MAB2075Z
Anti-Integrin β6 Antibody, clone R6G9, azide free
clone R6G9, Chemicon®, from mouse
Synonym(s):
MAB2075
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
R6G9, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
flow cytometry: suitable
immunoprecipitation (IP): suitable
isotype
IgG2a
suitability
not suitable for Western blot
not suitable for activity/function inhibition
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... ITGB6(3694)
Specificity
Monoclonal antibody MAB2075Z, raised by immunizing Balb/c mice with murine NIH 3T3 cells stably transfected with the human beta6 subunit, recognizes the human beta6 subunit by flow cytometry and is an excellent antibody for immunoprecipitation.
Immunogen
Murine NIH 3T3 cells stably transfected with the human (6 subunit
Application
Anti-Integrin β6 Antibody, clone R6G9, azide free is an antibody against Integrin β6 for use in FC & IP.
Flow cytometry
Immunoprecipitation: Effective; however because this antibody is an IgG2a, protein G or rabbit anti-mouse IgG is helpful for capture.
Immunohistochemistry/immunocytochemistry: The antibody recognizes alphaVbeta6 by immunohistochemistry and immunocytochemistry (acetone fix), but nuclear background staining limits usefulness in these techniques.
Then antibody is not function blocking and not effective for western blot.
Optimal working dilutions must be determined by end user.
Immunoprecipitation: Effective; however because this antibody is an IgG2a, protein G or rabbit anti-mouse IgG is helpful for capture.
Immunohistochemistry/immunocytochemistry: The antibody recognizes alphaVbeta6 by immunohistochemistry and immunocytochemistry (acetone fix), but nuclear background staining limits usefulness in these techniques.
Then antibody is not function blocking and not effective for western blot.
Optimal working dilutions must be determined by end user.
Physical form
Format: Purified
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
12 - Non Combustible Liquids
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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Yasuyuki Taooka et al.
Respiration; international review of thoracic diseases, 86(5), 367-375 (2012-12-22)
Repeated aspiration pneumonia is a serious problem in the elderly. In aspiration pneumonia, neutrophils play an important role in acute lung injury, while CD18-independent neutrophil transmigration pathways have also been reported in acid-aspiration pneumonia animal models. However, the involvement of
Alison Burman et al.
Journal of virology, 80(19), 9798-9810 (2006-09-16)
Foot-and-mouth disease virus (FMDV) can use a number of integrins as receptors to initiate infection. Attachment to the integrin is mediated by a highly conserved arginine-glycine-aspartic acid (RGD) tripeptide located on the GH loop of VP1. Other residues of this
Liudmila S Chesnokova et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(48), 20464-20469 (2009-11-19)
Epstein-Barr virus (EBV) is a ubiquitous human herpesvirus that is causally implicated in the development of lymphoid and epithelial tumors. Entry of virus requires fusion of virus envelopes and cell membranes. Fusion with B lymphocytes requires virus glycoprotein gB and
John J Grzesiak et al.
International journal of cancer, 129(12), 2905-2915 (2011-04-15)
To address the role of β(1) integrins in pancreatic cancer progression, we stably knocked down β(1) integrin subunit expression in human FG-RFP pancreatic cancer cells using lentiviral-based RNA interference. We then examined the effects of β(1) integrin
Terry Jackson et al.
Journal of virology, 78(9), 4533-4540 (2004-04-14)
Field isolates of foot-and-mouth disease virus (FMDV) have been shown to use three alphav integrins, alphavbeta1, alphavbeta3, and alphavbeta6, as cellular receptors. Binding to the integrin is mediated by a highly conserved RGD motif located on a surface-exposed loop of
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