Antibody data
- Antibody Data
- Antigen structure
- References [8]
- Comments [0]
- Validations [0]
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- Product number
- ABIN351093 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN351093, RRID:AB_10804068
- Product name
- anti-Transient Receptor Potential (4th Cytoplasmic Loop) antibody
- Antibody type
- Polyclonal
- Antigen
- 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.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Epitope
- 4th Cytoplasmic Loop
- Vial size
- 150 μL
- 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.
- Handling
- Avoid freeze and thaw cycles.
Submitted references Single amino acid change in the fifth transmembrane segment of the TRP Ca2+ channel causes massive degeneration of photoreceptors.
The genome sequence of Drosophila melanogaster.
TRPgamma, a drosophila TRP-related subunit, forms a regulated cation channel with TRPL.
Reversible phosphorylation of the signal transduction complex in Drosophila photoreceptors.
Coassembly of TRP and TRPL produces a distinct store-operated conductance.
Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex.
TRP, a protein essential for inositide-mediated Ca2+ influx is localized adjacent to the calcium stores in Drosophila photoreceptors.
Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction.
Hong YS, Park S, Geng C, Baek K, Bowman JD, Yoon J, Pak WL
The Journal of biological chemistry 2002 Sep 13;277(37):33884-9
The Journal of biological chemistry 2002 Sep 13;277(37):33884-9
The genome sequence of Drosophila melanogaster.
Adams MD, Celniker SE, Holt RA, Evans CA, Gocayne JD, Amanatides PG, Scherer SE, Li PW, Hoskins RA, Galle RF, George RA, Lewis SE, Richards S, Ashburner M, Henderson SN, Sutton GG, Wortman JR, Yandell MD, Zhang Q, Chen LX, Brandon RC, Rogers YH, Blazej RG, Champe M, Pfeiffer BD, Wan KH, Doyle C, Baxter EG, Helt G, Nelson CR, Gabor GL, Abril JF, Agbayani A, An HJ, Andrews-Pfannkoch C, Baldwin D, Ballew RM, Basu A, Baxendale J, Bayraktaroglu L, Beasley EM, Beeson KY, Benos PV, Berman BP, Bhandari D, Bolshakov S, Borkova D, Botchan MR, Bouck J, Brokstein P, Brottier P, Burtis KC, Busam DA, Butler H, Cadieu E, Center A, Chandra I, Cherry JM, Cawley S, Dahlke C, Davenport LB, Davies P, de Pablos B, Delcher A, Deng Z, Mays AD, Dew I, Dietz SM, Dodson K, Doup LE, Downes M, Dugan-Rocha S, Dunkov BC, Dunn P, Durbin KJ, Evangelista CC, Ferraz C, Ferriera S, Fleischmann W, Fosler C, Gabrielian AE, Garg NS, Gelbart WM, Glasser K, Glodek A, Gong F, Gorrell JH, Gu Z, Guan P, Harris M, Harris NL, Harvey D, Heiman TJ, Hernandez JR, Houck J, Hostin D, Houston KA, Howland TJ, Wei MH, Ibegwam C, Jalali M, Kalush F, Karpen GH, Ke Z, Kennison JA, Ketchum KA, Kimmel BE, Kodira CD, Kraft C, Kravitz S, Kulp D, Lai Z, Lasko P, Lei Y, Levitsky AA, Li J, Li Z, Liang Y, Lin X, Liu X, Mattei B, McIntosh TC, McLeod MP, McPherson D, Merkulov G, Milshina NV, Mobarry C, Morris J, Moshrefi A, Mount SM, Moy M, Murphy B, Murphy L, Muzny DM, Nelson DL, Nelson DR, Nelson KA, Nixon K, Nusskern DR, Pacleb JM, Palazzolo M, Pittman GS, Pan S, Pollard J, Puri V, Reese MG, Reinert K, Remington K, Saunders RD, Scheeler F, Shen H, Shue BC, Sidén-Kiamos I, Simpson M, Skupski MP, Smith T, Spier E, Spradling AC, Stapleton M, Strong R, Sun E, Svirskas R, Tector C, Turner R, Venter E, Wang AH, Wang X, Wang ZY, Wassarman DA, Weinstock GM, Weissenbach J, Williams SM, WoodageT, Worley KC, Wu D, Yang S, Yao QA, Ye J, Yeh RF, Zaveri JS, Zhan M, Zhang G, Zhao Q, Zheng L, Zheng XH, Zhong FN, Zhong W, Zhou X, Zhu S, Zhu X, Smith HO, Gibbs RA, Myers EW, Rubin GM, Venter JC
Science (New York, N.Y.) 2000 Mar 24;287(5461):2185-95
Science (New York, N.Y.) 2000 Mar 24;287(5461):2185-95
TRPgamma, a drosophila TRP-related subunit, forms a regulated cation channel with TRPL.
Xu XZ, Chien F, Butler A, Salkoff L, Montell C
Neuron 2000 Jun;26(3):647-57
Neuron 2000 Jun;26(3):647-57
Reversible phosphorylation of the signal transduction complex in Drosophila photoreceptors.
Liu M, Parker LL, Wadzinski BE, Shieh BH
The Journal of biological chemistry 2000 Apr 21;275(16):12194-9
The Journal of biological chemistry 2000 Apr 21;275(16):12194-9
Coassembly of TRP and TRPL produces a distinct store-operated conductance.
Xu XZ, Li HS, Guggino WB, Montell C
Cell 1997 Jun 27;89(7):1155-64
Cell 1997 Jun 27;89(7):1155-64
Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex.
Chevesich J, Kreuz AJ, Montell C
Neuron 1997 Jan;18(1):95-105
Neuron 1997 Jan;18(1):95-105
TRP, a protein essential for inositide-mediated Ca2+ influx is localized adjacent to the calcium stores in Drosophila photoreceptors.
Pollock JA, Assaf A, Peretz A, Nichols CD, Mojet MH, Hardie RC, Minke B
The Journal of neuroscience : the official journal of the Society for Neuroscience 1995 May;15(5 Pt 2):3747-60
The Journal of neuroscience : the official journal of the Society for Neuroscience 1995 May;15(5 Pt 2):3747-60
Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction.
Montell C, Rubin GM
Neuron 1989 Apr;2(4):1313-23
Neuron 1989 Apr;2(4):1313-23
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