Anti-SK2 potassium channel Antibody 75-403 from Antibodies Inc.

Product Specs
ItemAnti-SK2 potassium channel Antibody
CompanyAntibodies Inc.
Price Pricing Info Supplier Page View Company Product Page
Catalog Number75-403
Antibody TypePrimary Antibody
ClonalityMonoclonal
ReactivityHuman, Mouse, and Rat
Regulatory StatusThese antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans
FormatLiquid, Purified by Protein A chromatography
ApplicationsIHC, ICC, WB
CloneK78/29
Gene NameKcnn2
HostMouse
Quantity100 µL
Molecular Weight50-80 kDa (and larger due to isoforms and dimerization/aggregation)
TargetSK2 potassium channel
IsotypeIgG1
Conjugate/TagUnconjugated
Brand/TrademarkNeuroMab
ImmunogenSynthetic peptide amino acids 546-562 (ENYDKHVTYNAERSRSS, cytoplasmic C-terminus) of rat SK2 (accession number P70604)
ValidationEach new lot of antibody is quality control tested by IHC on either rat or mouse brain and confirmed to give the expected staining pattern
NCBI Gene AliasesKCa2.2, SK2, SKCa 2, SKCa2

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Antibodies Inc.

P.O. Box 1560

Davis, CA 95617-1560

United States

Phone: (800) 824-8540

Email: orders@antibodiesinc.com

Company Profile

Website: https://www.antibodiesinc.com/

(1) The role of cap-dependent translation in aged-related changes in neuroimmunity and affective behaviorsNeurobiology of AgingFebruary 1, 2021Prapti H. Mody, Natalia Lucia Lucia dos Santos, Melissa E. Lenert, Luz R. Barron, Bethany A. Nottingham, Michael D. BurtonIL-1β (1:1000 Abcam ab9722), phosphorylated eIF4E (1:1000 Abcam ab76256), SK2 (1:500 Antibodies Inc. 75-403), CaMKIIα (1:1000 Sigma-Aldrich, 05-532 ), NR2B (1:1000 Sigma-Aldrich, 06-600), and β-actin (1:3000

(2) Computational Analysis of Thermal Adaptation in Extremophilic Chitinases: The Achilles’ Heel in Protein Structure and Industrial UtilizationMoleculesJanuary 29, 2021Dale L. Ang, Mubasher Zahir Hoque, Md. Abir Hossain, Gea Guerriero, Roberto Berni, Jean-Francois Hausman, Saleem A Bokhari, Wallace J. Bridge, Khawar Sohail Siddiqui[CrossRef] [PubMed] Siddiqui, K.S.; Cavicchioli, R. Cold-Adapted Enzymes. Annu. Rev. Biochem. 2006, 75, 403–433. [CrossRef] [PubMed] Protein Adaptation in Extremophiles; Siddiqui, K.S.; Thomas, T. (Eds.) Nova

(3) Temperature acclimation and adaptation of enzyme physiology in Neurospora discretaFungal EcologyOctober 1, 2018Steven D. Allison, Adriana L. Romero-Olivares, Lucy Lu, John W. Taylor, Kathleen K. Treseder5490–5504. Siddiqui, K.S. & Cavicchioli, R., 2006. Cold-Adapted Enzymes. Annual Review of Biochemistry, 75, 403–433. Snider, M.J., Gaunitz, S., Ridgway, C., Short, S.A. & Wolfenden, R., 2000. Temperature effects on

(4) Temperature sensitivities of extracellular enzyme V max and K m across thermal environmentsGlobal Change BiologyJuly 1, 2018Steven D. Allison, Adriana L. Romero‐Olivares, Ying Lu, John W. Taylor, Kathleen K. Treseder3578–3586. 535 536 537 538 539 540 Siddiqui KS, Cavicchioli R (2006) Cold-Adapted Enzymes. Annual Review of Biochemistry, 75, 403–433. Sinsabaugh RL (1994) Enzymic analysis of microbial pattern and process. Biology and Fertility of

(5) A comparative study of cold- and warm-adapted Endonucleases A using sequence analyses and molecular dynamics simulationsPLOS ONEFebruary 13, 2017Davide Michetti, Bjørn Olav Brandsdal, Davide Bon, Geir Villy Isaksen, Matteo Tiberti, Elena Papaleo10.1016/j. biotechadv.2015.11.001 PMID: 26585268 5. Siddiqui KS, Cavicchioli R. Cold-Adapted Enzymes. Annu Rev Biochem. 2006; 75:403–33. doi: 10. 1146/annurev.biochem.75.103004.142723 PMID: 16756497 6. Struvay C, Feller G. Optimization

(6) Assessing the Ecophysiology of Methanogens in the Context of Recent Astrobiological and Planetological StudiesLife (Basel)December 3, 2015Ruth-Sophie Taubner, Christa Schleper, Maria G. Firneis, Simon K.-M. R. Rittmann2012, 55, 415–421. Siddiqui, K.S.; Cavicchioli, R. Cold-Adapted Enzymes. Annu. Rev. Biochem. 2006, 75, 403–433. Feller, G.; Gerday, C. Psychrophilic enzymes: Hot topics in cold adaptation. Nat. Rev. Microbiol.

(7) Optimization of Medium for Protease Production by Enterobacteriaceae sp. PAMC 25617 by Response Surface MethodologyKorean Chemical Engineering ResearchAugust 1, 2015Hyun-do Kim, Chul-Won Yun, Jong-il Choi, Se Jong Han285-290(2001). 19. Siddiqui, K. S. and Cavicchioli, R., “Cold-adapted Enzymes,” Annual Rev. Biochem., 75, 403-433(2006). 20. Kackar, R. N., “Off-line Quality Control, Parameter Design, and the Taguchi Method,”

(8) Cloning and characterization of a psychrophilic catalase gene from an antarctic bacteriumAfrican Journal of Microbiology ResearchSeptember 30, 2011Wang Wei, Wang Fang, Ji Xiaofeng, Liu Shanhong, Yuan Cui, Sun Midoi:10.1101/pdb.prot3487. Siddiqui KS, Cavicchioli R (2006). Cold-Adapted Enzymes. Annu. Rev. Biochem., 75: 403–433. Villegas A, Kropinski AM (2008). An analysis of initiation codon utilization in the Domain Bacteria

(9) A Flow Cytometry–Based Screening System for Directed Evolution of ProteasesJ Biomol ScreenMarch 1, 2011Ran Tu, Ronny Martinez, Radivoje Prodanovic, Mathias Klein, Ulrich Schwanebergwww.slas.org 293 Tu et al. 3. Siddiqui, K. S.; Cavicchioli, R. Cold-Adapted Enzymes. Annu. Rev. Biochem. 2006, 75, 403–433. 4. Haki, G. D.; Rakshit, S. K. Developments in Industrially Important Thermostable Enzymes: A Review.

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Anti-SK2 potassium channel Antibody from Antibodies Inc.

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Anti-SK2 potassium channel Antibody from Antibodies Inc.

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