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Merck
CN

SAB4300133

Anti-phospho-STAT1 (pSer727) antibody produced in rabbit

affinity isolated antibody

别名:

Anti-DKFZp686B04100 antibody produced in rabbit, Anti-ISGF-3 antibody produced in rabbit, Anti-STAT91 antibody produced in rabbit, Anti-signal transducer and activator of transcription 1, 91kDa antibody produced in rabbit

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, IHC (p), WB
Citations:
3
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biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~91 kDa

species reactivity

human, mouse

concentration

1 mg/mL

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50-1:100, indirect immunofluorescence: 1:100-1:200, western blot: 1:500-1:1000

isotype

IgG

immunogen sequence

(P-M-SP-P-E)

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pSer727)

Quality Level

Gene Information

human ... STAT1(6772)

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General description

Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

Immunogen

Peptide sequence around phosphorylation site of serine 727 (P-M-S(p)-P-E), according to the protein STAT1.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

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.

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存储类别

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
低风险生物材料
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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Song Qin et al.
Oncology letters, 15(2), 1630-1638 (2018-02-13)
In cancer immunotherapy, dendritic cell (DC)-based vaccines represent a promising, yet challenging, treatment method. In addition to overcoming the low expression levels of antigenic epitopes on cancer cells, it is also necessary to overcome the inhibitory effect of suppressor of
Xiaoliang Zhang et al.
Journal of cellular physiology, 234(5), 6917-6926 (2018-11-28)
Imbalance of M1/M2 macrophages phenotype activation is a key point in diabetic nephropathy (DN). This study aimed to investigate whether active vitamin D (VD) suppresses macrophage transition to the M1 phenotype via inhibiting the high glucose-induced STAT-1 phosphorylation to reduce
Xiaoliang Zhang et al.
Journal of cellular physiology, 234(5), 6917-6926 (2018-11-28)
Imbalance of M1/M2 macrophages phenotype activation is a key point in diabetic nephropathy (DN). This study aimed to investigate whether active vitamin D (VD) suppresses macrophage transition to the M1 phenotype via inhibiting the high glucose-induced STAT-1 phosphorylation to reduce

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