MAB1987
Anti-Integrin β1 Antibody, clone P4C10
culture supernatant, clone P4C10, Chemicon®
Synonym(s):
CD29
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
mouse
Quality Level
antibody form
culture supernatant
antibody product type
primary antibodies
clone
P4C10, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2a
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... ITGB1(3688)
Related Categories
Specificity
Reacts with the beta-1 subunit of the integrin protein family. Appears to be human specific. Unlike many beta-1 monoclonals 4C10′s epitope is not trypsin sensitive.
Application
Detect Integrin β1 using this Anti-Integrin β1 Antibody, clone P4C10 validated for use in ELISA, IP, WB & IC.
Inhibits attachment of UCLA-P3 cells to collagen type I (Wayner, 1991). Inhibits endodermal and keratinocytes to collagen, fibronectin and laminin. It also inhibits cell to cell adhesion. Typical dilution ranges are 1:50-1:500.
Immunoflourescence
Immunoblotting
Immunoprecipitation
ELISA
Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected Integrin β1 in HeLa cells.
Optimal working dilutions must be determined by end user.
Immunoflourescence
Immunoblotting
Immunoprecipitation
ELISA
Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected Integrin β1 in HeLa cells.
Optimal working dilutions must be determined by end user.
Research Category
Cell Structure
Cell Structure
Research Sub Category
Integrins
Integrins
Physical form
Tissue Culture supernatant, containing 0.1% sodium azide.
Storage and Stability
Maintain frozen at -20°C in undiluted aliquots for up to 12 months.
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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Pricing
WGK
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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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M Fornaro et al.
Molecular biology of the cell, 11(7), 2235-2249 (2000-07-11)
The integrin cytoplasmic domain modulates cell proliferation, adhesion, migration, and intracellular signaling. The beta(1) integrin subunits, beta(1C) and beta(1A), that contain variant cytoplasmic domains differentially affect cell proliferation; beta(1C) inhibits proliferation, whereas beta(1A) promotes it. We investigated the ability of
W-C Liao et al.
Placenta, 36(4), 357-364 (2015-02-11)
Glycosylation controls diverse protein functions and regulates various cellular phenotypes. Trophoblast invasion is essential for normal placental development. However, the role of glycosylation in human placenta throughout pregnancy is still unclear. The β-1,4-galactosyltransferase III (B4GALT3) has been found to regulate
Tsutomu Sato et al.
Cancer research, 65(15), 6950-6956 (2005-08-03)
CD26 is an antigen with key role in T-cell biology and is expressed on selected subsets of aggressive T-cell malignancies. To elucidate the role of CD26 in tumor behavior, we examine the effect of CD26 depletion by small interfering RNA
Platelet matrix metalloprotease-1 mediates thrombogenesis by activating PAR1 at a cryptic ligand site.
Trivedi, V; Boire, A; Tchernychev, B; Kaneider, NC; Leger, AJ; O'Callaghan, K; Covic et al.
Cell null
Ann-Marie Baker et al.
Journal of the National Cancer Institute, 103(5), 407-424 (2011-02-02)
Emerging evidence implicates lysyl oxidase (LOX), an extracellular matrix-modifying enzyme, in promoting metastasis of solid tumors. We investigated whether LOX plays an important role in the metastasis of colorectal cancer (CRC). We analyzed LOX expression in a patient CRC tissue
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