|The Trpv3 trpv3 (Catalog #MBS800330) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The TrpV3 Antibody: ATTO 594 reacts with Human, Mouse, Rat and may cross-react with other species as described in the data sheet. MyBioSource\'s TrpV3 can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), Immunocytochemistry (ICC), Immunoprecipitation (IP), Immunoflurorescence (IF).
1-10ug/mL (WB), 0.1-1.0ug/mL (Perox) (IHC/ICC), 1.0-10ug/mL (IF). Researchers should empirically determine the suitability of the Trpv3 trpv3 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The Trpv3 trpv3 product has the following accession number(s) (GI #429535830) (NCBI Accession #NP_001020928) (Uniprot Accession #Q4QYD9). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
To buy or view more detailed product information and pricing, please click on the technical datasheet page below:
Please refer to the product datasheet for known applications of a given antibody. We\'ve tested the TrpV3 Antibody: ATTO 594 with the following immunoassay(s):
Testing Data (Western blot analysis of TrpV3 in a human cell line mix using a 1:1000 dilution.)
Testing Data #2 (IF analysis of TrpV3 in human hippocampal tissues.)
Background Info: Detects ~70kDa
Scientific Background: Ion channels are integral membrane proteins that help establish and control the small voltage gradient across the plasma membrane of living cells by allowing the flow of ions down their electrochemical gradient (1). They are present in the membranes that surround all biological cells because their main function is to regulate the flow of ions across this membrane. Whereas some ion channels permit the passage of ions based on charge, others conduct based on an ionic species, such as sodium or potassium. Furthermore, in some ion channels, the passage is governed by a gate which is controlled by chemical or electrical signals, temperature, or mechanical forces. There are a few main classifications of gated ion channels. There are voltage- gated ion channels, ligand-gated, other gating systems and finally those that are classified differently, having more exotic characteristics. The first are voltage- gated ion channels which open and close in response to membrane potential. These are then separated into sodium, calcium, potassium, proton, transient receptor, and cyclic nucleotide-gated channels; each of which is responsible for an unique role. Ligand-gated ion channels are also known as ionotropic receptors, and they open in response to specific ligand molecules binding to the extracellular domain of the receptor protein. The other gated classifications include activation and inactivation by second messengers, inward-rectifier potassium channels, calcium-activated potassium channels, two-pore-domain potassium channels, light-gated channels, mechano-sensitive ion channels and cyclic nucleotide-gated channels. Finally, the other classifications are based on less normal characteristics such as two-pore channels, and transient receptor potential channels (2). The TRPV3 protein belongs to a family of nonselective cation channels that function in a variety of processes, including temperature sensation and vasoregulation. The thermosensitive members of this family are expressed in subsets of sensory neurons that terminate in the skin, and are activated at distinct physiological temperatures. This channel is activated at temperatures between 22 and 40 degrees C. The gene lies in close proximity to another family member (TRPV1) gene on chromosome 17, and the two encoded proteins are thought to associate with each other to form heteromeric channels (3, 4).