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MAB1957

Sigma-Aldrich

Anti-Integrin β3 Antibody, clone 25E11

clone 25E11, Chemicon®, from mouse

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Synonym(s):
CD61
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

25E11, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

flow cytometry: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable

isotype

IgM

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ITGB3(3690)

Related Categories

Specificity

Reacts with human integrin beta3 (GPIIIa, vitronectin receptor beta chain). The protein detectable is a complex of CD41 and CD61. The apparent molecular weight of the GPIIIa by SDS-PAGE is 105 kDa reduced and 90 kDa unreduced. Ligands are fibronectin, fibrinogen, von Willebrand factor, vitronectin and thrombospondin. Residues 237-248 of GPIIIa or CD61 are critical in adhesive protein binding. The monocytoid cell line U937 is highly positive.

(original paper claimed IgG2ak)

Immunogen

Normal blood mononuclear cells activated by mixed lymphocyte reaction and cultured for 10 days in medium containing IL-2.

Application

Immunoprecipitation

Immunocytochemistry (acetone fixation required)

Flow cytometry

Inhibits platelet aggregation, 10 μg/mL

Optimal working dilutions must be determined by end user.
Research Category
Cell Structure
Research Sub Category
Integrins
This Anti-Integrin β3 Antibody, clone 25E11 is validated for use in FC, IP, IC, FUNC for the detection of Integrin β3.

Linkage

Replaces: 04-1060

Physical form

Format: Purified
In buffer of 0.02M phosphate, 0.25M sodium chloride, pH 7.6, 0.1% sodium azide.

Storage and Stability

Maintain between 2 and 8°C.

Other Notes

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

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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.

WGK

WGK 2

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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Francisco M Vega et al.
Open biology, 2(5), 120076-120076 (2012-06-23)
The Rho GTPase RhoB has been shown to affect cell migration, but how it does this is not clear. Here we show that cells depleted of RhoB by RNAi are rounded and have defects in Rac-mediated spreading and lamellipodium extension
Cyp1b1 mediates periostin regulation of trabecular meshwork development by suppression of oxidative stress.
Zhao, Y; Wang, S; Sorenson, CM; Teixeira, L; Dubielzig, RR; Peters, DM; Conway et al.
Molecular and cellular biology null
Diane Palmieri et al.
The Journal of biological chemistry, 277(43), 40950-40957 (2002-08-15)
Plasminogen activator inhibitor-1 (PAI-1), an inhibitor of urokinase plasminogen activator, is paradoxically associated with a poor prognosis in breast cancer. PAI-1 is linked to several processes in the metastatic cascade. However, the role of PAI-1 in metastatic processes, which may
S S Akimov et al.
The Journal of cell biology, 148(4), 825-838 (2000-02-23)
The protein cross-linking enzyme tissue transglutaminase binds in vitro with high affinity to fibronectin via its 42-kD gelatin-binding domain. Here we report that cell surface transglutaminase mediates adhesion and spreading of cells on the 42-kD fibronectin fragment, which lacks integrin-binding
Platelet matrix metalloprotease-1 mediates thrombogenesis by activating PAR1 at a cryptic ligand site.
Trivedi, V; Boire, A; Tchernychev, B; Kaneider, NC; Leger, AJ; O'Callaghan, K; Covic et al.
Cell null

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