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Merck
CN

MAB2057

Anti-Integrin α3 Antibody, clone ASC-6

clone ASC-6, Chemicon®, from mouse

别名:

CD49c

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
ASC-6, monoclonal
Application:
flow cytometry
immunohistochemistry
immunoprecipitation (IP)
Species reactivity:
human
Citations:
10
Technique(s):
flow cytometry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
Uniprot accession no.:
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产品名称

Anti-Integrin α3 Antibody, clone ASC-6, clone ASC-6, Chemicon®, from mouse

biological source

mouse

conjugate

unconjugated

antibody form

purified antibody

antibody product type

primary antibodies

clone

ASC-6, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

flow cytometry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

Gene Information

human ... ITGA3(3675)

Physical form

Liquid in 0.02M PB pH 7.6, 0.25M NaCl containing 0.1% sodium azide.
Format: Purified

Preparation Note

Maintain at 2-8°C in undiluted aliquots for up to 6 months.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Application

Anti-Integrin α3 Antibody, clone ASC-6 is an antibody against Integrin α3 for use in FC, IP, IH.
Inhibition of cell attachment: inhibits SCC9 cell adhesion to human and EHS laminin, but not laminin peptide GD-2. Potentiates inhibition of SKOV-3 cell adhesion to EHS laminin by anti-integrin alpha 5 antibody GoH3. Does not inhibit either cell′s adhesion to fibronectin or collagen type IV.

Immunohistochemistry: on acetone-fixed frozen human epithelial tissues including tongue,foreskin and ovary. Not for use on formalin-fixed tissue.

Flow cytometry: stains human squamous cell carcinoma (SCC9), ovarian carcinoma (SKOV-3) and umbilical vein endothelial cells (HUVEC).

Working dilutions must be determined by end user.
Research Category
Cell Structure
Research Sub Category
Integrins

Biochem/physiol Actions

Human alpha3 integrin (CD49c)

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 squamous cell carcinoma cells (SCC9)

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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存储类别

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Yu-Chen Gu et al.
Blood, 101(3), 877-885 (2002-10-24)
Laminins are alphabetagamma heterotrimeric extracellular proteins that regulate cellular functions by adhesion to integrin and nonintegrin receptors. Laminins containing alpha4 and alpha5 chains are expressed in bone marrow, but their interactions with hematopoietic progenitors are unknown. We studied human bone
Yi I Wu et al.
The Biochemical journal, 407(2), 171-177 (2007-07-26)
The transmembrane collagenase MT1-MMP (membrane-type 1 matrix metalloproteinase), also known as MMP-14, has a critical function both in normal development and in cancer progression, and is subject to extensive controls at the post-translational level which affect proteinase activity. As zymogen
Andrey Makarov et al.
Cell biology international, 37(10), 1080-1088 (2013-05-21)
Glioblastoma is the most common brain cancer. Ephrins and their Eph receptors play important roles in the development of central nervous system and the regulation of cancer cell migration and invasion. In a search for the Eph receptor complexes, we
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
Piia Vehviläinen et al.
The Journal of biological chemistry, 278(27), 24705-24713 (2003-04-30)
Of the four latent transforming growth factor (TGF)-beta-binding proteins (LTBPs), LTBP-2 is different in the respect that it does not bind small latent forms of TGF-beta. LTBP-2 is therefore likely to have other roles in the extracellular matrix. LTBP-2 contains

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