Skip to Content
Merck
All Photos(1)

Key Documents

PLA0310

Sigma-Aldrich

Rabbit anti-Phospho RPA32 (S33) Antibody, Affinity Purified

Synonym(s):

32kDa, REPA2, RF-A protein 2, RP-A p32, RP-A p34, RPA32, replication factor A protein 2, replication protein A 34 kDa subunit, replication protein A2, replication protein A2 (32kD)

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

100

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

species reactivity

human

technique(s)

western blot: 1:1,000-1:5,000

accession no.

NP_002937.1

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

phosphorylation (pSer33)

Gene Information

human ... RPA2(6118)

General description

Replication protein A2 (RPA2) is a 32kDa protein and one of the subunits of replication protein A complex. The gene encoding it is localized on human chromosome 1p35.

Immunogen

Immunogen was a phosphorylated synthetic peptide, which represented a portion of human replication protein A2, 32 kDa surrounding phosphorylated serine that corresponded to position 33 using the numbering given in entry NP_002937.1 (GeneID 6118).

Biochem/physiol Actions

Replication protein A2 (RPA2) is involved in DNA repair and replication. The protein has been shown to be phosphorylated as a response to DNA damage and apoptosis in vitro.

Physical form

Tris-citrate/phosphate buffer, pH 7 to 8 containing 0.09% Sodium Azide

Other Notes

Replication protein A (RPA) is a multisubunit complex that carries out DNA mismatch repair (MMR) in association with MSH2 (a subunit of human MutS heterodimers), MLH1 (a subunit of human MutL heterodimers), PCNA, and DNA polymerase-delta. RPA is composed of a heterotrimer that includes subunits of 70 kDa (RPA1), 32kDa (RPA2), and 14kDa (RPA3). RPA2, the 32kDa 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.

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
3

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Identification of proteins that may directly interact with human RPA.
Nakaya R, et al.
Journal of Biochemistry, 148(5), 539-547 (2010)
Loss of heterozygosity at chromosome 1p in different solid human tumours: association with survival.
Ragnarsson G
British Journal of Cancer, 79(9-10), 1468-1474 (1999)
Proteomic analysis of BRCA1-depleted cell line reveals a putative role for replication protein A2 up-regulation in BRCA1 breast tumor development.
Bouley J
Proteomics. Clinical Applications, 4(5), 489-498 (2010)
Phosphorylation of replication protein A middle subunit (RPA32) leads to a disassembly of the RPA heterotrimer.
Treuner K
The Journal of Biological Chemistry, 274(22), 15556-15561 (1999)
Holger Stephan et al.
Nucleic acids research, 37(18), 6028-6041 (2009-08-13)
The human single-stranded DNA-binding protein, replication protein A (RPA), is regulated by the N-terminal phosphorylation of its 32-kDa subunit, RPA2. RPA2 is hyperphosphorylated in response to various DNA-damaging agents and also phosphorylated in a cell-cycle-dependent manner during S- and M-phase

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service