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| Cat.No | ACP10131 | Target Name | PCDHA6 |
|---|---|---|---|
| Form | Lyophilized powder | Expression System | Custom Production. Please inquire and provide the desire expression system. |
| Protein Length | Partial | Purity | >85% (SDS-PAGE) |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q9UN73 |
|---|
Uniprot Id
Q9UN73
Target Species
Human
Target Name
PCDHA6
Target Full Name
Protocadherin alpha-6
Target Function
Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Target Subcellular Location
[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.
Target Synonyms
Cadherin related neuronal receptor 2; CNR 2; CNR2; CNRN 2; CNRN2; CNRS 2; CNRS2; CRNR 2; CRNR2; KIAA0345 like 8; PCDA6_HUMAN; PCDH alpha6; PCDH-alpha-6; PCDHA 6; PCDHA6; Protocadherin alpha 6; Protocadherin alpha-6
Target 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.
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