PCDHA12 Antibody | 23-627

PCDHA12 Antibody | 23-627 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse, Rat

Homology: N/A

Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 713-792 of human PCDHA12 (NP_114070.1) .

Research Area: Cancer, Cell Cycle, Neuroscience, Signal Transduction

Tested Application: WB, IHC

Application: WB: 1:500 - 1:2000
IHC: 1:50 - 1:100

Specificiy: N/A

Positive Control 1: HL-60

Positive Control 2: NCI-H460

Positive Control 3: NIH/3T3

Positive Control 4: Mouse spinal cord

Positive Control 5: Mouse brain

Positive Control 6: Mouse lung

Molecular Weight: Observed: 102kDa

Validation: N/A

Isoform: N/A

Purification: Affinity purification

Clonality: Polyclonal

Clone: N/A

Isotype: IgG

Conjugate: Unconjugated

Physical State: Liquid

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Concentration: N/A

Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.

Alternate Name: PCDHA12, MGC138485, MGC141932, PCDH-ALPHA12

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: This gene is a member of the protocadherin alpha gene cluster, one of three related gene clusters tandemly linked on chromosome five that demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The alpha gene cluster is composed of 15 cadherin superfamily genes related to the mouse CNR genes and consists of 13 highly similar and 2 more distantly related coding sequences. The tandem array of 15 N-terminal exons, or variable exons, are followed by downstream C-terminal exons, or constant exons, which are shared by all genes in the cluster. The large, uninterrupted N-terminal exons each encode six cadherin ectodomains while the C-terminal exons encode the cytoplasmic domain. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. Alternative splicing has been observed and additional variants have been suggested but their full-length nature has yet to be determined.