Item no. |
PTM-652RM |
Manufacturer |
PTM Biolabs
|
Amount |
100 ul |
Category |
|
Type |
Antibody Monoclonal |
Format |
Lyophilized powder |
Applications |
WB, CHIP |
Clone |
PA-144-12 |
Specific against |
Human (Homo sapiens), Mouse (Murine, Mus musculus), Rat (Rattus norvegicus) |
Host |
Rabbit |
Isotype |
IgG |
Conjugate/Tag |
Unconjugated |
ECLASS 10.1 |
42030590 |
ECLASS 11.0 |
42030590 |
UNSPSC |
12352203 |
Alias |
H3R2me2 (sy) |
Shipping condition |
Room temperature |
Available |
|
Manufacturer - Type |
Primary Antibodies |
Manufacturer - Category |
Histone & Histone Modification Antibodies |
Manufacturer - Targets |
Histone H3 |
Shipping Temperature |
Ambient temperature |
Storage Conditions |
Store at -20°C. Avoid freeze/thaw cycles. |
Molecular Weight |
15 |
Stability |
Stable for 12 months from date of receipt/reconstitution. |
Manufacturer - Research Area |
Epigenetics |
Product description |
The ε-amino lysine acetylation of proteins is an important reversible modification controlling protein activity. The amino-terminal tails of core histones undergo lysine methylation in multiple sites, termed as “histone code” or “epigenetic code”. Lysine methylation in core histones is a major determinant for the formation of active and inactive regions of the genome and therefore plays vital roles in multiple cellular events. In most species, lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing. Methylation in histones modulated by specific histone methyltransferases (HMTs) and histone demethylases (HDMs) is impaired in the pathologies of cancer and other diseases and therefore, enzymes regulating histone lysine methylation have become promising targets for anti-cancer drugs. |
Purification Method |
Protein A purified |
Manufacturer - Specificity |
Anti-Symmetric Dimethyl-Histone H3 (Arg2) Rabbit mAb detects histone H3 only when it is Symmetricated at Arg2. |
Formula |
PBS, Glycerol, BSA |
PTM |
Symmetric Dimethyl |
Modification Site |
Arg2 |
Clonality |
Recombinant Monoclonal |
Background |
The ε-amino lysine acetylation of proteins is an important reversible modification controlling protein activity. The amino-terminal tails of core histones undergo lysine methylation in multiple sites, termed as “histone code” or “epigenetic code”. Lysine methylation in core histones is a major determinant for the formation of active and inactive regions of the genome and therefore plays vital roles in multiple cellular events. In most species, lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing. Methylation in histones modulated by specific histone methylases (HMTs) and histone demethylases (HDMs) is impaired in the pathologies of cancer and other diseases and therefore, enzymes regulating histone lysine methylation have become promising targets for anti-cancer drugs. |
Cellular Localization |
Nucleus |
Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.
All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.