NA26
Anti-MSH2 (Ab-1) Mouse mAb (GB12)
liquid, clone GB12, Calbiochem®
Synonym(s):
Anti-Mismatch Repair Protein 2
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
GB12, monoclonal
form
liquid
contains
≤0.1% sodium azide as preservative
species reactivity
human
should not react with
mouse
manufacturer/tradename
Calbiochem®
storage condition
do not freeze
isotype
IgG1
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
Gene Information
human ... MSH2(4436)
General description
Purified mouse monoclonal antibody generated by immunizing BALB/c mice with the specified immunogen and fusing splenocytes with SP20 mouse myeloma cells. Recognizes the ~100 kDa MSH2 protein.
Recognizes the ~100 kDa MSH2 protein in HCT116 and SW480 cells and colon tissue.
This Anti-MSH2 (Ab-1) Mouse mAb (GB12) is validated for use in Frozen Sections, Immunoblotting, Immunoprecipitation, Paraffin Sections for the detection of MSH2 (Ab-1).
Immunogen
Human
an N-terminal fragment of human MSH2
Application
Frozen Sections (5 µg/ml)
Immunoblotting (1 µg/ml)
Immunoprecipitation (1 µg/reaction)
Paraffin Sections (3 µg/ml, heat pre-treatment required)
Immunoblotting (1 µg/ml)
Immunoprecipitation (1 µg/reaction)
Paraffin Sections (3 µg/ml, heat pre-treatment required)
Packaging
Please refer to vial label for lot-specific concentration.
Warning
Toxicity: Standard Handling (A)
Physical form
In 50 mM sodium phosphate buffer, 0.2% gelatin, pH 7.5.
Analysis Note
Negative Control
LoVo cells
LoVo cells
Positive Control
HCT116 or SW480 cells or colon tissue
HCT116 or SW480 cells or colon tissue
Other Notes
Bronner, C. E., et al. 1994. Nature368, 258.
Papadopoulos, N., et al. 1994. Science263, 1625.
Peltomäki, P. T. 1994. Annals of Medicine26, 215.
Fishel, R., et al. 1993. Cell75, 1027-1038, 1993.
Leach, F. S., et al. 1993. Cell75, 1215.
Lindbolm, A., et al. 1993. Nature Genetics5, 279.
Papadopoulos, N., et al. 1994. Science263, 1625.
Peltomäki, P. T. 1994. Annals of Medicine26, 215.
Fishel, R., et al. 1993. Cell75, 1027-1038, 1993.
Leach, F. S., et al. 1993. Cell75, 1215.
Lindbolm, A., et al. 1993. Nature Genetics5, 279.
For paraffin sections, pre-treat with heat for 20 min. Antibody should be titrated for optimal results in individual systems.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Leah C Young et al.
The American journal of pathology, 179(1), 411-421 (2011-06-28)
The fusion tyrosine kinase NPM-ALK is central to the pathogenesis of ALK-positive anaplastic large cell lymphoma (ALK(+)ALCL). We recently identified that MSH2, a key DNA mismatch repair (MMR) protein integral to the suppression of tumorigenesis, is an NPM-ALK-interacting protein. In
Myrella Vlenterie et al.
Oncotarget, 6(33), 34680-34690 (2015-09-29)
Over 95% of all synovial sarcomas (SS) share a unique translocation, t(X;18), however, they show heterogeneous clinical behavior. We analyzed multiple SS to reveal additional genetic alterations besides the translocation. Twenty-six SS from 22 patients were sequenced for 409 cancer-related
Laure Droy-Dupré et al.
United European gastroenterology journal, 2(4), 307-314 (2014-08-02)
Villous tumours of the rectosigmoid are historically defined as broad-based lesions associated with secretory diarrhoea. This study aimed to perform a reappraisal of these tumours, on the basis of newly introduced histological, immunohistochemical and molecular parameters. For this study, 22
M B Weiss et al.
Cancer gene therapy, 14(1), 98-104 (2006-11-04)
The use of gene therapy to correct mutated or lost gene function for the treatment of human cancers has been an active, yet problematic area of biomedical research. Many technical difficulties, including efficient tissue-specific delivery, integration site specificity and general
MutSβ abundance and Msh3 ATP hydrolysis activity are important drivers of CTG•CAG repeat expansions.
Norma Keogh et al.
Nucleic acids research, 45(17), 10068-10078 (2017-10-04)
CTG•CAG repeat expansions cause at least twelve inherited neurological diseases. Expansions require the presence, not the absence, of the mismatch repair protein MutSβ (Msh2-Msh3 heterodimer). To evaluate properties of MutSβ that drive expansions, previous studies have tested under-expression, ATPase function
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