• Product nameAnti-L1CAM antibody [UJ181.4]
    See all L1CAM primary antibodies
  • Description
    Mouse monoclonal [UJ181.4] to L1CAM
  • SpecificityBinds to tumours of neural and glial origin and does not bind to paediatric or adult brain.
  • Tested applicationsSuitable for: IP, WBmore details
  • Species reactivity
    Reacts with: Human
  • Immunogen

    Tissue, cells or virus corresponding to Human L1CAM. 16 week human foetal brain
    Database link: P32004

  • General notesL1CAM can be detected between 200-220 kD. In brain samples it is typically seen at ~ 200 kD. When the protein is overexpressed in vitro it is often detected as a doublet with bands at 200 and 220 kD. The unglycosylated, unprocessed L1CAM is ~ 140-150 kDa. The protein has 21 putative N-glycosylation sites on the extracellular portion of the protein which, when they are all glycosylated, results in a detected MW of 200-220 kD depending upon how many residues are actually glycosylated. L1CAM can be cleaved by the metalloprotease ADAM10 resulting in fragments of 180 kD and 40 kD. L1CAM can also be cleaved by plasmin resulting in fragments of 140 kD and 80 kD. In theory, therefore, one could detect bands at ~220, 200, 180, 140, 80 and 40 kD. UJ181.4 can be used in diagnosis of primitive neuroectodermal tumours. It can be used for bone marrow purging and intrathecal targeting.



Our Abpromise guarantee covers the use of ab20149 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
  • Application notesIP: Use at an assay dependent dilution.
    WB: Use at an assay dependent dilution. Predicted molecular weight: 200-220 kDa. It may also detect smaller cleavage fragments (please see Notes below).

    Not yet tested in other applications.
    Optimal dilutions/concentrations should be determined by the end user.
  • Target

    • FunctionCell adhesion molecule with an important role in the development of the nervous system. Involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. Binds to axonin on neurons.
    • Involvement in diseaseDefects in L1CAM are the cause of hydrocephalus due to stenosis of the aqueduct of Sylvius (HSAS) [MIM:307000]. Hydrocephalus is a condition in which abnormal accumulation of cerebrospinal fluid in the brain causes increased intracranial pressure inside the skull. This is usually due to blockage of cerebrospinal fluid outflow in the brain ventricles or in the subarachnoid space at the base of the brain. In children is typically characterized by enlargement of the head, prominence of the forehead, brain atrophy, mental deterioration, and convulsions. In adults the syndrome includes incontinence, imbalance, and dementia. HSAS is characterized by mental retardation and enlarged brain ventricles.
      Defects in L1CAM are the cause of mental retardation-aphasia-shuffling gait-adducted thumbs syndrome (MASA) [MIM:303350]; also known as corpus callosum hypoplasia, psychomotor retardation, adducted thumbs, spastic paraparesis, and hydrocephalus or CRASH syndrome. MASA is an X-linked recessive syndrome with a highly variable clinical spectrum. Main clinical features include spasticity and hyperreflexia of lower limbs, shuffling gait, mental retardation, aphasia and adducted thumbs. The features of spasticity have been referred to as complicated spastic paraplegia type 1 (SPG1). Some patients manifest corpus callosum hypoplasia and hydrocephalus. Inter- and intrafamilial variability is very wide, such that patients with hydrocephalus, MASA, SPG1, and agenesis of corpus callosum can be present within the same family.
      Defects in L1CAM are the cause of spastic paraplegia X-linked type 1 (SPG1) [MIM:303350]. Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs.
      Note=Defects in L1CAM may contribute to Hirschsprung disease by modifying the effects of Hirschsprung disease-associated genes to cause intestinal aganglionosis.
      Defects in L1CAM are a cause of partial agenesis of the corpus callosum (ACCPX) [MIM:304100]. A syndrome characterized by partial corpus callosum agenesis, hypoplasia of inferior vermis and cerebellum, mental retardation, seizures and spasticity. Other features include microcephaly, unusual facies, and Hirschsprung disease in some patients.
    • Sequence similaritiesBelongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family.
      Contains 5 fibronectin type-III domains.
      Contains 6 Ig-like C2-type (immunoglobulin-like) domains.
    • Cellular localizationCell membrane.
    • Information by UniProt
    • Database links
    • Alternative names
      • Antigen identified by monoclonal antibody R1 antibody
      • CAML1 antibody
      • CD171 antibody
      • CD171 antigen antibody
      • HSAS antibody
      • HSAS1 antibody
      • Hyd antibody
      • L1 antibody
      • L1 cell adhesion molecule antibody
      • L1-NCAM antibody
      • L1cam antibody
      • L1CAM_HUMAN antibody
      • MASA antibody
      • MIC5 antibody
      • N CAML1 antibody
      • N-CAM-L1 antibody
      • NCAM-L1 antibody
      • NCAML1 antibody
      • Nerve-growth factor-inducible large external glycoprotein antibody
      • Neural cell adhesion molecule L1 antibody
      • NILE antibody
      • OTTHUMP00000025992 antibody
      • S10 antibody
      • SPG1 antibody
      see all

    References for Anti-L1CAM antibody [UJ181.4] (ab20149)

    This product has been referenced in:
    • Bourne S  et al. Monoclonal antibodies M340 and UJ181.4 recognize antigens associated with primitive neuroectodermal tumours/tissues. Hybridoma 8:415-26 (1989). Read more (PubMed: 2550359) »

    See 1 Publication for this product

    Product Wall

    Dear Professor Nikiforov, Thank you for your email and your patience. I have all of the information that you requested. L1CAM can be detected between 200-220 kD. In brain samples it is typically seen at ~ 200 kD. When the protein is overexpres...

    Read More