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Sigma-Aldrich

Glycoprotein Detection Kit

Sufficient for 10 mini-gels (10 × 10 cm) or 5 gels or membranes (16.5 × 19 cm)

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

usage

 kit sufficient for 10 mini-gels (10 × 10 cm)
 kit sufficient for 5 gels or membranes (16.5 × 19 cm)

carbohydrate detection limit measuring range

25-100 ng/band

storage temp.

2-8°C

Application

The Glycoprotein Detection Kit is designed for the selective staining of glycoproteins on polyacrylamide gels and membranes using a modification of the Periodic Acid-Schiff (PAS) method. Staining of sugar moieties of glycoproteins yields magenta bands with a colorless background. The periodic acid/Schiff reagent stains vicinal diol groups found mainly on peripheral sugars and sialic acids and is used as a general glycoprotein stain.

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Signal Word

Danger

Hazard Classifications

Acute Tox. 3 Dermal - Acute Tox. 3 Inhalation - Acute Tox. 3 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - Carc. 1B - Eye Dam. 1 - Met. Corr. 1 - Ox. Liq. 1 - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT RE 1 Oral - STOT SE 1

Target Organs

Eyes, Thyroid

Supplementary Hazards

EUH031

Storage Class Code

5.1A - Strongly oxidizing hazardous materials

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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BMC biotechnology, 12, 59-59 (2012-09-08)
Single-domain antibodies (sdAbs), also known as nanobodies or VHHs, are characterized by high stability and solubility, thus maintaining the affinity and therapeutic value provided by conventional antibodies. Given these properties, VHHs offer a novel alternative to classical antibody approaches. To
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The envelope (env) protein of the human endogenous retrovirus type K (HERV-K) family is commonly expressed on the surface of breast cancer cells. We assessed whether HERV-K env is a potential target for antibody-based immunotherapy of breast cancer. We examined
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Andrews, A.T., ed.
Biochemical and Clinical Applications, 2nd ed, 38-42 (1988)
Anthony G Tsolaki et al.
Molecular immunology, 54(3-4), 278-283 (2013-01-22)
In this study, we investigated the potential molecular and immunological differences of a recombinant fusion protein (Hybrid-1), comprising of the immunodominant antigens Ag85B and ESAT-6 from Mycobacterium tuberculosis, derived from two different expression systems, namely Mycobacterium smegmatis and Escherichia coli.
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