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MAB2250

Sigma-Aldrich

Anti-Integrin β1 Antibody, clone 21C8

clone 21C8, Chemicon®, from mouse

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

purified immunoglobulin

antibody product type

primary antibodies

clone

21C8, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

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

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ITGB1(3688)

Specificity

Reacts with the human integrin beta1 subunit. Specificity verified by preclearing of beta1in immunoprecipitation, flow cytometry on transfectant cells displaying human beta1 integrin, and reactivity with purified beta1.

Immunogen

Jurkat T-leukemic cell line

Application

Anti-Integrin β1 Antibody, clone 21C8 is an antibody against Integrin β1 for use in FC, IP, FUNC, IH.
Immunoprecipitation

Immunohistochemistry on frozen sections

Flow cytometry

Stimulates adhesion of cells to extracellular matrix proteins (Wilkins et al., 1996)

Does not bind reduced beta1 integrin on Western blot

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

Physical form

Format: Purified
Purified immunoglobulin from Protein A Sepharose chromatography. Liquid in 0.02M PB pH 7.6, 0.25M NaCl containing 0.1% sodium azide.

Storage and Stability

Maintain at 2-8°C in undiluted aliquots for up to 6 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
Sepharose is a trademark of Cytiva

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

10 - Combustible liquids

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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Stretch of beta 1 integrin activates an outwardly rectifying chloride current via FAK and Src in rabbit ventricular myocytes.
Browe, DM; Baumgarten, CM
The Journal of General Physiology null
David M Browe et al.
The Journal of general physiology, 127(3), 237-251 (2006-03-01)
Stretch of beta1 integrins activates an outwardly rectifying, tamoxifen-sensitive Cl(-) current (Cl(-) SAC) via AT1 receptors, NADPH oxidase, and reactive oxygen species, and Cl(-) SAC resembles the volume-sensitive Cl(-) current (I(Cl,swell)). Epidermal growth factor receptor (EGFR) kinase undergoes transactivation upon
hGAAP promotes cell adhesion and migration via the stimulation of store-operated Ca2+ entry and calpain 2.
Saraiva, N; Prole, DL; Carrara, G; Johnson, BF; Taylor, CW; Parsons, M; Smith, GL
The Journal of cell biology null
Rebecca J Burkhalter et al.
The Journal of biological chemistry, 290(36), 22143-22154 (2015-07-16)
During tumor progression, epithelial ovarian cancer (EOC) cells undergo epithelial-to-mesenchymal transition (EMT), which influences metastatic success. Mutation-dependent activation of Wnt/β-catenin signaling has been implicated in gain of mesenchymal phenotype and loss of differentiation in several solid tumors; however, similar mutations
R C Casey et al.
The American journal of pathology, 159(6), 2071-2080 (2001-12-06)
Ovarian carcinoma multicellular spheroids are an in vitro model of micrometastasis whose adhesive abilities have not been elucidated. In this study, we identified adhesion molecules that mediate the formation of ovarian carcinoma spheroids and their subsequent adhesion to extracellular matrix

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