Trp-Like (TRPL) (4th Cytoplasmic Loop) antibody

Antigen: Trp-Like (TRPL)

Binding Site: 4th Cytoplasmic Loop

Clonality: Polyclonal

Host: Rabbit

Reactivity: Fruit Fly (Drosophila melanogaster)

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN351177

Additional Information

Alternative name: TRPL (Transient receptor potential like protein)

UniProt: P48994

Immunogen: A synthetic peptide from 4th cytoplasmic loop of drosophila TRPL (Transient receptor potential like protein) conjugated to an immunogenic carrier protein was used as the immunogen.

Format: Lyophilized

Isotype: IgG

Description: FUNCTION: A light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. Required for vision in the dark and in dim light. Binds calmodulin. Trp and trpl act together in the light response, although it is unclear whether as heteromultimers or distinct units. Also forms a functional cation channel with trp-gamma. Activated by fatty acids, metabolic stress, inositols and GTP-binding proteins. SUBUNIT: Forms heteromultimers with trp-gamma and, to a lower extent, with trp. Interacts with FKBP59 in vivo and is found in the inaD signaling complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Note: In the dark, there is 20 fold more rhabdomeral trpl protein forming plasma membrane channels than in the light. In the light, the protein translocates to an intracellular compartment. Protein levels remain unchanged in light and dark conditions. Also known as: Transient receptor potential like protein, Transient-receptor-potential-like protein.

Specificity: Appears to be specific for TRPL.

Application Details

Application Notes: IHC, WB. A concentration of 10-50 µg/ml is recommended. The optimal concentration should be determined by the end user.

Purity: IgG

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Restrictions: For Research Use only

Publications

Phillips, Bull, Kelly: "Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene." in: Neuron, Vol. 8, Issue 4, pp. 631-42, 1992 (PubMed).

Xu, Li, Guggino et al.: "Coassembly of TRP and TRPL produces a distinct store-operated conductance." in: Cell, Vol. 89, Issue 7, pp. 1155-64, 1997 (PubMed).

Lan, Brereton, Barritt: "The role of calmodulin-binding sites in the regulation of the Drosophila TRPL cation channel expressed in Xenopus laevis oocytes by ca2+, inositol 1,4,5-trisphosphate and GTP-binding proteins." in: The Biochemical journal, Vol. 330 ( Pt 3), pp. 1149-58, 1998 (PubMed).

Chyb, Raghu, Hardie: "Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL." in: Nature, Vol. 397, Issue 6716, pp. 255-9, 1999 (PubMed).

Adams, Celniker, Holt et al.: "The genome sequence of Drosophila melanogaster." in: Science (New York, N.Y.), Vol. 287, Issue 5461, pp. 2185-95, 2000 (PubMed).

Xu, Chien, Butler et al.: "TRPgamma, a drosophila TRP-related subunit, forms a regulated cation channel with TRPL." in: Neuron, Vol. 26, Issue 3, pp. 647-57, 2000 (PubMed).

Baehner, Frechter, Da Silva et al.: "Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current." in: Neuron, Vol. 34, Issue 1, pp. 83-93, 2002 (PubMed).