Tyrosinase-Related Protein 1 (TYRP1) (4th Cytoplasmic Loop) antibody

Details for Product No. ABIN351093
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Antigen
Synonyms hm:zeh0659, tyrp1, zgc:100893, TYRP1, TRP1, tyrp-1, Trrp1, CAS2, CATB, GP75, OCA3, TRP, TYRP, b-PROTEIN, TRP-1, Tyrp, b, brown, isa, B
Epitope
4th Cytoplasmic Loop
(7), (3), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1)
Reactivity
Fruit Fly (Drosophila melanogaster)
(46), (16), (14), (14), (5), (3), (2), (2), (2), (1)
Host
Rabbit
(41), (16)
Clonality
Polyclonal
Conjugate
Un-conjugated
(2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (IHC), Western Blotting (WB)
(41), (15), (10), (9), (6), (5), (3), (2), (2), (2), (2)
Pubmed 8 references available
Quantity 500 µg
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Catalog No. ABIN351093
454.67 $
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Immunogen A synthetic peptide from 4th cytoplasmic loop of drosophila TRP (Transient receptor potential protein) conjugated to an immunogenic carrier protein was used as the antigen.
Isotype IgG
Specificity Specific for TRP.
Alternative Name TRP
Background Function: A light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. Ca(2+) influx may then feed back and inhibit PLC, thereby facilitating phosphatidylinositol 4,5 bisphosphate (PIP2) recycling. Trp and trpl act together in the light response, though it is unclear whether as heteromultimers or as distinct units, and are activated by fatty acids and metabolic stress. Also required forolfactory adaptation and may be involved inolfactory system development.
Subunit: The C-terminus interacts with a PDZ domain of inaD to form the core of the inaD signaling complex. Other members of the complex include norpA (PLC), inaC (PKC), and possibly trpl, ninaC, FKBP59, calmodulin and rhodopsin. Forms homomultimers and heteromultimers with trpl. Interaction with trpl is mediated in part by the N-terminal region and thetransmembrane domains. Also interacts, though to a lower extent, with trp-gamma.
Subcellular location: Membrane, Multi-pass membrane protein. Note: Localized on plasma membrane loops found at the base of the rhabdomere, in close proximity to the calcium stores.
Tissue specificity: Expressed predominantly in the rhabdomeres of photoreceptor cells. Expressed in the third antennal segment and in theolfactory segment at approximately 70 hours after puparium formation during antennal development. Also known as: Transient receptor potential cation channel protein.
Application Notes A concentration of 10-50 µg/ml is recommended.
The optimal concentration should be determined by the end user.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment 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.
Expiry Date 12 months
General Montell, Rubin: "Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction." in: Neuron, Vol. 2, Issue 4, pp. 1313-23, 1990 (PubMed).

Pollock, Assaf, Peretz et al.: "TRP, a protein essential for inositide-mediated Ca2+ influx is localized adjacent to the calcium stores in Drosophila photoreceptors." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 15, Issue 5 Pt 2, pp. 3747-60, 1995 (PubMed).

Chevesich, Kreuz, Montell: "Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex." in: Neuron, Vol. 18, Issue 1, pp. 95-105, 1997 (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).

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).

Liu, Parker, Wadzinski et al.: "Reversible phosphorylation of the signal transduction complex in Drosophila photoreceptors." in: The Journal of biological chemistry, Vol. 275, Issue 16, pp. 12194-9, 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).

Hong, Park, Geng et al.: "Single amino acid change in the fifth transmembrane segment of the TRP Ca2+ channel causes massive degeneration of photoreceptors." in: The Journal of biological chemistry, Vol. 277, Issue 37, pp. 33884-9, 2002 (PubMed).

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