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Western blotAntibody data
- Antibody Data
- Antigen structure
- References [10]
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- Product number
- ABIN264868 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Calnexin (CANX) antibody
- Antibody type
- Polyclonal
- Antigen
- A 19 residue synthetic peptide based on Canine Calnexin and the peptide coupled to KLH
- Reactivity
- Human, Mouse, Rat, Bovine, Canine, Chicken/Avian, Guinea Pig, Hamster, Porcine, Rabbit, Sheep, Simian, Xenopus
- Host
- Rabbit
- Isotype
- IgG
- Vial size
- 0.2 mL
- Storage
- Store the antibody undiluted at 2-8°C one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. Shelf life: one year from despatch.
Submitted references β1D chain increases α7β1 integrin and laminin and protects against sarcolemmal damage in mdx mice.
Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells.
Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis.
The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
Calnexin and the immunoglobulin binding protein (BiP) coimmunoprecipitate with AMPA receptors.
Although calnexin is essential in S. pombe, its highly conserved central domain is dispensable for viability.
Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin.
Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5.
Retention of unassembled components of integral membrane proteins by calnexin.
The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.
Liu J, Milner DJ, Boppart MD, Ross RS, Kaufman SJ
Human molecular genetics 2012 Apr 1;21(7):1592-603
Human molecular genetics 2012 Apr 1;21(7):1592-603
Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells.
Janiszewski M, Lopes LR, Carmo AO, Pedro MA, Brandes RP, Santos CX, Laurindo FR
The Journal of biological chemistry 2005 Dec 9;280(49):40813-9
The Journal of biological chemistry 2005 Dec 9;280(49):40813-9
Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis.
Raggo C, Rapin N, Stirling J, Gobeil P, Smith-Windsor E, O'Hare P, Misra V
Molecular and cellular biology 2002 Aug;22(16):5639-49
Molecular and cellular biology 2002 Aug;22(16):5639-49
The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M
Molecular cell 2001 Sep;8(3):633-44
Molecular cell 2001 Sep;8(3):633-44
Calnexin and the immunoglobulin binding protein (BiP) coimmunoprecipitate with AMPA receptors.
Rubio ME, Wenthold RJ
Journal of neurochemistry 1999 Sep;73(3):942-8
Journal of neurochemistry 1999 Sep;73(3):942-8
Although calnexin is essential in S. pombe, its highly conserved central domain is dispensable for viability.
Elagöz A, Callejo M, Armstrong J, Rokeach LA
Journal of cell science 1999 Dec;112 ( Pt 23):4449-60
Journal of cell science 1999 Dec;112 ( Pt 23):4449-60
Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin.
Otteken A, Moss B
The Journal of biological chemistry 1996 Jan 5;271(1):97-103
The Journal of biological chemistry 1996 Jan 5;271(1):97-103
Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5.
Tjoelker LW, Seyfried CE, Eddy RL Jr, Byers MG, Shows TB, Calderon J, Schreiber RB, Gray PW
Biochemistry 1994 Mar 22;33(11):3229-36
Biochemistry 1994 Mar 22;33(11):3229-36
Retention of unassembled components of integral membrane proteins by calnexin.
Rajagopalan S, Xu Y, Brenner MB
Science (New York, N.Y.) 1994 Jan 21;263(5145):387-90
Science (New York, N.Y.) 1994 Jan 21;263(5145):387-90
The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.
Galvin K, Krishna S, Ponchel F, Frohlich M, Cummings DE, Carlson R, Wands JR, Isselbacher KJ, Pillai S, Ozturk M
Proceedings of the National Academy of Sciences of the United States of America 1992 Sep 15;89(18):8452-6
Proceedings of the National Academy of Sciences of the United States of America 1992 Sep 15;89(18):8452-6
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