 μl/well) can bind Human Nectin-4-His .The ED50 of Human Nectin-4-His is 16.29-50 ng/mL. 2.Measured by the ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 2.94 μg/mL, corresponding to a specific activity is 3.4×105 units/mg. 3. Loaded Bulumtatug (HY-P990977) on AHC2 biosensor, can bind Nectin-4 Protein, Human (HEK293, His) with an affinity constant of 4.327E-09 M as determined in BLI assay. Measured by the ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 2.94 μg/mL, corresponding to a specific activity is 3.4×105 units/mg. Loaded Bulumtatug (HY-P990977) on AHC2 biosensor, can bind Nectin-4 Protein, Human (HEK293, His) with an affinity constant of 4.327E-09 M as determined in BLI assay.
-
Alternative Names
PVRL4; Nectin-4; Ig superfamily receptor LNIR; Poliovirus receptor-related protein 4; PRR4; LNIR; Nectin4
-
Species
Human
-
Source
HEK293
-
Tag
C-6*His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96NY8-1
-
Expression Region
G32-V351
-
AA Sequence
GELETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQADEGEYECRVSTFPAGSFQARLRLRVLVPPLPSLNPGPALEEGQGLTLAASCTAEGSPAPSVTWDTEVKGTTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQDQRITHILHVSFLAEASVRGLEDQNLWHIGREGAMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVDVLDPQEDSGKQVDLVSASVV
-
Protein Length
Partial
-
Molecular Weight
40-48 kDa.
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Nectin-4 is a member of the immunoglobulin superfamily and plays a crucial role in cellular adhesion and signaling. It is predominantly expressed in epithelial tissues and is known for its involvement in various physiological processes, including cellular differentiation, proliferation, and immune response regulation. Recent studies have highlighted Nectin-4 as an emerging target in cancer research, particularly in breast and ovarian cancers, where it is often overexpressed. This overexpression correlates with poor prognosis and increased tumor aggressiveness, making Nectin-4 a potential biomarker for cancer progression. The generation of recombinant Nectin-4 proteins has facilitated the exploration of its functional properties and interactions with other cellular components. Such research aims to understand the molecular mechanisms by which Nectin-4 contributes to tumorigenesis and cancer metastasis. Furthermore, recombinant Nectin-4 is being investigated as a target for novel therapeutic strategies, including antibody-based treatments that can elicit immune responses against Nectin-4-expressing tumor cells. Overall, the study of recombinant Nectin-4 proteins is paving the way for innovative cancer therapies and improved diagnostic tools, ultimately contributing to better management of Nectin-4-associated malignancies.











