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Key Documents

SAB4504196

Sigma-Aldrich

Anti-phospho-Histone H1 (pThr17) antibody produced in rabbit

affinity isolated antibody

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 22 kDa

species reactivity

human, mouse, rat

concentration

~1 mg/mL

technique(s)

ELISA: 1:1000
immunofluorescence: 1:100-1:500
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

NCBI accession no.

P10412
P16401
P16402

UniProt accession no.

P16402

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pThr17)

Gene Information

human ... HIST1H1B(3009) , HIST1H1D(3007) , HIST1H1E(3008)

Immunogen

The antiserum was produced against synthesized peptide derived from human Histone H1 around the phosphorylation site of Thr17.

Immunogen Range: 1-50

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

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
110948

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Tingting Zhou et al.
Journal of cellular physiology (2019-02-17)
The p75 neurotrophin receptor (p75NTR), a member of tumor necrosis factor receptor superfamily, involves in neuronal apoptosis after intracerebral hemorrhage (ICH). It has been previously demonstrated that phosphorylation of p35 is a crucial factor for fighting against the proapoptotic p25/CDK5
Juhyung Lee et al.
Scientific reports, 8(1), 13676-13676 (2018-09-14)
Cyclin-dependent kinase 5 (CDK5) plays a pivotal role in neural development and neurodegeneration. CDK5 activity can be regulated by posttranslational modifications, including phosphorylation and S-nitrosylation. In this study, we demonstrate a novel mechanism by which the acetylation of CDK5 at

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