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

Details for Product anti-TYRP1 Antibody No. ABIN351091, Fournisseur: Connectez-vous pour afficher
Antigène
  • 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
  • tyrosinase-related protein 1b
  • tyrosinase-related protein 1
  • transient receptor potential cation channel, subfamily C, member 1
  • tyrosinase-related protein 1a
  • tyrp1b
  • TYRP1
  • tyrp1
  • LOC100136490
  • tyrp-1
  • LOC100218715
  • LOC100342170
  • Trpc1
  • Tyrp1
  • tyrp1a
Épitope
4th Cytoplasmic Loop
14
12
7
5
4
4
3
3
3
3
3
2
2
2
2
2
2
1
1
1
Reactivité
Mouche des fruits (Drosophila melanogaster)
189
118
12
11
9
7
7
6
6
6
5
4
4
4
4
3
3
1
Hôte
Lapin
101
100
1
Clonalité
Polyclonal
Conjugué
Cet anticorp Tyrosinase-Related Protein 1 est non-conjugé
10
8
8
6
5
5
4
4
4
4
4
4
4
4
4
4
2
2
2
2
1
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (IHC), Western Blotting (WB)
104
100
94
72
70
59
51
19
13
8
8
Options
Fournisseur
Connectez-vous pour afficher
Supplier Product No.
Connectez-vous pour afficher
Immunogène A synthetic peptide from 4th cytoplasmic loop of drosophila TRP (Transient receptor potential protein) conjugated to an immunogenic carrier protein was used as the immunogen.
Isotype IgG
Specificité Specific for TRP.
Autre désignation TRP (TYRP1 Antibody Extrait)
Sujet 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.
Indications d'application 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.
Conseil sur la manipulation Avoid freeze and thaw cycles.
Stock 4 °C/-20 °C
Stockage commentaire 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.
Date de péremption 12 months
Background publications Hong, Park, Geng, Baek, Bowman, Yoon, Pak: "Single amino acid change in the fifth transmembrane segment of the TRP Ca2+ channel causes massive degeneration of photoreceptors." dans: The Journal of biological chemistry, Vol. 277, Issue 37, pp. 33884-9, 2002 (PubMed).

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

Liu, Parker, Wadzinski, Shieh: "Reversible phosphorylation of the signal transduction complex in Drosophila photoreceptors." dans: The Journal of biological chemistry, Vol. 275, Issue 16, pp. 12194-9, 2000 (PubMed).

Adams, Celniker, Holt, Evans, Gocayne, Amanatides, Scherer, Li, Hoskins, Galle, George, Lewis, Richards, Ashburner, Henderson, Sutton, Wortman, Yandell, Zhang, Chen, Brandon, Rogers, Blazej, Champe, Pfeiffer, Wan, Doyle, Baxter, Helt, Nelson, Gabor, Abril: "The genome sequence of Drosophila melanogaster." dans: Science (New York, N.Y.), Vol. 287, Issue 5461, pp. 2185-95, 2000 (PubMed).

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

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

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

Montell, Rubin: "Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction." dans: Neuron, Vol. 2, Issue 4, pp. 1313-23, 1990 (PubMed).

Avez-vous cherché autre chose?