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SAB4200694

Sigma-Aldrich

Anti-Talin antibody, Mouse monoclonal

clone 8D4, purified from hybridoma cell culture

Synonym(s):

Tln

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

8D4, monoclonal

form

buffered aqueous solution

species reactivity

Xenopus, rat, chicken, human, bovine, sheep, hamster

concentration

~1 mg/mL

technique(s)

ELISA: suitable
flow cytometry: suitable
immunoblotting: 1-2 μg/mL using whole extract of hamster CHO cells.
immunofluorescence: 2.5-5 μg/mL using chicken UMNSAH/DF1 cells.

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

chicken ... Tln1(395194)
human ... TLN1(7094)
rat ... Tln1(313494)

General description

Anti-Talin antibody, Mouse monoclonal, (mouse IgG1 isotype) is derived from the hybridoma 8D4 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with purified cytoskeletal Talin, from chicken gizzard. Talin is a high molecular weight cytoplasmic adapter protein. It is localized at a subset of adherens junctions. Talin contains an N-terminal FERM domain (the head) linked to a flexible rod comprised of 13 amphipathic helical bundles and a C-terminal helix (DD) that forms an anti-parallel dimer. It may be found either as monomer or dimer.

Immunogen

purified cytoskeletal Talin, from chicken gizzard.

Application

Anti-Talin antibody, Mouse monoclonal has been used in:
  • immunoblotting
  • immunofluorescence
  • fluorescence-activated cell sorting (FACS)
  • enzyme-linked immunosorbent assay (ELISA)

Biochem/physiol Actions

Talin is essential for integrin-mediated adhesion to the extracellular matrix (ECM). Talin links the actin cytoskeleton to integrins at the plasma membrane and presents in a variety of tissues and cell types. In cultured cells, Talin is absent in cell-cell junctions and is found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin contains multiple binding sites for the cytoskeletal protein, vinculin. It is considered as a mechanosensor, undergoing a progressive mechanoresponse to the varying forces exerted throughout adhesion and migration, such as conformational changes, disrupted or exposed ligand binding sites and exposing hidden protease cleavage sites.

Physical form

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

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 Code

10 - Combustible liquids

WGK

WGK 1

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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Sanceau J., et al.,
The Journal of Biological Chemistry, 278, 36537-3646 (2003)
Integrin Mechano-chemical Signaling Generates Plasma Membrane Nanodomains that Promote Cell Spreading
Kalappurakkal JM, et al.
Cell, 177(7), 1738-1756 (2019)
Talin contains three similar vinculin-binding sites predicted to form an amphipathic helix
SMITH BJ, et al.
The Biochemical Journal, 341(2), 257-263 (1999)
Huriye Ercan et al.
Cancers, 13(9) (2021-06-03)
In order to comprehensively expose cancer-related biochemical changes, we compared the platelet proteome of two types of cancer with a high risk of thrombosis (22 patients with brain cancer, 19 with lung cancer) to 41 matched healthy controls using unbiased
Talin dependent mechanosensitivity of cell focal adhesions
Yan J, et al.
Cellular and Molecular Bioengineering, 8(1), 151-159 (2015)

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