MAB1965
Anti-Integrin β1 Antibody, a.a. 82-87, clone JB1A (a.k.a. J10)
ascites fluid, clone JB1A (J10), Chemicon®
Synonym(s):
CD29
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
100
300
antibody form
ascites fluid
antibody product type
primary antibodies
clone
JB1A (J10), monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
flow cytometry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... ITGB1(3688)
Related Categories
General description
The primary function of the integrin family is to mediate cell-cell and cell-matrix adhesion interaction. CD29 is ubiquitous, with broad tissue distribution, but is not expressed on erythrocytes and is expressed only weakly on granulocytes. Integrins play an important role in cell adhesion and migration, and their normal function is critical in the induction and maintenance of cell differentiation. Loss or downregulation of CD29 has been proposed to be one of the general pathways through which carcinoma cells may acquire a more invasive and differentiated phenotype. Furthermore, loss or downregulation of integrin occurs relatively frequently in poorly differentiated colorectal and breast carcinomas as determined by immunohistochemistry.
Specificity
Reacts with the human integrin beta 1. Note: integrin beta 1 is expressed in all tissues/cell types except erythrocytes. The epitope recognized by JB1a was recently mapped to residues 82-87 of the mature beta 1 integrin chain. In this study Mn++ was found to inhibit binding of JB1a both to mature beta 1 integrin and to a synthetic peptide corresponding to residues 82-87{Ni, 1998}.
Immunogen
Epitope: a.a. 82-87
Purified beta 1 integrin and Jurkat cells
Application
Inhibition of Jurkat binding to collagen and fibronectin:
1:100 Note: epitope is trypsin sensitive; cells should be prepared with PBS + EDTA (2mM) or other non-enzymatic methods. Blocking will not occur with trypsinized cells with JB1A.
Immunoprecipitation: 1:250-500
Western blotting (reducing, 115 kDa; non-reducing, 130 kDa): 1:1000-2000
Note: binding of antibody may be inhibited by magnesium ion concentrations exceeding 0.5mM.
Immunocytochemistry/Immunohistochemistry: JB1A can be used on unfixed cells in flow cytometry and culture {Akimov, 2001; Blood 98(5):1567-1576}. Often times fixing with 2-3% PFA for 5 minutes after primary antibody incubation will assist in obtain strong signals since it fixes the primary antibodies to the tissues.
FACS: JB1A has been primarily used against live cells at 1:200-1:500 followed by goat anti-mouse conjugated secondaries
Optimal working dilutions must be determined by end user.
1:100 Note: epitope is trypsin sensitive; cells should be prepared with PBS + EDTA (2mM) or other non-enzymatic methods. Blocking will not occur with trypsinized cells with JB1A.
Immunoprecipitation: 1:250-500
Western blotting (reducing, 115 kDa; non-reducing, 130 kDa): 1:1000-2000
Note: binding of antibody may be inhibited by magnesium ion concentrations exceeding 0.5mM.
Immunocytochemistry/Immunohistochemistry: JB1A can be used on unfixed cells in flow cytometry and culture {Akimov, 2001; Blood 98(5):1567-1576}. Often times fixing with 2-3% PFA for 5 minutes after primary antibody incubation will assist in obtain strong signals since it fixes the primary antibodies to the tissues.
FACS: JB1A has been primarily used against live cells at 1:200-1:500 followed by goat anti-mouse conjugated secondaries
Optimal working dilutions must be determined by end user.
Research Category
Cell Structure
Cell Structure
Research Sub Category
Integrins
Integrins
This Anti-Integrin β1 Antibody, a.a. 82-87, clone JB1A (a.k.a. J10) is validated for use in FC, IH, IP, FUNC, WB for the detection of Integrin β1.
Target description
88 kDa
Physical form
Ascites fluid containing no preservatives.
Unpurified
Storage and Stability
Maintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Analysis Note
Control
Human lung, liver, and skeletal muscle tissues
Human lung, liver, and skeletal muscle tissues
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.
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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
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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The Glycoprotein B Disintegrin-like Domain Binds Beta 1 Integrin to Mediate Cytomegalovirus Entry.
Feire AL, Roy RM, Manley K, Compton T
Journal of virology null
B lymphocyte fibronectin receptors: expression and utilization.
Stupack, D G, et al.
Scandinavian Journal of Immunology, 34, 761-769 (1991)
Spatial expressions of fibronectin and integrins by human and rodent dermal fibroblasts.
M Yasuda, Y Miyachi, O Ishikawa, K Takahashi
British Journal of Dermatology null
Juliette Ezpeleta et al.
Scientific reports, 7(1), 7671-7671 (2017-08-11)
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N-Glycosylation of integrin alpha5beta1 plays a crucial role in cell spreading, cell migration, ligand binding, and dimer formation, but the detailed mechanisms by which N-glycosylation mediates these functions remain unclear. In a previous study, we showed that three potential N-glycosylation
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