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Calnexin-NT Antibody: PerCP

Rabbit Anti-Human Calnexin-NT Polyclonal

Product Specifications

Background

Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into mulit-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

CAS Number

9007-83-4

Specifications

Detects the N-terminal domain of Calnexin ~90kDa.

Product Name Alternative

Cell Signaling, Tags and Cell Markers, Organelle Markers

UNSPSC

12352203

Gene ID

403908

Swiss Prot

P24643

Accession Number

NP_001003232.1

Cellular Locus

Endoplasmic Reticulum | Endoplasmic Reticulum Membrane | Melanosome

Host

Rabbit

Species Reactivity

Human,Mouse,Rat,Bovine,Chicken,Dog,Guinea Pig,Hamster,Pig,Monkey,Rabbit,Sheep,Xenopus

Immunogen

A 19 residue synthetic peptide based on dog calnexin and the peptide coupled to KLH

Target

Calnexin

Clonality

Polyclonal

Conjugation

PerCP

Validated Applications

WB,IHC,ICC/IF,ELISA

Purification

Rabbit Antiserum

Dilution

WB (1:5000), IHC (1:100), ICC/IF (1:100), IP (1:100); optimal dilutions for assays should be determined by the user.

Weight

0.2

Buffer

95.64mM Phosphate, 2.48mM MES and 2mM EDTA

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

References & Citations

1. Rajagopalan S., Xu Y., and Brenner M.B. (1994) Science 263(5145): 387-90. 2. Tjoelker L.W., et al. (1994) Biochemistry 33:3229. 3. Schrag J. et al. (2001) Molecular Cell 8(3): 633-644. 4. Janiszewski M. (2005) J. Biol Chem. 280(49):40813-40819. 5. Elagoz A., Callejo M., Armstrong J., and Rokeach L. A. (1999) J. Cell Sci. 112: 4449-4460. 6. Otteken A. and Moss B. (1996) J Bio Chem. 271(1): 97-103. 7. Galvin K. et al. (1992) Proc Natl Acad Sci USA. 89(18): 8452-6. 8. Raggo C., et al. (2002) Mol Cell Biol. 22: 5639-5649. 9. Rubio M.E., and Wenthold R.J. (1999) J Neurochem. 73: 942-948.
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