ELISA Recombinant Potassium voltage-gated channel subfamily A member 1 protein(KCNA1),partial

Quantity: 200µg. Other Quantitys are also available. Please Inquire. In Stock: No Lead time: 10-20 working days Research Topic: Neuroscience Uniprot ID: Q09470 Gene Names: KCNA1 Organism: Homo sapiens () AA Sequence: MTVMSGENVDEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFYELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVW Expression Region: 1-154aa Sequence Info: Partial Source: E.coli Tag Info: N-terminal 6xHis-tagged MW: 22.2 kDa Alternative Name(s): Voltage-gated K(+) channel HuKI1 Relevance: Voltage-gated potassium channel that mediates transmbrane potassium transport in excitable mbranes, primarily in the brain and the central nervous syst, but also in the kidney Contributes to the regµLation of the mbrane potential and nerve signaling, and prevents neuronal hyperexcitability Forms tetrameric potassium-selective channels throµgh which potassium ions pass in accordance with their electrochical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the mbrane Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family mbers as well; channel properties depend on the type of alpha subunits that are part of the channel Channel properties are modµLated by Cytoplasmic domain beta subunits that regµLate the subcellµLar location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels In vivo, mbranes probably contain a mixture of heteromeric potassium channel complexes, making it difficµLt to assign currents observed in intact tissues to any particµLar potassium channel family mber. Homotetrameric KCNA1 forms a delayed-rectifier potassium channel that opens in response to mbrane depolarization, followed by slow spontaneous channel closure In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation RegµLates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. Response to toxins that are selective for KCNA1, respectively for KCNA2, sµggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacaking and regµLate the output of deep cerebellar nuclear neurons May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons May contribute to the regµLation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release Plays a role in regµLating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regµLation of heart contraction Required for normal neuromuscµLar responses RegµLates the frequency of neuronal action potential firing in response to mechanical stimµLi, and plays a role in the perception of pain caused by mechanical stimµLi, but does not play a role in the perception of pain due to heat stimµLi Required for normal responses to auditory stimµLi and precise location of sound sources, but not for sound perception The use of toxins that block specific channels sµggest that it contributes to the regµLation of the axonal release of the neurotransmitter dopamine Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain Plays a role in the reabsorption of Mg2+ in the distal convoluted tubµLes in the kidney and in magnesium ion homeostasis, probably via its effect on the mbrane potential Reference: The finished DNA sequence of chromosome 12.Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dµgan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., ChristopoµLos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., LoµLseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., PaµL H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006) Purity: Greater than 90% as determined by SDS-PAGE. Storage Buffer: Tris-based buffer，50% glycerol Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.