Product: CALR Antibody
Catalog: DF6211
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Bovine, Horse, Sheep, Rabbit
Mol.Wt.: 60kD; 48kD(Calculated).
Uniprot: P27797
RRID: AB_2838177

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Reactivity:
Human,Mouse,Rat,Monkey
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%)
Clonality:
Polyclonal
Specificity:
CALR Antibody detects endogenous levels of total CALR.
RRID:
AB_2838177
Cite Format: Affinity Biosciences Cat# DF6211, RRID:AB_2838177.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Autoantigen RO; CALR; CALR protein; CALR_HUMAN; Calregulin; Calreticulin; cC1qR; CRP55; CRT; CRTC; Endoplasmic reticulum resident protein 60; Epididymis secretory sperm binding protein Li 99n; ERp60; FLJ26680; grp60; HACBP; HEL S 99n; RO; Sicca syndrome antigen A (autoantigen Ro; calreticulin); Sicca syndrome antigen A; SSA;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Description:
Calcium is a universal signaling molecule involved in many cellular functions such as cell motility, metabolism, protein modification, protein folding and apoptosis. Calcium is stored in the endoplasmic reticulum (ER), where it is buffered by calcium binding chaperones such as calnexin and calreticulin, and is released via the IP3 Receptor (1). Calreticulin also functions as an ER chaperone that ensures proper folding and quality control of newly synthesized glycoproteins. As such, calreticulin presumably does not alter protein folding but ensures proper timing for efficient folding and subunit assembly. Furthermore, calreticulin retains proteins in non-native conformation within the ER and targets them for degradation (2,3).
Sequence:
MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Rabbit
100
Xenopus
45
Zebrafish
45
Dog
0
Chicken
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P27797 As Substrate

Site PTM Type Enzyme
Y22 Phosphorylation
K24 Sumoylation
K24 Ubiquitination
T34 Phosphorylation
S35 Phosphorylation
K41 Ubiquitination
S44 Phosphorylation
K48 Acetylation
K48 Ubiquitination
S52 Phosphorylation
S53 Phosphorylation
K55 Ubiquitination
Y57 Phosphorylation
K62 Acetylation
K62 Ubiquitination
K64 Acetylation
K64 Ubiquitination
R73 Methylation
Y75 Phosphorylation
S78 Phosphorylation
S80 Phosphorylation
S85 Phosphorylation
C105 S-Nitrosylation
Y109 Phosphorylation
K111 Methylation
K142 Acetylation
K143 Ubiquitination
Y150 Phosphorylation
K151 Ubiquitination
K153 Acetylation
K153 Ubiquitination
K159 Acetylation
K159 Ubiquitination
T169 Phosphorylation
Y172 Phosphorylation
T181 Phosphorylation
Y182 Phosphorylation
S195 Phosphorylation
K206 Acetylation
K206 Ubiquitination
K207 Acetylation
K207 Ubiquitination
K209 Acetylation
K209 Ubiquitination
S214 Phosphorylation
R222 Methylation
T229 Phosphorylation
S231 Phosphorylation
K238 Acetylation
K238 Methylation
Y271 Phosphorylation
Y285 Phosphorylation
Y299 Phosphorylation
S300 Phosphorylation
T333 Phosphorylation
N344 N-Glycosylation
K351 Ubiquitination
R366 Methylation

Research Backgrounds

Function:

Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).

Subcellular Location:

Endoplasmic reticulum lumen. Cytoplasm>Cytosol. Secreted>Extracellular space>Extracellular matrix. Cell surface. Sarcoplasmic reticulum lumen.
Note: Also found in cell surface (T cells), cytosol and extracellular matrix (PubMed:10358038). Associated with the lytic granules in the cytolytic T-lymphocytes.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 and SPACA9 (By similarity). Interacts with TRIM21. Interacts with NR3C1. Interacts with PPIB. Interacts (via P-domain) with PDIA5. Interacts with GABARAP. Interacts with HLA-E-B2M and HLA-G-B2M complexes. Interacts with HLA-F. Interacts with CLCC1.

Family&Domains:

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.

The interaction with glycans occurs through a binding site in the globular lectin domain.

The zinc binding sites are localized to the N-domain.

Associates with PDIA3 through the tip of the extended arm formed by the P-domain.

Belongs to the calreticulin family.

Research Fields

· Cellular Processes > Transport and catabolism > Phagosome.   (View pathway)

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Organismal Systems > Immune system > Antigen processing and presentation.   (View pathway)

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