MAB1955
Anti-Integrin α4 Antibody, clone P4C2
ascites fluid, clone P4C2, Chemicon®
Sinónimos:
CD49d
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
mouse
Quality Level
antibody form
ascites fluid
antibody product type
primary antibodies
clone
P4C2, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
isotype
IgG3
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... ITGA4(3676)
Specificity
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
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
Cell Structure
Research Sub Category
Integrins
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
12 - Non Combustible Liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Huanqing Gao et al.
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
Sonia A Cunningham et al.
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.
L Koivisto et al.
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
Maria J Calzada et al.
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
Michelle B Chen et al.
Cancer research, 76(9), 2513-2524 (2016-03-19)
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
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