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Przeciwciało anty-fosfo-histonowe H2A.X (Ser139), klon JBW301, koniugat biotyny

clone JBW301, Upstate®, from mouse

Synonim(y):

H2AXS139P, histon H2A.X (fosfo S139), rodzina histonów H2A, członek X, histon H2AX

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Gabaryty przesyłkiSKUDostępnośćCena netto
100 μg

Przewidywany termin wysyłki24 marca 2026zKuehne + Nagel Sp. z o.o.

2960,00 zł

Informacje o tej pozycji

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
biotin conjugate
Clone:
JBW301, monoclonal
Application:
ICC, WB
Citations:
43

2960,00 zł


Przewidywany termin wysyłki24 marca 2026Szczegóły


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biological source

mouse

Quality Level

conjugate

biotin conjugate

antibody form

purified antibody

antibody product type

primary antibodies

clone

JBW301, monoclonal

species reactivity

human

manufacturer/tradename

Upstate®

technique(s)

immunocytochemistry: suitable, western blot: suitable

isotype

IgG1

General description

15 kDa
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures.

Immunogen

Epitope: Ser139
KLH-conjugated, synthetic peptide (CKATQA[pS]QEY) corresponding to amino acids 134-142 of human histone H2A.X. The immunizing sequence has 8 identical amino acids in yeast and mouse.

Application

Anti-phospho-Histone H2A.X (Ser139) Antibody, clone JBW301, biotin conjugate is a Mouse Monoclonal Antibody for detection of phospho-Histone H2A.X (Ser139) also known as H2AXS139P, H2AX histone & has been validated in ICC & WB.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones

Biochem/physiol Actions

A broad species cross-reactivity is expected based on conservation of sequence homology.
Recognizes Histone H2A.X phosphorylated at Ser139, Mr 15kDa.

Physical form

Protein G Purified
Purified biotin conjugated mouse monoclonal IgG1 in buffer containing 70% storage buffer (0.02 M Phosphate buffer, pH7.6, 0.25 M NaCl, 0.1% sodium azide) and 30% glycerol

Preparation Note

Stable for 1 year at -20ºC from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerolcontaining solutions to become frozen during storage.

Analysis Note

Control
Staurosporine-treated Jurkat cell lysates.
Routinely evaluated in acid extracted histone from Jurkat cell lysates treated with 0.5mM staurosporine (19-123).

Western Blot Analysis:
0.5-1 μg/mL of this lot detected phosphorylated histone H2A.X (Ser139) in acid extracted histone from Jurkat cell lysates treated with 0.5μM staurosporine (Catalog # 19-123).

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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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Klasa składowania

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Lars H Jensen et al.
BMC pharmacology, 4, 31-31 (2004-12-04)
Bisdioxopiperazine anti-cancer agents are inhibitors of eukaryotic DNA topoisomerase II, sequestering this protein as a non-covalent protein clamp on DNA. It has been suggested that such complexes on DNA represents a novel form of DNA damage to cells. In this
Jeffrey M Cloutier et al.
PLoS genetics, 11(10), e1005462-e1005462 (2015-10-29)
Chromosome abnormalities are common in the human population, causing germ cell loss at meiotic prophase I and infertility. The mechanisms driving this loss are unknown, but persistent meiotic DNA damage and asynapsis may be triggers. Here we investigate the contribution
Sascha Schäuble et al.
PloS one, 7(8), e42150-e42150 (2012-08-11)
Primary human fibroblasts in tissue culture undergo a limited number of cell divisions before entering a non-replicative "senescent" state. At early population doublings (PD), fibroblasts are proliferation-competent displaying exponential growth. During further cell passaging, an increasing number of cells become
Fabienne Cocchiarella et al.
Molecular therapy. Methods & clinical development, 3, 16038-16038 (2016-08-31)
The Sleeping Beauty (SB) transposase and, in particular, its hyperactive variant SB100X raises increasing interest for gene therapy application, including genome modification and, more recently, induced pluripotent stem cells (iPS) reprogramming. The documented cytotoxicity of the transposase, when constitutively expressed
Tristan Winters et al.
The EMBO journal, 33(11), 1256-1270 (2014-05-07)
The cohesin complex is essential for mitosis and meiosis. The specific meiotic roles of individual cohesin proteins are incompletely understood. We report in vivo functions of the only meiosis-specific STAG component of cohesin, STAG3. Newly generated STAG3-deficient mice of both

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