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Key Documents

Safety Information

FCABS325PE

Sigma-Aldrich

Milli-Mark® Anti-acetyl-Histone H3-PE Antibody

Milli-Mark®, from rabbit

Synonym(s):

H3t, H3/t, H3/g, Histone H3.1t

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

100

conjugate

PE

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity

Tetrahymena sp., human, mouse

manufacturer/tradename

Milli-Mark®

technique(s)

flow cytometry: suitable

isotype

IgG

NCBI accession no.

NP_003484

UniProt accession no.

Q16695

shipped in

wet ice

target post-translational modification

acetylation (Lys9,Lys14)

Gene Information

human ... H3F3B(3021)

Related Categories

General description

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the ′beads on a string′ structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Acetylation of histone H3 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs). Acetylation of lysine14 is commonly seen in genes that are being actively transcribed into RNA.

Specificity

Antibody recognizes Tetrahymena acetyl Histone H3
This sequence is highly conserved and predicted to have broad species crossreactivity.

Immunogen

KLH-conjugated peptide corresponding to amino acids 1-20 of Tetrahymena histone H3 (ARTKQTAR[K*]STGG[K*]APRKQLC) where K* is acetylated

Application

This Milli-Mark Anti-acetyl-Histone H3-PE Antibody is validated for use in FC for the detection of acetyl-Histone H3.

Quality

Evaluated by flow cytometry using HeLa cells

Target description

15.5 kDa Calculated

Physical form

Purified rabbit polyclonal IgG conjugated to PE in PBS with 0.1% sodium azide and 15 mg/mL BSA

Legal Information

MILLI-MARK is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

FCABS325PE:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Archin, NM; Bateson, R; Tripathy, MK; Crooks, AM; Yang, KH; Dahl, NP; Kearney et al.
The Journal of Infectious Diseases null
Adam M Spivak et al.
Retrovirology, 13(1), 88-88 (2016-12-22)
Despite the durable viral suppression afforded by antiretroviral therapy, HIV-1 eradication will require strategies to target latently infected cells that persist in infected individuals. Protein kinase C (PKC) activation is a promising strategy to reactivate latent proviruses and allow for
Addie May I Nesbitt et al.
PloS one, 9(5), e94224-e94224 (2014-05-03)
Genetic, pharmacological, and environmental interventions that alter total levels of histone acetylation in specific brain regions can modulate behaviors and treatment responses. Efforts have been made to identify specific genes that are affected by alterations in total histone acetylation and
Valeria Barili et al.
Nature communications, 11(1), 604-604 (2020-02-01)
Hepatitis C virus infection (HCV) represents a unique model to characterize, from early to late stages of infection, the T cell differentiation process leading to exhaustion of human CD8+ T cells. Here we show that in early HCV infection, exhaustion-committed

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