产品名称
Anti-phospho-Glycogen Synthase Kinase 3α/β (pTyr279/216) antibody produced in rabbit, affinity isolated antibody, aqueous glycerol solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
aqueous glycerol solution
mol wt
antigen 47-51 kDa
species reactivity
human, mouse, rat
technique(s)
dot blot: suitable
indirect ELISA: suitable
western blot: 1:1000 using MCF-7 cell extract
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
phosphorylation (pTyr279/pTyr216)
Quality Level
Gene Information
human ... GSK3A(2931)
mouse ... Gsk3a(606496)
rat ... Gsk3a(50686)
Application
Anti-phospho-Glycogen Synthase Kinase 3α/β (p(Tyr279/216)) antibody is suitable for use in indirect ELISA, dot blot and western blot (1:1000 using MCF-7 cell extract).
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
GSK-3 functions a serine-threonine kinase and modulates a wide range of cellular activities such as cell signaling, cell cycle, cell growth and differentiation. Mammalian GSK-3 has two isoforms, namely, GSK-3α and GSK-3 β. GSK-3α has been implicated in Alzheimer′s disease, whereas both, GSK-3α and GSK-3β have been implicated in leukemia . Anti-phospho-Glycogen Synthase Kinase 3α/β (p(Tyr279/216)) antibody is specific for phosphorylated forms of GSK-3α (51 kDa) and GSK-3β (47 kDa) that contain a phosphate moiety on tyrosine 279 and 216 respectively. The antibody does not bind to non-tyrosine phosphorylated GSK-3α/β protein. The product recognizes human, mouse and rat GSK-3α/β.
Immunogen
synthetic phosphopeptide derived from the regions of GSK-3α/β that contain tyrosine279/216.
Physical form
Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, with 50% glycerol, 1.0 mg/ml BSA (IgG and protease free), and 0.05% sodium azide.
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存储类别
10 - Combustible liquids
wgk
WGK 3
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
Emma Y Song et al.
Experimental hematology, 38(10), 908-921 (2010-06-15)
The objective of this study was to investigate the effect of small molecule inhibitors of glycogen synthase kinase-3β (GSK-3β) on leukemia cell growth and survival. Analysis of cytotoxicity and cell proliferation was conducted using the MTS assay, cell-cycle analysis, and
Bradley W Doble et al.
Developmental cell, 12(6), 957-971 (2007-06-05)
In mammalian cells, glycogen synthase kinase-3 (GSK-3) exists as two homologs, GSK-3alpha and GSK-3beta, encoded by independent genes, which share similar kinase domains but differ substantially in their termini. Here, we describe the generation of an allelic series of mouse
Christopher J Phiel et al.
Nature, 423(6938), 435-439 (2003-05-23)
Alzheimer's disease is associated with increased production and aggregation of amyloid-beta (Abeta) peptides. Abeta peptides are derived from the amyloid precursor protein (APP) by sequential proteolysis, catalysed by the aspartyl protease BACE, followed by presenilin-dependent gamma-secretase cleavage. Presenilin interacts with
Versha Banerji et al.
The Journal of clinical investigation, 122(3), 935-947 (2012-02-14)
Acute myeloid leukemia (AML) is the most common form of acute leukemia in adults. Long-term survival of patients with AML has changed little over the past decade, necessitating the identification and validation of new AML targets. Integration of genomic approaches
Kashif Aziz Khan et al.
Molecular and cellular biology, 35(17), 3029-3043 (2015-06-24)
Induction of an antiviral innate immune response relies on pattern recognition receptors, including retinoic acid-inducible gene 1-like receptors (RLR), to detect invading pathogens, resulting in the activation of multiple latent transcription factors, including interferon regulatory factor 3 (IRF3). Upon sensing
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