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Merck
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主要文件

04-1481

Sigma-Aldrich

Anti-RPA2 p34 Antibody, clone RPA20 1-46

from mouse, clone RPA20, clone 1-46

别名:

RF-A protein 2, RP-A p32, RP-A p34, Replication factor A protein 2, replication protein A2 (32kD), replication protein A2, 32kDa, Replication protein A 32kDa subunit, RF-A, replication factor-A protein 2, p32, p34, RPA2, REPA2, RPA32.

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About This Item

分類程式碼代碼:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物源

mouse

品質等級

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

1-46, monoclonal
RPA20, monoclonal

物種活性

human, mouse

包裝

antibody small pack of 25 μg

技術

western blot: suitable

同型

IgG1κ

NCBI登錄號

UniProt登錄號

運輸包裝

ambient

目標翻譯後修改

unmodified

基因資訊

human ... RPA2(6118)

相关类别

一般說明

RPA is a heterotrimeric protein complex that binds specifically to single-stranded DNA (ssDNA). It is composed of three subunits, RPA1 (70 kDa), RPA2 (32 kDa), and RPA3 (14 kDa), and plays multiple roles in DNA metabolism. RPA is required for DNA replication initiation, as well as replication elongation. At the onset of DNA replication, RPA is loaded onto chromatin after the binding of Cdc45 to origins. RPA is needed for subsequent loading of DNA polymerase and other replication proteins to initiate DNA replication. After DNA replication begins, RPA moves with replication forks, stabilizing ssDNA and assisting in DNA synthesis. In addition to its replication function, RPA is also known to play essential roles in damage repair and recombination.The 32 kDa subunit, is phosphorylated by the cdc2 family of kinases when cells enter S-phase and in response to DNA damage by ATM, ATR, and DNA-PK. Alternate names for RPA32 include replication protein A 32 kDa subunit, RP-A, RF-A, replication factor-A protein 2, p32, p34, RPA2, REPA2, and RPA32.

特異性

This antibody recognizes RPA2.

免疫原

Epitope: Unknown
His-tagged recombinant protein corresponding to human RPA2.

應用

Anti-RPA2 p34 Antibody, clone RPA20 1-46 is a Mouse Monoclonal Antibody for detection of RPA2 p34 also known as Replication factor A protein 2 & has been validated in WB.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Cell Cycle, DNA Replication & Repair

Chromatin Biology
Western Blot (SNAP ID) Analysis: 0.5 µg/mL from a previous lot detected RPA2 on 10 µg of NIH/3T3 cell lysate.

品質

Evaluated by Western Blot in HeLa cell lysate.

Western Blot Analysis: 0.5 µg/mL of this antibody detected RPA2 on 10 µg of HeLa cell lysate.

標靶描述

~32 kDa

外觀

Protein G Purified
Format: Purified
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.

儲存和穩定性

Stable for 1 year at 2-8°C from date of receipt.

分析報告

Control
HeLa cell lysate

其他說明

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

免責聲明

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.

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Jang-Won Ahn et al.
Nucleic acids research, 43(13), 6321-6333 (2015-06-13)
DNA double-strand breaks (DSBs) are the most severe type of DNA damage and are primarily repaired by non-homologous end joining (NHEJ) and homologous recombination (HR) in the G1 and S/G2 phase, respectively. Although CtBP-interacting protein (CtIP) is crucial in DNA
Lauren M Young et al.
Cell reports, 13(3), 451-459 (2015-10-13)
PARP1 is the main sensor of single- and double-strand breaks in DNA and, in building chains of poly(ADP-ribose), promotes the recruitment of many downstream signaling and effector proteins involved in the DNA damage response (DDR). We show a robust physical
Nanda Kumar Sasi et al.
Neoplasia (New York, N.Y.), 20(10), 985-995 (2018-08-30)
CDC7-DBF4 kinase (DDK) initiates DNA replication in eukaryotes by activating the replicative MCM helicase. DDK has diverse and apparently conflicting roles in the replication checkpoint response in various organisms, but the underlying mechanisms are far from settled. We show that

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