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Merck
CN

C265

Monoclonal Anti-CaM Kinase IIα (CaMKIIα) antibody produced in mouse

clone 6G9, purified immunoglobulin, buffered aqueous solution

别名:

Anti-CAMKA, Anti-CaMKIINalpha, Anti-CaMKIIalpha, Anti-MRD53, Anti-MRT63

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.44
MDL number:
Conjugate:
unconjugated
Clone:
6G9, monoclonal
Application:
indirect immunofluorescence
western blot
Species reactivity:
rat, mouse
Citations:
19
Technique(s):
indirect immunofluorescence: suitable using rat hippocampus
western blot: 0.5-1.0 μg/mL
Uniprot accession no.:
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产品名称

Monoclonal Anti-CaM Kinase IIα (CaMKIIα) antibody produced in mouse, clone 6G9, purified immunoglobulin, buffered aqueous solution

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

6G9, monoclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

rat, mouse

technique(s)

indirect immunofluorescence: suitable using rat hippocampus
western blot: 0.5-1.0 μg/mL

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

rat ... Camk2a(25400)

Application

Monoclonal Anti-CaM Kinase IIα (CaMKIIα) antibody produced in mouse has been used in immunohistochemistry and western blotting.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

CaM Kinase II α is a Ca2+/calmodulin-dependent kinase that belongs to the serine/threonine protein kinases family. It facilitates the regulation of NMDAR-dependent AMPA receptor trafficking to the synapses. Mouse anti-CaM kinase II α antibody reacts specifically with phosphorylated and non-phosphorylated forms of native and recombinant CaM (Ca2+/calmodulin-dependent) kinase II α subunit in rats. The product has shown no reactivity for phosphorylated or non-phosphorylated β subunit (60kD).

Immunogen

partially purified rat CaM kinase II.

Physical form

Solution in phosphate buffered saline containing 0.05% sodium azide

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存储类别

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Ke-Hui Hu et al.
Behavioural brain research, 359, 81-88 (2018-10-27)
Ischemic stroke is a major cause of disability and mortality worldwide, while no unequivocally efficacious drug is currently available to treat post-stroke functional impairments. Animal and clinical investigations suggest that the motor cortex stimulation constitutes a particularly promising approach for
Metabotropic signal transduction for bradykinin in submucosal neurons of guinea pig small intestine
Hu HZ, et al.
Journal of Pharmacology and Experimental Therapeutics, 309(1), 310-319 (2004)
Wen Fong Ooi et al.
PLoS genetics, 9(9), e1003795-e1003795 (2013-09-27)
Burkholderia pseudomallei (Bp), the causative agent of the often-deadly infectious disease melioidosis, contains one of the largest prokaryotic genomes sequenced to date, at 7.2 Mb with two large circular chromosomes (1 and 2). To comprehensively delineate the Bp transcriptome, we
Jay F Muller et al.
The Journal of comparative neurology, 519(4), 790-805 (2011-01-20)
The basolateral nucleus of the amygdala receives an extremely dense cholinergic innervation from the basal forebrain that is critical for memory consolidation. Although previous electron microscopic studies determined some of the postsynaptic targets of cholinergic afferents, the majority of postsynaptic
Muna L Hilal et al.
Cerebral cortex (New York, N.Y. : 1991), 27(12), 5635-5651 (2017-10-03)
Planar cell polarity (PCP) signaling is well known to play a critical role during prenatal brain development; whether it plays specific roles at postnatal stages remains rather unknown. Here, we investigated the role of a key PCP-associated gene scrib in

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