製品名
Anti-phospho-SRPK2 (Ser494) Antibody, from rabbit, purified by affinity chromatography
biological source
rabbit
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human, mouse
species reactivity (predicted by homology)
Xenopus (based on 100% sequence homology), rat (based on 100% sequence homology)
technique(s)
inhibition assay: suitable (peptide)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
phosphorylation (pSer494)
Quality Level
Gene Information
human ... SRPK2(6733)
Analysis Note
Control
Untreated and insulin treated HepG2 cell lysate
Untreated and insulin treated HepG2 cell lysate
Evaluated by Western Blot in untreated and insulin treated HepG2 cell lysate.
Western Blot Analysis: 1 µg/mL of this antibody detected SRPK2 in 10 µg HepG2 cell lysate.
Western Blot Analysis: 1 µg/mL of this antibody detected SRPK2 in 10 µg HepG2 cell lysate.
Application
Anti-phospho-SRPK2 (Ser494) Antibody is an antibody against phospho-SRPK2 (Ser494) for use in WB, PIA.
Peptide Inhibition Analysis: 1 µg/mL from a representative lot detected SRPK2 in 10 µg of insulin treated HepG2 cell lysate.
Research Category
Signaling
Signaling
Research Sub Category
Cell Cycle, DNA Replication & Repair
Cell Cycle, DNA Replication & Repair
Biochem/physiol Actions
This antibody is specific for the protein kinase domain of SRPK2 phosphorylated at Ser494, independent of observed phosphorylation at Ser497.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Along with Serine/threonine protein kinase 2 (SRPK2), SRPK1 phosphorylates serine residues found in RS-domain-containing proteins, such as SFRS1 and SFRS2. These kinases also phosphorylate the same serine residues on the HBV core protein both in vitro and in vivo. The cytoplasmic proteins are critical for nuclear import of SR proteins in a phosphorylation-dependent manner. Additionally, they mediate the trafficking of splicing factors and play a role in spliceosome assembly and mitogenesis.
~120 kDa observed. Two isoforms at ~77 kDa and ~79 kDa may be observed in some cell lysates.
Immunogen
Epitope: Protein kinase domain
KLH-conjugated linear peptide corresponding to the protein kinase domain of SRPK2 phosphorylated at Ser494.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Physical form
Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Preparation Note
Stable for 1 year at 2-8°C from date of receipt.
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保管分類
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
試験成績書(COA)
製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
Mousumi Khatun et al.
Hepatology (Baltimore, Md.), 74(1), 41-54 (2020-11-26)
HCV often causes chronic infection in liver, cirrhosis, and, in some instances, HCC. HCV encodes several factors' those impair host genes for establishment of chronic infection. The long noncoding RNAs (lncRNAs) display diverse effects on biological regulations. However, their role
Aneesha Radhakrishnan et al.
Cancer biology & therapy, 17(2), 219-229 (2016-02-09)
Signaling plays an important role in regulating all cellular pathways. Altered signaling is one of the hallmarks of cancers. Phosphoproteomics enables interrogation of kinase mediated signaling pathways in biological systems. In cancers, this approach can be utilized to identify aberrantly
グローバルトレードアイテム番号
| カタログ番号 | GTIN |
|---|---|
| 07-1817 | 04053252437175 |
ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.
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