Transient Receptor Potential Cation Channel, Subfamily M, Member 5 (TRPM5) (1st Extracellular Loop) antibody

Details for Product No. ABIN351207
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Antigen
Synonyms LTRPC5, MTR1, 9430099A16Rik, LTrpC-5, Ltrpc5, Mtr1
Epitope
1st Extracellular Loop
(6), (4), (1), (1), (1)
Reactivity
Human
(25), (20), (18), (12), (3), (2)
Host
Rabbit
(26), (4)
Clonality
Polyclonal
Conjugate
Un-conjugated
(1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (IHC), Western Blotting (WB)
(21), (10), (9), (5), (5)
Pubmed 4 references available
Quantity 100 μL
Options
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Catalog No. ABIN351207
454.67 $
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Immunogen A synthetic peptide from the 1t extracellular loop of human TRPM5 (LTRPC5, MTR1, Long transient receptor potential channel 5) conjugated to an immunogenic carrier protein was used as the antigen.
Specificity Specific for TRPM5.
Purification Whole serum
Alternative Name TRPM5
Background Function: Voltage-modulated Ca(2+)-activated, monovalent cation channel (VCAM) that mediates a transient membrane depolarization and plays a central role in taste transduction. Monovalent-specific, non-selective cation channel that mediates the transport of Na(+), K(+) and Cs(+) ions equally well. Activated directly by increases in intracellular Ca(2+), but is impermeable to it. Gating is voltage-dependent and displays rapid activation and deactivation kinetics upon channel stimulation even during sustained elevations in Ca(2+). Also activated by a fast intracellular Ca(2+) increase in response to inositol 1,4,5-triphosphate-producing receptor agonists. The channel is blocked by extracellular acidification. External acidification has 2 effects, a fast reversible block of the current and a slower irreversible enhancement of current inactivation. Is a highly temperature-sensitive, heat activated channel showing a steep increase of inward currents at temperatures between 15 and 35 degrees Celsius. Heat activation is due to a shift of the voltage-dependent activation curve to negative potentials. Activated by arachidonic acid in vitro. May be involved in perception of bitter, sweet and umami tastes. May also be involved in sensing semiochemicals.
Subcellular location: Cell membrane, Multi-pass membrane protein.
Tissue specificity: Strongly expressed in fetal brain, liver and kidney, and in adult prostate, testis, ovary, colon and peripheral blood leukocytes. Also expressed in a large proportion of Wilms' tumors and rhabdomyosarcomas. In monochromosomal cell lines shows exclusive paternal expression. Also known as: LTRPC5, MLSN1- and TRP-related gene 1 protein, TRPM5, LTRPC5, MTR1, Transient receptor potential cation channel subfamily M member 5.
Research Area Neurology
Application Notes A dilution of 1 : 300 to 1 : 2000 is recommended.
The optimal dilution should be determined by the end user.
Not yet tested in other applications.
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 Prawitt, Enklaar, Klemm et al.: "Identification and characterization of MTR1, a novel gene with homology to melastatin (MLSN1) and the trp gene family located in the BWS-WT2 critical region on chromosome 11p15.5 and showing allele-specific expression." in: Human molecular genetics, Vol. 9, Issue 2, pp. 203-16, 2000 (PubMed).

Prawitt, Monteilh-Zoller, Brixel et al.: "TRPM5 is a transient Ca2+-activated cation channel responding to rapid changes in [Ca2+]i." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, Issue 25, pp. 15166-71, 2003 (PubMed).

Taylor, Noguchi, Totoki et al.: "Human chromosome 11 DNA sequence and analysis including novel gene identification." in: Nature, Vol. 440, Issue 7083, pp. 497-500, 2006 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).

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