Fixation generally influences subsequent staining procedures. A recommended approach would be to fix identical tissue sections in alcohol and 10% Neutral Buffered Formalin and then determine which method yields the best staining outcome.
L7381
Lectin from Arachis hypogaea (peanut)
FITC conjugate, lyophilized powder
Synonym(s):
PNA, Peanut agglutinin
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1 MG
$136.00
2 MG
$230.00
5 MG
$457.00
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1 MG
$136.00
2 MG
$230.00
5 MG
$457.00
About This Item
UNSPSC Code:
12352202
NACRES:
NA.32
$136.00
Please contact Customer Service for Availability
Recommended Products
conjugate
FITC conjugate
Quality Level
form
lyophilized powder
composition
Protein, ~10% Lowry
extent of labeling
4-8 mol FITC per mol protein
storage temp.
−20°C
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General description
Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in β-strands and possesses a carbohydrate binding sites on the surface.[1]
Application
Lectin from Arachis hypogaea (peanut) has been used:
- to determine the acrosomal status (presence or absence of acrosomal matrix corresponding to intact or acrosome-reacted spermatozoa) on viable sperm cells[2]
- to probe cryosections of mediastinal lymph nodes (mLNs) with fluorochrome-labeled PNA and anti-B220 to detect germinal centers (GCs)[3]
- to visualize the cone outer segments of pre-treated retinal sections[4]
Biochem/physiol Actions
Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling. This is because of its specific interaction with oligosaccharides, glycoproteins and glycolipids. In plants and fungi, lectin defends against pathogens/feeders. Lectin participates in host recognition and tissue adhesion, thereby aids in the pathogenesis of microorganism.[1]
PNA does not agglutinate normal human erythrocytes, but strongly agglutinates neuraminidase treated erythrocytes. PNA has potent anti-T activity similar to the anti-T antibody in human sera. The lectin can be used to distinguish between human lymphocyte subsets.
Physical form
Contains phosphate buffer salts and NaCl
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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If samples are stored in 100% ethanol, it there an issue for the actual binding of the lectin to surface sugars?
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What is the Department of Transportation shipping information for this product?
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Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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How does the storage temperature relate to shipping conditions?
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The storage conditions that a Sigma-Aldrich catalog and label recommend for products are deliberately conservative. For many products, long-term storage at low temperatures will increase the time during which they are expected to remain in specification and therefore are labeled accordingly. Where short-term storage, shipping time frame, or exposure to conditions other than those recommended for long-term storage will not affect product quality, Sigma-Aldrich will ship at ambient temperature. The products sensitive to short-term exposure to conditions other than their recommended long-term storage are shipped on wet or dry ice. Ambient temperature shipping helps to control shipping costs for our customers. At any time, our customers can request wet- or dry-ice shipment, but the special handling is at customer expense if our product history indicates that the product is stable for regular shipment.
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Is the peanut lectin (Lectin from Arachis hypogaea) a glycoprotein? If so, what is the carbohydrate content?
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Peanut lectin is not a glycoprotein. Although peanut lectin binds specifically to a particular carbohydrate (beta-gal(1-->3)galNac) in other molecules, the lectin itself does not contain any carbohydrate. Please see page 231 of the following paper: R. Banerjee, et al., "Crystal structure of peanut lectin, a protein with an unusual quaternary structure". Proc. Nat. Acad. Sci., USA, 91, 227-231 (1994).
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