产品名称
Anti-Integrin β3 Antibody, clone PM6/13, clone PM6/13, Chemicon®, from mouse
biological source
mouse
antibody form
purified immunoglobulin
clone
PM6/13, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
flow cytometry: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... ITGB3(3690)
Application
FACS: As a marker for megakaryoblastic/cytic leukaemias and idiopathic thrombocythemia
Optimal working dilutions must be determined by the end user.
Optimal working dilutions must be determined by the end user.
Research Category
Cell Structure
Cell Structure
Research Sub Category
Integrins
Integrins
This Anti-Integrin β3 Antibody, clone PM6/13 is validated for use in FC, IP, WB, IH, IH(P) for the detection of Integrin β3.
Biochem/physiol Actions
The antibody is specific for the 110 kDa platelet glycoprotein GP IIIa and inhibits platelet aggregation and activation induced by thrombin and collagen. The platelet glycoprotein is the integrin beta3 chain of the vitronectin receptor and GPIIb/IIIa. The antigen is present on platelets and megakaryocytes.
Antigen distribution:
Platelets >98%
Megakaryocytes >98%
Granulocytes 0%
Monocytes 0%
LGL cells 0%
B cells 0%
T cells 0%
Peripheral blood lymphocytes 0%
FUSION PARTNER: SP2/0 myeloma cell line
Antigen distribution:
Platelets >98%
Megakaryocytes >98%
Granulocytes 0%
Monocytes 0%
LGL cells 0%
B cells 0%
T cells 0%
Peripheral blood lymphocytes 0%
FUSION PARTNER: SP2/0 myeloma cell line
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.
Immunogen
Human platelet plasma membrane
Other Notes
Replaces: MAB1381
Physical form
Format: Purified
The monoclonal is presented at a concentration of 100μg/1ml in phosphate buffered saline containing 10mM sodium azide and 1mg/ml bovine serum albumin. We recommend that each laboratory determine an optimum working titre for use in its particular application.
Preparation Note
For use within 1 month of purchase store at +4°C, for long term storage aliquot antibody into small volumes and store at -20°C.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
D Boettiger et al.
Molecular biology of the cell, 12(5), 1227-1237 (2001-05-22)
Integrin receptors serve as mechanical links between the cell and its structural environment. Using alpha(v)beta3 integrin expressed in K562 cells as a model system, the process by which the mechanical connection between alpha(v)beta3 and vitronectin develops was analyzed by measuring
Pharmacology of the novel antiangiogenic peptide ATN-161 (Ac-PHSCN-NH2): observation of a U-shaped dose-response curve in several preclinical models of angiogenesis and tumor growth.
Do?ate, F; Parry, GC; Shaked, Y; Hensley, H; Guan, X; Beck, I; Tel-Tsur, Z; Plunkett et al.
Clinical cancer research : an official journal of the American Association for Cancer Research null
Vineet Gupta et al.
Journal of immunology (Baltimore, Md. : 1950), 180(3), 1713-1718 (2008-01-23)
Formation of the integrin alphabeta heterodimer is essential for cell surface expression and function. At the core of the alphabeta interface is a conserved Arg/Lys "finger" from the beta-subunit that inserts into a cup-like "cage" formed of two layers of
Loss of dipeptidyl peptidase IV immunostaining discriminates malignant melanomas from deep penetrating nevi.
Roesch, A; Wittschier, S; Becker, B; Landthaler, M; Vogt, T
Modern Pathology null
Nikos E Tsopanoglou et al.
American journal of physiology. Cell physiology, 283(5), C1501-C1510 (2002-10-10)
Thrombin has been reported to be a potent angiogenic factor both in vitro and in vivo, and many of the cellular effects of thrombin may contribute to activation of angiogenesis. In this report we show that thrombin-treatment of human endothelial
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