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ANTI-CALRETICULIN

Basic information Safety Supplier Related

ANTI-CALRETICULIN Basic information

Product Name:
ANTI-CALRETICULIN
Synonyms:
  • Anti-Calreticulin antibody produced in rabbit
  • Anti-CALR (AB2) antibody produced in rabbit
  • Anti-Calreticulin antibody produced in chicken
  • Anti-CALR (AB1) antibody produced in rabbit
  • ANTI-CALRETICULIN, HUMAN
  • ANTI-CALRETICULIN, HUMAN (MOUSE)
  • ANTI-CALRETICULIN MOUSE MAB
  • ANTI-CALRETICULIN
MW:
0
Product Categories:
  • Alphabetical Index
  • Antibodies for Intracellular Calcium Signaling
  • Antibodies to Calcium-Associated ProteinsCell Biology
  • Antibodies to Cell and Organelle Proteins
  • C1 to CA
  • Functional Profiling of Stem Cells
  • Antibodies against Proteins/Bioactives/Markers/ReceptorsCell Biology
  • Antibodies to ER and Golgi ProteinsAntibodies
  • Stem Cell Biology
Mol File:
Mol File
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ANTI-CALRETICULIN Chemical Properties

storage temp. 
-20°C
form 
buffered aqueous solution
biological source
rabbit
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Safety Information

Hazard Codes 
Xn
Risk Statements 
21/22
Safety Statements 
36/37
WGK Germany 
-
Storage Class
12 - Non Combustible Liquids

MSDS

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ANTI-CALRETICULIN Usage And Synthesis

Uses

Anti-Calreticulin antibody produced in rabbit has been used in:

  • immunoblotting
  • immunofluorescence
  • immunocytochemistry{91
  • immunoprecipitation

General Description

The gene for calreticulin (CALR) is located on the human chromosome 19p13.13. The encoded protein is a predominantly conserved calcium-binding chaperone, which is localized primarily to the lumen of the endoplasmic reticulum (ER). Calreticulin comprises three domains, a globular N-domain, a proline-rich P-domain, and a highly acidic C-domain.

Biochem/physiol Actions

Calreticulin facilitates transient interaction with newly synthesized cellular and extracellular proteins for folding and assembling in the endoplasmic reticulum (ER) before its localization to the cytosol or cell surface. Calreticulin acts as a lectin-like chaperone binding oligosaccharide residues of newly synthesized N-linked glycoproteins and misfolded proteins. It is believed to play a critical role in quality control processes during protein synthesis and folding and calcium (Ca2+) homeostasis. Increased expression of calreticulin increases the Ca2+ storage capacity of the ER. It also appears to modulate store-operated Ca2+-influx and to alter Ca2+ transport by the sarcoplasmic/ER Ca2+-adenosine triphosphatase (ATPase) (SERCA). Overexpression of calreticulin results in increased sensitivity of HeLa cells to drug-induced apoptosis. However, increased resistance to apoptosis has been observed in calreticulin-deficient cells.

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