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Merck
CN

CC102C

Human Integrin αVβ5 Protein, Triton X-100 Formulation

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UNSPSC Code:
12352202
NACRES:
NA.41
eCl@ss:
32160405
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biological source

human

assay

>95% (silver stain, SDS-PAGE)

form

liquid

manufacturer/tradename

Chemicon®

concentration

0.325 mg/mL

NCBI accession no.

UniProt accession no.

Gene Information

human ... ITGAV(3685)

General description

Integrin alphaV beta5 was purified from human placenta by affinity chromatography using immobilized monoclonal antibodies to alphaV beta5 integrin. Two bands are identified with silver stain, corresponding to alphaV (145kDa) and beta5 (90kDa) subunits under nonreducing conditions. Product was tested and found negative for HIV, HBsAg, syphilis, and hepatitis. Integrin alphaV beta5 interacts with vitronectin in ELISA.

Application

Electrophoresis

Immunoblotting (nonreduced conditions)

Ligand Binding studies.

Optimal working dilutions must be determined by end user.

Physical form

Purified protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM MgCl, 0.2% Triton X-100, with no preservatives.

Preparation Note

Maintain at -70°C in undiluted aliquots. Avoid repeated freeze/ thaw cycles.

Analysis Note

Two main protein bands corresponding to aV (145 kD) and β5 (90 kD) subunits are seen in silver stained gel under non-reduced conditions.

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.

存储类别

12 - Non Combustible Liquids

wgk

WGK 2


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Caulollins from Caulobacter crescentus, a pair of partially unstructured proteins of betagamma-crystallin superfamily, gain structure upon binding calcium.
Maroor K Jobby,Yogendra Sharma
Biochemistry null
V M Belkin et al.
The Journal of cell biology, 111(5 Pt 1), 2159-2170 (1990-11-01)
A membrane glycoprotein complex was isolated and purified from human smooth muscle by detergent solubilization and affinity chromatography on collagen-Sepharose. The complex was identified as VLA-1 integrin and consisted of two subunits of 195 and 130 kD in SDS-PAGE. Liposomes

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