ALEXIS Biochemicals: Monoclonal Antibody to PDI (RL77)

ALX-804-013

Revised 29-Sep-05

Monoclonal Antibody to PDI (RL77)
SYNONYMS	anti-Protein Disulfide-isomerase MAb (RL77)
PRODUCT LINE	Protein Synthesis, Modification & Degradation
PRODUCT CATEGORY	Protein Synthesis, Modification & Degradation Other Products

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-804-013-R100		100 µl	379.00 USD

Product Specification

SPECIES CROSSREACTIVITY:	Human Mouse Rat Others
CLONE:	RL77
ISOTYPE:	Mouse IgG2b
FORMULATION:	Liquid. Ascites fluid containing 0.05% sodium azide.
IMMUNOGEN:	Purified rat liver PDI (protein disulphide-isomerase).
SPECIFICITY:	Recognizes human, mouse, rat and hamster and Xenopus laevis PDI. Detects a band of ~59kDa (rat liver PDI) or ~61KDa (human liver PDI).
APPLICATION:	Immunohistochemistry (paraffin sections (1:100)) Immunoprecipitation (inhibits activity of PDI in vitro) Western Blot (1:1'000)
SHIPPING:	SHIPPED ON BLUE ICE
LONG TERM STORAGE:	-20°C
HANDLING:	Avoid freeze/thaw cycles.

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Product Specific Literature References

Protein disulphide-isomerase from human placenta and rat liver. Purification and immunological characterization with monoclonal antibodies: C.S. Kaetzel, et al.; Biochem. J. 241, 39 (1987) Abstract

General Information

The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide-Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Further Categories Containing This Product:

Endoplasmatic Reticulum Stress • Monoclonal Antibodies

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