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MAB2078Z

Sigma-Aldrich

Anti-Integrin α9β1 Antibody, clone Y9A2, azide free

clone Y9A2, Chemicon®, from mouse

Synonym(s):

MAB2078

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

Y9A2, monoclonal

species reactivity

human, guinea pig

should not react with

rat

manufacturer/tradename

Chemicon®

technique(s)

flow cytometry: suitable
immunoprecipitation (IP): suitable

isotype

IgG1

suitability

not suitable for Western blot
not suitable for immunohistochemistry

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ITGA9(3680)

Related Categories

Specificity

Reactive with human and guinea pig alpha9beta1.

Immunogen

Murine L cells transfected with human alpha9.

Application

Detect Integrin α9β1 using this Anti-Integrin α9β1 Antibody, clone Y9A2, azide free validated for use in FC & IP.
Immunoprecipitation

FACS Analysis

Function blocking: 100% inhibition of alpha9beta1-mediated adhesion to the third fibronectin type III repeat in tenascin at <10 μg/mL.

Not effective for immunohistochemistry, immunocytochemistry or western blot.

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

Physical form

Format: Purified
Protein A Purified mouse immunoglobulin in 20 mM sodium phosphate, 250 mM NaCl, pH. 7.6, with no preservatives.
Protein A purified

Storage and Stability

Maintain for 1 year at 2–8°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
Integrin alpha9beta1 positive tissues include basal keratinocytes, hepatocytes, muscle (smooth and skeletal), and airway epithelium.

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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wgk_germany

WGK 2

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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A V Timoshenko et al.
British journal of cancer, 97(8), 1090-1098 (2007-10-04)
Vascular endothelial growth factor C (VEGF-C) is a lymphangiogenic factor over-expressed in highly metastatic, cyclooxygenase (COX)-2 expressing breast cancer cells. We tested the hypothesis that tumour-derived VEGF-C may play an autocrine role in metastasis by promoting cellular motility through one
Differential regulation of airway epithelial integrins by growth factors.
Wang, A, et al.
American Journal of Respiratory Cell and Molecular Biology, 15, 664-672 (1996)
Patrick M Lelliott et al.
ImmunoHorizons, 6(2), 170-183 (2022-02-24)
Anti-neutrophil cytoplasmic Ab (ANCA)-associated vasculitis (AAV) is a life-threatening condition characterized by improper activation of neutrophils and the release of neutrophil extracellular traps (NETs) in small vessels. This study aimed to explain the role of NETs in AAV pathogenesis by
Andrew Filer et al.
Arthritis and rheumatism, 54(7), 2096-2108 (2006-06-28)
Synovial fibroblasts share a number of phenotype markers with fibroblasts derived from bone marrow. In this study we investigated the role of matched fibroblasts obtained from 3 different sources (bone marrow, synovium, and skin) to test the hypothesis that synovial
Saji Oommen et al.
The Journal of biological chemistry, 286(2), 1083-1092 (2010-11-13)
Integrin α9β1 mediates accelerated cell adhesion and migration through interactions with a number of diverse extracellular ligands. We have shown previously that it directly binds the vascular endothelial growth factors (VEGF) A, C, and D and contributes to VEGF-induced angiogenesis

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