- PA1-903 - Invitrogen Antibodies CALR antibody

Submitted references Insulin Treatment Reduces Susceptibility to Atrial Fibrillation in Type 1 Diabetic Mice.

Maria Z, Campolo AR, Scherlag BJ, Ritchey JW, Lacombe VA
Frontiers in cardiovascular medicine 2020;7:134

Glial Growth Factor 2 Regulates Glucose Transport in Healthy Cardiac Myocytes and During Myocardial Infarction via an Akt-Dependent Pathway.

Shoop S, Maria Z, Campolo A, Rashdan N, Martin D, Lovern P, Lacombe VA
Frontiers in physiology 2019;10:189

Diabetes Alters the Expression and Translocation of the Insulin-Sensitive Glucose Transporters 4 and 8 in the Atria.

Maria Z, Campolo AR, Lacombe VA
PloS one 2015;10(12):e0146033

mTOR-Controlled Autophagy Requires Intracellular Ca(2+) Signaling.

Decuypere JP, Kindt D, Luyten T, Welkenhuyzen K, Missiaen L, De Smedt H, Bultynck G, Parys JB
PloS one 2013;8(4):e61020

Bilateral acute pyogenic conjunctivitis with iritis induced by unilateral topical application of bacterial peptidoglycan muramyl dipeptide in adult rabbits.

Langford MP, Foreman BD, Srur L, Ganley JP, Redens TB
Experimental eye research 2013 Nov;116:324-36

Gestational exposure to diethylstilbestrol alters cardiac structure/function, protein expression and DNA methylation in adult male mice progeny.

Haddad R, Kasneci A, Mepham K, Sebag IA, Chalifour LE
Toxicology and applied pharmacology 2013 Jan 1;266(1):27-37

Ins(1,4,5)P3 receptor-mediated Ca2+ signaling and autophagy induction are interrelated.

Decuypere JP, Welkenhuyzen K, Luyten T, Ponsaerts R, Dewaele M, Molgó J, Agostinis P, Missiaen L, De Smedt H, Parys JB, Bultynck G
Autophagy 2011 Dec;7(12):1472-89

Comparative proteomics profiling of a phospholamban mutant mouse model of dilated cardiomyopathy reveals progressive intracellular stress responses.

Gramolini AO, Kislinger T, Alikhani-Koopaei R, Fong V, Thompson NJ, Isserlin R, Sharma P, Oudit GY, Trivieri MG, Fagan A, Kannan A, Higgins DG, Huedig H, Hess G, Arab S, Seidman JG, Seidman CE, Frey B, Perry M, Backx PH, Liu PP, MacLennan DH, Emili A
Molecular & cellular proteomics : MCP 2008 Mar;7(3):519-33

Cardiac mitochondrial connexin 43 regulates apoptosis.

Goubaeva F, Mikami M, Giardina S, Ding B, Abe J, Yang J
Biochemical and biophysical research communications 2007 Jan 5;352(1):97-103

Localization of the iron transport proteins Mobilferrin and DMT-1 in the duodenum: the surprising role of mucin.

Simovich M, Hainsworth LN, Fields PA, Umbreit JN, Conrad ME
American journal of hematology 2003 Sep;74(1):32-45

The ferrireductase paraferritin contains divalent metal transporter as well as mobilferrin.

Umbreit JN, Conrad ME, Hainsworth LN, Simovich M
American journal of physiology. Gastrointestinal and liver physiology 2002 Mar;282(3):G534-9

C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells.

Ogden CA, deCathelineau A, Hoffmann PR, Bratton D, Ghebrehiwet B, Fadok VA, Henson PM
The Journal of experimental medicine 2001 Sep 17;194(6):781-95

Interactions of HLA-B27 with the peptide loading complex as revealed by heavy chain mutations.

Harris MR, Lybarger L, Myers NB, Hilbert C, Solheim JC, Hansen TH, Yu YY
International immunology 2001 Oct;13(10):1275-82

Association of ERp57 with mouse MHC class I molecules is tapasin dependent and mimics that of calreticulin and not calnexin.

Harris MR, Lybarger L, Yu YY, Myers NB, Hansen TH
Journal of immunology (Baltimore, Md. : 1950) 2001 Jun 1;166(11):6686-92

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

Calreticulin inhibits repetitive intracellular Ca2+ waves.

Camacho P, Lechleiter JD
Cell 1995 Sep 8;82(5):765-71

Calreticulin inhibits repetitive intracellular Ca2+ waves.

Camacho P, Lechleiter JD
Cell 1995 Sep 8;82(5):765-71

Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms.

Wada I, Imai S, Kai M, Sakane F, Kanoh H
The Journal of biological chemistry 1995 Sep 1;270(35):20298-304

No comments: Submit comment

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 1 shows a Western blot of calreticulin on HeLa cell extract using Product # PA1-903.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 2 shows a Western blot of calreticulin (transfected and endogenous levels) on HEK cell microsomes using Product # PA1-903.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis was performed on membrane enriched extracts (30 µg lysate) of MCF7 (Lane 1), MDA-MB-231 (Lane 2), HeLa (Lane 3), K-562 (Lane 4), Jurkat (Lane 5) and A549 (Lane 6). The blot was probed with Chicken Anti-Calreticulin Polyclonal Antibody (Product # PA1-903, 1:2000 dilution) and detected by chemiluminescence using Goat anti-Chicken IgY (H+L) Secondary Antibody, HRP conjugate (Product # A16054, 0.4 µg/mL, 1:2500 dilution). A 55 kDa band corresponding to Calreticulin was observed across the cell lines tested. Known quantity of protein samples were electrophoresed using Novex®NuPAGE®4-12 % Bis-Tris gel (Product # NP0321BOX), XCell SureLock Electrophoresis System (Product # EI0002) and Novex® Sharp Pre-Stained Protein Standard (Product # LC5800). Resolved proteins were then transferred onto a nitrocellulose membrane with iBlot® 2 Dry Blotting System (Product # IB21001). The membrane was probed with the relevant primary and secondary Antibody using iBind Flex Western Starter Kit (Product # SLF2000S). Chemiluminescent detection was performed using Pierce™ ECL Western Blotting Substrate (Product # 32106).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Fig 1 Regional heterogeneity of the insulin-sensitive GLUT4 and GLUT8 in the healthy myocardium. Higher total protein expression of A) GLUT4 and lower B) GLUT8 content in the healthy atrial compared to ventricular myocytes. Top panels: representative Western blot from total lysate of isolated rat myocytes; calsequestrin (CLSQ) was used as a loading control; representative bands were obtained from the same membrane. Bottom panels: Mean +- SE of total GLUT protein content (values expressed relative to atria; n = 6/group); * P

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Fig 2 Analysis of the downstream insulin signaling pathways in the healthy atria. A) Insulin stimulates phosphorylation of Akt at s473 and Th308 site in atrial myocytes. Top panel: representative Western blot from total lysate of isolated rat atrial myocytes incubated with (0.01muM) and without (basal) insulin; calsequestrin (CLSQ) was used as a loading control. Bottom panel: Mean +- SE of protein expression (values expressed relative to basal; n = 5/group); # P

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 3 Rapamycin reduces the ER Ca 2+ -leak rate. A-B) Western-blot analysis for luminal Ca 2+ -binding proteins in HeLa cells treated with the indicated concentrations of rapamycin (Rapa) for 5 h: calreticulin (CRT) (A) and BiP/Grp78 (BiP) (B). Upper panels: representative Western blots; lower panels: quantification of the protein/GAPDH ratio ( n = 4). C) Western-blot analysis for SERCA2 in HeLa cells treated with the indicated concentrations of rapamycin for 5 h. Upper panels: representative Western blots; lower panel: quantification of the SERCA2/GAPDH ratio ( n = 4). D) Representative plot showing the decrease in ER 45 Ca 2+ content (logarithmic scale) in a Ca 2+ -free efflux medium without ATP as a function of time in permeabilized HeLa cells pretreated for 5 h with 1 uM rapamycin or with DMSO. The passively bound Ca 2+ was determined by loading the cells with 45 Ca 2+ in the presence of 10 uM of the Ca 2+ ionophore A23187 and then subtracted from the stored 45 Ca 2+ . The ER Ca 2+ -leak rate can be estimated as the rate of decline of the ER 45 Ca 2+ -store content as a function of time. E) Quantification of the mean 45 Ca 2+ -store content at the beginning of the measurement (t 0 ) ( n = 5). F) Quantification of the mean slope of the curve in D after transformation to a linear scale, which is a measure of the 45 Ca 2+ -leak rate ( n = 5). * p

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Fig 4 Alteration of the trafficking of the insulin-sensitive GLUTs in the diabetic atria. Decreased atrial A) GLUT4 and B) GLUT8 content during type 1 diabetes (T1Dx). Top panels: representative Western blot from crude membrane extract of perfused mouse atria, calsequestrin (CLSQ) was used as a loading control. Bottom panels: Mean +- SE of GLUT protein content (values expressed relative to control; n = 7-8/group). Type 1 diabetes decreased C) GLUT4 and D) GLUT8 trafficking to the atrial cell surface. Top panels: representative Western blot. Bottom panels: Mean +- SE of cell surface GLUT protein content (values expressed relative to control; n = 4-5/group). Majority of E) GLUT4 and F) GLUT8 is intracellular under basal conditions (mean +- SE, values expressed relative to control labeled, n = 5/group). Methods: Intact perfused mouse hearts were photolabeled with bio-LC-ATB-BGPA to determine the amount of cell surface (L: labeled fraction) and intracellular (UL: unlabeled fraction) content. T1Dx: type 1 diabetic; Con: control; * P

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Fig 5 Intact insulin signaling pathway in the atria of insulin-deficient diabetic animals. Type 1 diabetes (T1 Dx) did not alter A) Akt or B) AS160 phosphorylation in the atria . Top panels: representative Western blot from total lysate of mouse atria; calsequestrin (CLSQ) was used as a loading control. Bottom panels: Mean +- SE of protein expression (values expressed relative to control; n = 4-5/group). Insulin stimulates C) GLUT4 and D) GLUT8 trafficking to the atrial cell surface in type 1 diabetic (T1 Dx) subjects . Top panels: representative Western blot. Bottom panels: Mean +- SE of cell surface GLUT protein content (values expressed relative to control basal labeled; n = 4-6/group). Methods: Intact mouse hearts were perfused with and without insulin, and photolabeled with bio-LC-ATB-BGPA to determine the amount of cell surface (L: labeled fraction) and intracellular (UL: unlabeled fraction) content. T1Dx: type 1 diabetic; *P

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 3 Alterations in glucose transporter (GLUT) trafficking in the atria of insulin-deficient type 1 diabetic (T1Dx) animals were rescued by in vivo insulin treatment. Total expression of (A) GLUT4 and (B) GLUT8 in the atria of the T1Dx, insulin-treated type 1 diabetic (T1Dx+Insulin), and control (Con) animals. Top panels: representative Western blot from total lysate; loading control: calsequestrin (CLSQ). Bottom Panels: Mean +- SE of total GLUT protein content, normalized to calsequestrin (values normalized to respective controls). Methods: Western blotting. Control: n = 4, T1Dx: n = 3, and T1Dx+Ins: n = 4. Atrial cell surface (C) GLUT4 and (D) GLUT8 protein expression in T1Dx, T1Dx+Insulin, and control animals. Top panels: representative Western blot. Bottom Panels: Mean +- SE of cell surface GLUT protein content (values normalized to controls); Control: n = 4, T1Dx: n = 4, and T1Dx+Ins: n = 5. Methods: biotinylated photolabeling technique in the intact perfused mouse heart. L, Labeled (cell surface fraction); UL, Unlabeled (intracellular fraction). # P < 0.05 vs. Control, * P < 0.05 vs. T1Dx. Statistical test: 1-way ANOVA, two-tailed t -test.

PA1-903

Antibody data