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AB198676

Recombinant Human Histone H1 protein

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(7 Publications)

Recombinant Human Histone H1 protein is a Human Full Length protein, in the 2 to 194 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

H1F0, H1FV, H1-0, Histone H1.0, Histone H1', Histone H1(0)

1 Images
SDS-PAGE - Recombinant Human Histone H1 protein (AB198676)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Histone H1 protein (AB198676)

4-20% SDS-PAGE analysis of ab198676 (2 μg) with Coomassie staining.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P07305

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 79% PBS, 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Useful as a substrate for histone methyltransferase and acetyltransferase assays. Ideal for screening small molecular inhibitors of histone modifying enzymes for drug discovery and HTS applications.

Sequence info

[{"sequence":"MHHHHHHTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATPKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK","proteinLength":"Full Length","predictedMolecularWeight":"22 kDa","actualMolecularWeight":null,"aminoAcidEnd":194,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P07305","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

Function

Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division.

Sequence similarities

Belongs to the histone H1/H5 family.

Post-translational modifications

Phosphorylated on Ser-17 in RNA edited version.. ADP-ribosylated on Ser-104 in response to DNA damage.

Subcellular localisation

Nucleus

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division.
See full target information H1-0

Publications (7)

Recent publications for all applications. Explore the full list and refine your search

Acta pharmaceutica Sinica. B 15:1608-1625 PubMed40370560

2025

CDK5-triggered G6PD phosphorylation at threonine 91 facilitating redox homeostasis reveals a vulnerability in breast cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Yuncheng Bei,Sijie Wang,Rui Wang,Owais Ahmad,Meng Jia,Pengju Yao,Jianguo Ji,Pingping Shen

Life science alliance 5: PubMed35173014

2022

Quantitative profiling of adaptation to cyclin E overproduction.

Applications

Unspecified application

Species

Unspecified reactive species

Juanita C Limas,Amiee N Littlejohn,Amy M House,Katarzyna M Kedziora,Brandon L Mouery,Boyang Ma,Dalia Fleifel,Andrea Walens,Maria M Aleman,Daniel Dominguez,Jeanette Gowen Cook

Molecular cell 82:106-122.e9 PubMed34875212

2021

SUMOylation of linker histone H1 drives chromatin condensation and restriction of embryonic cell fate identity.

Applications

Unspecified application

Species

Unspecified reactive species

Daoud Sheban,Tom Shani,Roey Maor,Alejandro Aguilera-Castrejon,Nofar Mor,Bernardo Oldak,Merav D Shmueli,Avital Eisenberg-Lerner,Jonathan Bayerl,Jakob Hebert,Sergey Viukov,Guoyun Chen,Assaf Kacen,Vladislav Krupalnik,Valeriya Chugaeva,Shadi Tarazi,Alejandra Rodríguez-delaRosa,Mirie Zerbib,Adi Ulman,Solaiman Masarwi,Meital Kupervaser,Yishai Levin,Efrat Shema,Yael David,Noa Novershtern,Jacob H Hanna,Yifat Merbl

Nucleic acids research 49:2450-2459 PubMed33733652

2021

Reversible chromatin condensation by the DNA repair and demethylation factor thymine DNA glycosylase.

Applications

Unspecified application

Species

Unspecified reactive species

Charles E Deckard,Jonathan T Sczepanski

Cell reports 29:1469-1481.e9 PubMed31693889

2019

NFE2L3 Controls Colon Cancer Cell Growth through Regulation of DUX4, a CDK1 Inhibitor.

Applications

Unspecified application

Species

Unspecified reactive species

Marina Bury,Benjamin Le Calvé,Frédéric Lessard,Thomas Dal Maso,James Saliba,Carine Michiels,Gerardo Ferbeyre,Volker Blank

Nucleic acids research 47:7418-7429 PubMed31127309

2019

Restriction of AID activity and somatic hypermutation by PARP-1.

Applications

Unspecified application

Species

Unspecified reactive species

Sandra Tepper,Oliver Mortusewicz,Ewelina Członka,Amanda Bello,Angelika Schmidt,Julia Jeschke,Arthur Fischbach,Ines Pfeil,Svend K Petersen-Mahrt,Aswin Mangerich,Thomas Helleday,Heinrich Leonhardt,Berit Jungnickel

Nature communications 9:1876 PubMed29760377

2018

Cyclin K regulates prereplicative complex assembly to promote mammalian cell proliferation.

Applications

Unspecified application

Species

Unspecified reactive species

Tingjun Lei,Peixuan Zhang,Xudong Zhang,Xue Xiao,Jingli Zhang,Tong Qiu,Qian Dai,Yujun Zhang,Ling Min,Qian Li,Rutie Yin,Ping Ding,Ni Li,Yi Qu,Dezhi Mu,Jun Qin,Xiaofeng Zhu,Zhi-Xiong Xiao,Qintong Li
View all publications

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