Type of antibody:
Primary antibodies
mouse IgG1κ
Alternative names:
PVRL1, CLPED1, ED4, HV1S, HveC, OFC7, PRR, PVRR, Nectin-1

Specifications for CD111 Antibody, anti-human


Clone R1.302 recognizes the CD111 antigen, a 75 kDa type I transmembrane glycoprotein also known as poliovirus receptor related 1 protein (PRR1), PVRL1, HveC, and Nectin-1. Nectins are involved in the formation of the mechanical adhesive puncta adherentia junctions of synapses. CD111 is an adhesion molecule that can be found in a wide range of tissues where it localizes in various junctions such as the adherens junction of epithelial tissue or the chemical synapse of neurons. In the chemical synapse, CD111 interacts with PVRL3 and both proteins can be found in neuronal tissue already in early stages of brain development as well as in aging brains. CD111 also functions as an entry receptor for herpes simplex virus and pseudorabies virus.

Alternative names

PVRL1, CLPED1, ED4, HV1S, HveC, OFC7, PRR, PVRR, Nectin-1

Detailed product information

Technical specifications

Isotypemouse IgG1κ
Isotype controlIsotype Control Antibody, mouse IgG1
Type of antibodyPrimary antibodies
Alternative names of antigenPVRL1, CLPED1, ED4, HV1S, HveC, OFC7, PRR, PVRR, Nectin-1
Molecular mass of antigen [kDa]54
Distribution of antigenother
Entrez Gene ID5818
RRIDAB_2654534, AB_2654535, AB_2654536, AB_2654537, AB_2654538, AB_2654539, AB_2654540, AB_2654541, AB_2654542, AB_2654533

Resources for CD111 Antibody, anti-human


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References for CD111 Antibody, anti-human


  1. Cocchi, F. et al. (1998) The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D. Proc. Natl. Acad. Sci. U.S.A. 95(26): 15700-15705
  2. Rikitake, Y. et al. (2012) The role of nectins in different types of cell-cell adhesion. J. Cell. Sci. 125: 3713-3722
  3. Takahashi, K. et al. (1999) Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein. J. Cell Biol. 145(3): 539-549

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