alpha4 integrin. The alpha4beta1 integrin receptor recognizes an RGD-independent alternative adhesion site in the CS-1 region of fibronectin.
Application
Immunofluorescence and immunoprecipitation.
Inhibits attachment of hematopoeitic cells and T-lymphocytes but not fibroblasts to fibronectin; typical titer is >1:1,000
Aggregation of Jurkat cells to 1:1600 dilution
Research Category Cell Structure
Research Sub Category Integrins
This Anti-Integrin α4 Antibody, clone P4C2 is validated for use in IP, IH, FUNC for the detection of Integrin α4.
Linkage
Replaces: 04-1131
Physical form
Liquid ascites containing sodium azide as a preservative.
Storage and Stability
Store at -20°C in undiluted aliquots for up to 12 months. Avoid repeated freeze/thaw cycles.
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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Storage Class Code
12 - Non Combustible Liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Biochemical and biophysical research communications, 491(1), 204-208 (2017-07-18)
Adipogenesis is a process of differentiation from preadipocyte into adipocyte, and is regulated by several transcription factors, including the peroxisome proliferator-activated receptor gamma (PPARγ) and the CCAAT-enhancer-binding protein alpha (C/EBPα). CD36 is a membrane protein which contributes to the metabolic
The Journal of biological chemistry, 277(31), 27589-27592 (2002-06-19)
We have previously reported that junctional adhesion molecule 2 (JAM2) adheres to T cells through heterotypic interactions with JAM3. An examination of the cation dependence of JAM2 adhesion to HSB cells revealed a Mn(2+)-enhanced binding component indicative of integrin involvement.
Cell adhesion and communication, 7(3), 245-257 (2000-01-08)
Collaborative role of various fibronectin-binding integrins (alpha5beta1, alphavbeta1 and alphavbeta6) as mediators of cell adhesion and migration on fibronectin was studied using cultured HaCaT keratinocytes. This cell line spontaneously expressed all three fibronectin-binding integrins. In addition, the expression of alphavbeta6
Tumor integrin β1 (ITGB1) contributes to primary tumor growth and metastasis, but its specific roles in extravasation have not yet been clearly elucidated. In this study, we engineered a three-dimensional microfluidic model of the human microvasculature to recapitulate the environment
The Journal of biological chemistry, 279(40), 41734-41743 (2004-08-05)
In addition to the three known beta(1) integrin recognition sites in the N-module of thrombospondin-1 (TSP1), we found that beta(1) integrins mediate cell adhesion to the type 1 and type 2 repeats. The type 1 repeats of TSP1 differ from
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