|The Trpm7 trpm7 (Catalog #MBS804607) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The TrpM7 Antibody: ATTO 390 reacts with Human, Mouse, Rat and may cross-react with other species as described in the data sheet. MyBioSource\'s TrpM7 can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), Immunoprecipitation (IP), Immunocytochemistry (ICC), Immunofluorescence (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 Trpm7 trpm7 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 Trpm7 trpm7 product has the following accession number(s) (GI #256773287) (NCBI Accession #NP_001157797.1) (Uniprot Accession #Q923J1). 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 TrpM7 Antibody: ATTO 390 with the following immunoassay(s):
Testing Data (Western blot analysis of TrpM7 tested in a human cell line mix at 1:1000 dilution.)
Testing Data #2 (IHC analysis of TrpM7 in human hippocampal tissues.)
Testing Data #3 (IHC analysis of TrpM7 tested on mouse brain using a dilution Strong positivity of the nuclear membrane of every cell.)
Background Info: Detects ~220kDa. No cross-reactivity against TrpM6
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). TRPs, mammalian homologs of the Drosophila transient receptor potential (trp) protein, are ion channels that are thought to mediate capacitative calcium entry into the cell. TRP-PLIK is a protein that is both an ion channel and a kinase. As a channel, it conducts calcium and monovalent cations to depolarize cells and increase intracellular calcium. As a kinase, it is capable of phosphorylating itself and other substrates. The kinase activity is necessary for channel function, as shown by its dependence on intracellular ATP and by the kinase mutants (3, 4).