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Merck

C4731

Sigma-Aldrich

Anti-Calnexin antibody produced in rabbit

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Synonym(e):

Anti-CNX, Anti-IP90, Anti-P90

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.44

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

IgG fraction of antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen 90 kDa

Speziesreaktivität

canine, rat, mouse, human

Verpackung

antibody small pack of 25 μL

Erweiterte Validierung

independent
Learn more about Antibody Enhanced Validation

Methode(n)

immunoprecipitation (IP): 1:2,000 using whole cell RIPA lysate of the human epitheloid carcinoma HeLa cell line
indirect immunofluorescence: 1:200 using 3% paraformaldehyde-fixed, 0.5% Triton X-100 treated, Madin Darby canine kidney MDCK cell line
microarray: suitable
western blot: 1:2,000 using whole cell RIPA lysate of the human hepatocytoma HepG2 cell line

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... CANX(821)
mouse ... Canx(12330)
rat ... Canx(29144)

Allgemeine Beschreibung

Calnexin contains a long (461 amino acids) N-terminal Ca2+ -binding domain extending into the lumen of the endoplasmic reticulum (ER), a short (22 amino acids) transmembrane segment and an acidic cytosolic domain (96 amino acids).
Calnexin, is a calcium binding type I integral membrane protein present mainly in the endoplasmic reticulum. It plays a pivotal role in quality control processes during protein synthesis and folding. Anti-calnexin antibody (diluted 1: 300) can be used in dual immunofluorescence staining to visualize TG2 transport.

Spezifität

Rabbit anti-calnexin antibody reacts specifically with calnexin (90 kDa) of dog, mouse, rat and human.

Immunogen

Synthetic peptide corresponding to the c-terminus of human calnexin (amino acids 573-592) conjugated to KLH.

Anwendung

Anti-Calnexin antibody produced in rabbit has been used in:
  • western blot analysis
  • immunofluorescence
  • dual immunofluorescence staining

Biochem./physiol. Wirkung

Calnexin binds newly synthesized glycoproteins and misfolded proteins and is believed to play a critical role in quality control processes during protein synthesis and folding. Calnexin acts as a lectin-like chaperone that binds oligosaccharide residues of newly synthesized N-linked glycoproteins. Calnexin has been shown to be associated with several cell surface proteins, including major histocompatibility complex (MHC) class I heavy chain, T-cell receptor (TCR), and B cell membrane immunoglobulin during translocation through the endoplasmic reticulum (ER). It also forms complexes with other resident ER proteins involved in Ca2+ -dependent retention of proteins.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Haftungsausschluss

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Die Dokumentenbibliothek aufrufen

STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER
Alpy F, et al.
Journal of Cell Science, 126(23), 5500-5512 (2013)
Quality control system of the endoplasmic reticulum and related diseases
Wu JC, et al.
Acta biochimica et biophysica Sinica, 38(4), 219-226 (2006)
Calnexin and calreticulin, molecular chaperones of the endoplasmic reticulum
Calreticulin, 49-62 (2003)
Juha M Torkko et al.
Molecular and cellular biology, 35(6), 914-927 (2015-01-07)
The type 1 diabetes autoantigen ICA512/IA-2/RPTPN is a receptor protein tyrosine phosphatase of the insulin secretory granules (SGs) which regulates the size of granule stores, possibly via cleavage/signaling of its cytosolic tail. The role of its extracellular region remains unknown.
N Echeverry et al.
Cell death and differentiation, 20(6), 785-799 (2013-02-23)
The pro-apoptotic BCL-2 family member BOK is widely expressed and resembles the multi-BH domain proteins BAX and BAK based on its amino acid sequence. The genomic region encoding BOK was reported to be frequently deleted in human cancer and it

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