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UNSPSC Code:
12352202
NACRES:
NA.77
eCl@ss:
32160405
Technischer Dienst
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Unterstützung erhaltenTechnischer Dienst
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Unterstützung erhaltenbiological source
human
form
liquid
manufacturer/tradename
Chemicon®
impurities
CONTAMINANT(S)
none detected
NCBI accession no.
UniProt accession no.
Quality Level
Gene Information
human ... ITGA5(3678)
Analysis Note
Nonreduced SDS-PAGE of 15 mg on 5-15% polyacrylamide slab gel and staining with Coomassie shows only two main bands at 110 kDa (beta1 subunit) and 155 kDa (alpha5 subunit).A weak band at 205 kDa is due to dimerization of the b1 subunit (Belkin et al., 1996)
Application
Electrophoresis and Immunoblotting control. Due to the existance of reduction sensitive sites within the integrin subunits, it is recommended that gels be run under non-reducing conditions for best results. Under non-reducing conditions, the alpha5 subunit will migrate at 155 kDa while the beta1 subunit will migrate at 110 kDa.
Function: Liposomes containing Integrin alpha5/beta1 adhere to surfaces coated with fibronectin in an RGD-dependent fashion.
Function: Liposomes containing Integrin alpha5/beta1 adhere to surfaces coated with fibronectin in an RGD-dependent fashion.
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.
General description
Integrin a5/b1 purified from smooth muscle and placental tissue under nondenaturing conditions by affinity chromatography on fibronectin-Sepharose (Belkin, 1990).
Two main protein bands corresponding to a5 (145 kD) and beta1 (120 kD) subunits are seen in silver stained 7.5%
polyacrylamide gels under nonreduced conditions. Minor protein band at the 210 kD corresponding to beta1 subunit disulfide dimmer, which is formed during electrophoresis and disappears after reduction.
Two main protein bands corresponding to a5 (145 kD) and beta1 (120 kD) subunits are seen in silver stained 7.5%
polyacrylamide gels under nonreduced conditions. Minor protein band at the 210 kD corresponding to beta1 subunit disulfide dimmer, which is formed during electrophoresis and disappears after reduction.
Product Source: Human smooth muscle and placental tissue.
Physical form
Purified protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM MgCl2 containing 0.2% Triton X-100. No preservatives. Source material for the enclosed purified human proteins, Integrin alpha5beta1, has been tested for antibodies to HIV, HCV, and HbsAg and found to be negative by an approved test.
Preparation Note
Maintain at -70°C in undiluted aliquots. Avoid repeated freeze/thaw cycles.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Lagerklasse
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Analysenzertifikate (COA)
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