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Calnexin Antibody

CALX, CANX, IP90, Major histocompatibility complex class I

Catalog No. Product Name Size List Price (US$) Quantity
PA000987-B0463 Calnexin (Ab-583) Polyclonal Antibody 50 ug 250.00
PA000987-B0463 Calnexin (Ab-583) Polyclonal Antibody 100 ug 350.00
Description

Introduction
Calnexin (CNX) is a 67 kDa integral protein (that appears variously as a 90 kDa, 80 kDa or 75 kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER). It consists of a large (50 kDa) N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail. Calnexin is one of the chaperone molecules, which are characterized by their main function of assisting protein folding and quality control, ensuring that only properly folded and assembled proteins proceed further along the secretory pathway. The function of calnexin is to retain unfolded or unassembled N-linked glycoproteins in the ER. Antibodies against calnexin can be used as markers for the ER in immmunofluorescence experiments.

PA000987-B0463: Calnexin (Ab-583) Polyclonal Antibody

Rabbit Polyclonal Antibody.
Specificity/Sensitivity: Calnexin (Ab-583) antibody detects endogenous levels of total Calnexin protein.
Applications: WB: 1:500~1:1000 IHC: 1:50~1:100 IF: 1:500~1:1000 ELISA: 1:10000.
Reactivity: Human, Mouse, Rat.
Immunogen: The antiserum was produced against synthesized non-phosphopeptide derived from human Calnexin around the phosphorylation site of serine 583 (N-R-SP-P-R).
Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Form of Antibody: Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl, 0.02% sodium azide and 50% glycerol.

Storage/Stability: Stable for 1 year at -20°C and 3 months at 4°C. For maximum recovery of the product, centrifuge the original vial after thawing and before removing the cap. Aliquot to avoid repeated freezing and thawing.

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