Reactive species
Human;Mouse
Applications
WB;IHC;IF;ELISA
Antibody type
Monoclonal antibodies
Protein name
Calreticulin
Immunogen
Synthetic peptide corresponding to aa (EEEDVPGQAKDELC) of human Calreticulin, conjugated to KLH.
Specificity
Calregulin Monoclonal Antibody detects endogenous levels of Calregulin protein.
Constitute
Ascitic fluid containing 0.03% sodium azide,0.5% BSA, 50%glycerol.
Dilution rate
Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/200 - 1/1000. Immunofluorescence: 1/200 - 1/1000. ELISA: 1/10000. Not yet tested in other applications.
Purification process
Affinity purification
Other name
CALR; CRTC; Calreticulin; CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP; grp60
Background
Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is almost identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. Calreticulin binds to antibodies in certain sera of systemic lupus and Sjogren patients which contain anti-Ro/SSA antibodies, it is highly conserved among species, and it is located in the endoplasmic and sarcoplasmic reticulum where it may bind calcium. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin can inhibit the binding of androgen receptor to its
Function
caution:Was originally (PubMed:2332496) thought to be the 52 kDa Ro autoantigen.,domain:Associates with PDIA3 through the tip of the extended arm formed by the P-domain.,domain:Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity.,domain:The interaction with glycans occurs through a binding site in the globular lectin domain.,domain:The zinc binding sites are localized to the N-domain.,function:Molecular calcium binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts
