Lysine Demethylase 6B (KDM6B) Antibody

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260€ (50 µl)

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935106861
info@markelab.com
name
Lysine Demethylase 6B (KDM6B) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx212083
tested applications
ELISA, WB

Description

KDM6B Antibody is a Rabbit Polyclonal against KDM6B.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Primary Antibodies
Immunogen Target
Lysine Demethylase 6B (KDM6B)
Host
Rabbit
Reactivity
Human, Mouse
Recommended Dilution
ELISA: 1/1000 - 1/2000, WB: 1/200 - 1/1000. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Purification
Antigen Affinity Chromatography.
Size 1
50 µl
Size 2
100 µl
Form
Liquid
Tested Applications
ELISA, WB
Buffer
PBS, pH 7.4, containing 0.05% NaN3 and 40% Glycerol.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
O15054
Gene ID
23135
Background
Antibody anti-KDM6B
Status
RUO

Descripción

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Covalent modification of histones plays critical role in regulating chromatin structure and transcription. While most covalent histone modifications are reversible, only recently has it been established that methyl groups are subject to enzymatic removal from histones. A family of novel JmjC domain-containing histone demethylation (JHDM) enzymes have been identified that perform this specific function. Histone demethylation by JHDM proteins requires cofactors Fe (II) and alpha-ketoglutarate. Family members include JHDM1 (demethylating histone 3 at lysine 36), and JHDM2A as well as JMJD2CH3K9 (both of which demethylate histone 3 at lysine 9). Contributions of histone demethylase activity to tumor development, decreases in cell proliferation, and hormone-dependent transcriptional activation have been observed.

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Covalent modification of histones plays critical role in regulating chromatin structure and transcription. While most covalent histone modifications are reversible, only recently has it been established that methyl groups are subject to enzymatic removal from histones. A family of novel JmjC domain-containing histone demethylation (JHDM) enzymes have been identified that perform this specific function. Histone demethylation by JHDM proteins requires cofactors Fe (II) and alpha-ketoglutarate. Family members include JHDM1 (demethylating histone 3 at lysine 36), and JHDM2A as well as JMJD2CH3K9 (both of which demethylate histone 3 at lysine 9). Contributions of histone demethylase activity to tumor development, decreases in cell proliferation, and hormone-dependent transcriptional activation have been observed.

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