Sialo-Xenoantigenic Glycobiology

Name: Sialo-Xenoantigenic Glycobiology
Brand: Springer Nature
SKU: 9783642340949
Availability: InStock

Best Price:
Buy Sialo-Xenoantigenic Glycobiology for $84.99 at @ Link.springer.com
No coupon is required — this is the standard retail price.

Set a price drop alert to never miss an offer.

1 Offer Price Range: $84.99 - $84.99

BEST PRICE

Single Product Purchase

$84.99

@ Link.springer.com BUY Now

Price Comparison

Seller	Contact Seller	List Price	On Sale	Shipping	Best Promo	Final Price	Volume Discount	Financing	Availability	Seller's Page
BEST PRICE 1 Product Purchase @ Link.springer.com		$84.99	$84.99			$84.99		See Site	In stock	Visit Store

Product Details

Brand

Springer Nature

Manufacturer

N/A

Part Number

GTIN

9783642340949

Condition

New

Product Description

Carbohydrate antigens on glycoconjugates of mammalian cells play crucial roles in various biological processes and are epitopes recognized by the immune system, as glycobiology has hugely been progressed during the past two decades. The book focuses on sialic acidbased xenoantigenes. In pig to human xenotransplantation, exposure of pig organs to human blood results in hyper acute rejection (HAR), caused by differences in carbohydrate epitopes between human and pig vascular endothelia. Although Gal-antigen as major antigen was eliminated, the remaining non-Gal antigens are considered to be xenoantigens. Sialosyl-Tn or Hanganutziu-Deicher (HD), are non-Gal antigens specific to natural antibodies in human. To overcome rejection responses such as HAR, studies of genes involved in carbohydrate antigens, causing xenoantigenicity, are necessary. Knowledge of pig glycosyltransferases are also useful to apply to xenoantigen masking or identification of the xenoantigenic sialylglycan(s). In the first chapter the screening for pig glycosyltransferase genes for xenoantigens is presented. In the chapter II to IV the cloning, characterization, and investigation of the regulatory mechanism of the pig CMAH gene in NeuGc biosynthesis is shown. Lastly, the effects of an alteration of pig glycosylation patterns on human serum-mediated cytotoxicity, caused by human sialyltransferases including hST6GalNAc IV is presented.

Available Colors

N/A

Available Sizes

N/A