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Rat Anti-PCDH12 Recombinant Antibody (15H131) (CBMAB-P0966-YC)


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Summary

Host Animal
Rat
Specificity
Mouse
Clone
15H131
Antibody Isotype
IgG
Application
IHC, WB

Basic Information

Immunogen
Recombinant protein corresponding to mouse Protocadherin-12
Specificity
Mouse
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized from PBS
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Protocadherin 12
Introduction
PCDH12 belongs to the protocadherin gene family, a subfamily of the cadherin superfamily. The encoded protein consists of an extracellular domain containing 6 cadherin repeats, a transmembrane domain and a cytoplasmic tail that differs from those of the classical cadherins. The gene localizes to the region on chromosome 5 where the protocadherin gene clusters reside. The exon organization of this transcript is similar to that of the gene cluster transcripts, notably the first large exon, but no significant sequence homology exists. The function of this cellular adhesion protein is undetermined but mouse protocadherin 12 does not bind catenins and appears to have no affect on cell migration or growth.
Entrez Gene ID
53601
UniProt ID
O55134
Alternative Names
Protocadherin 12; Vascular Cadherin-2; VE-Cadherin-2; VE-Cad-2; Vascular Endothelial Cadherin 2; Vascular Endothelial Cadherin-2; Protocadherin-12; VE-Cadherin 2; VECAD2;
Function
Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions (By similarity).
Acts as a regulator of cell migration, probably via increasing cell-cell adhesion (PubMed:21402705).
Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions (By similarity).
Unable to bind to catenins, weakly associates with the cytoskeleton (By similarity).
Biological Process
Calcium-dependent cell-cell adhesion via plasma membrane cell adhesion moleculesIEA:Ensembl
Cell adhesionManual Assertion Based On ExperimentIBA:GO_Central
Glycogen metabolic processIEA:Ensembl
Homophilic cell adhesion via plasma membrane adhesion moleculesIEA:Ensembl
Labyrinthine layer developmentIEA:Ensembl
Neuron recognitionManual Assertion Based On ExperimentTAS:ProtInc
Cellular Location
Protocadherin-12
Cell membrane
Cell junction
Protocadherin-12, secreted form
Secreted
The secreted form is produced following cleavage by ADAM10.
Involvement in disease
Diencephalic-mesencephalic junction dysplasia syndrome 1 (DMJDS1):
An autosomal recessive syndrome characterized by severe global developmental delay with profound intellectual disability, spasticity or dystonia, and congenital microcephaly. Brain imaging shows hypothalamic midbrain dysplasia, diencephalic-mesencephalic dysplasia, and intracerebral calcifications.
Topology
Extracellular: 25-718
Helical: 719-739
Cytoplasmic: 740-1184
PTM
Protocadherin-12
Cleaved by ADAM10 close to the transmembrane domain to release the Protocadherin-12, secreted form in the serum. Cleavage results in reduced cellular adhesion in a cell migration assay.
More Infomation

Rahşan, G. Ü. D. B. B., Gülen, G. P. Ö. Ş. K., & Haliloğlud, E. U. G. (2024). Many Faces of Diencephalic-Mesencephalic Junction Dysplasia Syndrome with GSX2 and PCDH12 Variants.

Rakotomamonjy, J., Rylaarsdam, L., Fares-Taie, L., McDermott, S., Davies, D., Yang, G., ... & Guemez-Gamboa, A. (2023). PCDH12 loss results in premature neuronal differentiation and impeded migration in a cortical organoid model. Cell reports, 42(8).

Rakotomamonjy, J., Rylaarsdam, L., Fares-Taie, L., McDermott, S., Davies, D., Yang, G., ... & Guemez-Gamboa, A. (2023). Impaired migration and premature differentiation underlie the neurological phenotype associated with PCDH12 loss of function. bioRxiv, 2023-01.

Fazeli, W., Bamborschke, D., Moawia, A., Bakhtiari, S., Tafakhori, A., Giersdorf, M., ... & Koy, A. (2022). The phenotypic spectrum of PCDH12 associated disorders-Five new cases and review of the literature. European Journal of Paediatric Neurology, 36, 7-13.

Aggarwal, S. (2022). Expanding spectrum of PCDH12 related phenotype begs exploration of multipronged pathomechanisms. European Journal of Paediatric Neurology, 36, A2-A3.

Accogli, A., El Kosseifi, C., Saint-Martin, C., Addour-Boudrahem, N., Rivière, J. B., Toffoli, D., ... & Srour, M. (2022). PCDH12 variants are associated with basal ganglia anomalies and exudative vitreoretinopathy. European Journal of Medical Genetics, 65(2), 104405.

Mattioli, F., Voisin, N., Preikšaitienė, E., Kozlovskaja, I., Kučinskas, V., & Reymond, A. (2021). Ophthalmic phenotypes associated with biallelic loss‐of‐function PCDH12 variants. American Journal of Medical Genetics Part A, 185(4), 1275-1281.

Reddy, C., Paria, P., Bhanudeep, S., Bhatia, V., & Saini, A. G. (2021). PCDH12-Related Movement Disorder. Journal of Pediatric Neurology, 19(06), 443-445.

Vineeth, V. S., Das Bhowmik, A., Balakrishnan, S., Dalal, A., & Aggarwal, S. (2019). Homozygous PCDH12 variants result in phenotype of cerebellar ataxia, dystonia, retinopathy, and dysmorphism. Journal of Human Genetics, 64(2), 183-189.

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For research use only. Not intended for any clinical use.

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