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MAB1974

Sigma-Aldrich

Anti-Integrin β3 Antibody, clone BB10

clone BB10, 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 immunoglobulin

antibody product type

primary antibodies

clone

BB10, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

immunocytochemistry: suitable
immunohistochemistry: suitable
western blot: suitable

isotype

IgG1

suitability

not suitable for immunohistochemistry (Paraffin)

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ITGB3(3690)

Specificity

Reacts with the beta-3 subunit of the integrin family, including GPIIIa of platelets. Recognized an extracellular epitope of beta-3.

Immunogen

Partially purified platelet glycoprotein IIb/lIIa complex.

Application

Anti-Integrin β3 Antibody, clone BB10 is an antibody against Integrin β3 for use in WB, IC, IH.
Immunoblotting: 1:1000 (Ylanne et al., 1988, 1990). The antibody is most effective when used against non-reduced samples.

immunohistochemistry (indirect immunofluorescence)1:200 - 1:400. (Ylanne et al., 1988).

Does not work on paraffin embedded sections.

Final working dilutions must be determined by end user.

Physical form

Format: Purified
Purified immunoglobulin. In PBS with 1% BSA and 0.1% sodium azide.

Storage and Stability

Maintain between 2 and 8°C up to 12 months.

Legal Information

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

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Gwendolyn F Elphick et al.
Blood, 113(17), 4078-4085 (2009-02-27)
Integrin-mediated cell migration is central to many biologic and pathologic processes. During inflammation, tissue injury results from excessive infiltration and sequestration of activated leukocytes. Recombinant human activated protein C (rhAPC) has been shown to protect patients with severe sepsis, although
D Seger et al.
The Journal of biological chemistry, 276(20), 16998-17006 (2001-03-30)
Phosphorylation of vitronectin (Vn) by casein kinase II was previously shown to occur at Thr50 and Thr57 and to augment a major physiological function of vitronectin-cell adhesion and spreading. Here we show that this phosphorylation increases cell adhesion via the
M A Scragg et al.
Infection and immunity, 67(4), 1837-1843 (1999-03-20)
Cell surface integrins mediate interactions between cells and their extracellular matrix and are frequently exploited by a range of bacterial pathogens to facilitate adherence and/or invasion. In this study we examined the effects of Porphyromonas gingivalis proteases on human gingival
Franco Klingberg et al.
The Journal of cell biology, 207(2), 283-297 (2014-10-22)
Integrin-mediated force application induces a conformational change in latent TGF-β1 that leads to the release of the active form of the growth factor from the extracellular matrix (ECM). Mechanical activation of TGF-β1 is currently understood as an acute process that
John C Morrison
Transactions of the American Ophthalmological Society, 104, 453-477 (2007-05-02)
To demonstrate that specific distributions of integrin-based focal mechanoreceptors exist in primate optic nerve heads, suitable for translating stress and strain into the cellular responses of glaucomatous optic neuropathy. Normal human (N = 20) and rhesus monkey (N = 14)

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