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LIN7A Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | O14910 |
| Other Accession | Q9Z250, Q8JZS0, Q32LM6, NP_004655.1 |
| Reactivity | Human |
| Predicted | Bovine, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 25997 Da |
| Antigen Region | 180-207 aa |
| Gene ID | 8825 |
|---|---|
| Other Names | Protein lin-7 homolog A, Lin-7A, hLin-7, Mammalian lin-seven protein 1, MALS-1, Tax interaction protein 33, TIP-33, Vertebrate lin-7 homolog 1, Veli-1, LIN7A, MALS1, VELI1 |
| Target/Specificity | This LIN7A antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 180-207 amino acids from the C-terminal region of human LIN7A. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | LIN7A Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | LIN7A |
|---|---|
| Synonyms | MALS1, VELI1 |
| Function | Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta- catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. |
| Cellular Location | Cell membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Cell junction {ECO:0000250|UniProtKB:Q8JZS0}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8JZS0}. Note=Mainly basolateral in renal epithelial cells. {ECO:0000250|UniProtKB:Q8JZS0} |
| Tissue Location | Expressed in brain, testis, kidney, placenta and liver. |
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Provided below are standard protocols that you may find useful for product applications.
Background
LIN7A plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Lanktree, M., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B (6), 945-951 (2008) :
Bohl, J., et al. J. Biol. Chem. 282(13):9392-9400(2007)
Dode, L., et al. J. Biol. Chem. 280(47):39124-39134(2005)
Olsen, O., et al. Am. J. Physiol. Renal Physiol. 288 (2), F345-F352 (2005) :
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