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Centrin

Manufactured by Merck Group
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Centrin is a laboratory equipment product manufactured by the Merck Group. It is a high-precision centrifuge designed for a wide range of scientific applications. The core function of Centrin is to separate components of a sample based on their density and sedimentation rate.

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Lab products found in correlation

Lsm 700, by Zeiss (4 mentions) Cep164, by Santa Cruz Biotechnology (3 mentions) Cep164, by Proteintech (2 mentions) Alexa fluor 488, by Thermo Fisher Scientific (2 mentions) Acetylated α tubulin, by Santa Cruz Biotechnology (2 mentions) Gelvatol, by Thermo Fisher Scientific (2 mentions) Par6α, by Abcam (2 mentions) Ninein, by BioLegend (2 mentions) Prolong diamond, by Thermo Fisher Scientific (2 mentions) Elyra ps 1, by Zeiss (2 mentions) Vectashield, by Vector Laboratories (2 mentions) β actin, by Proteintech (2 mentions) β actin, by Merck Group (2 mentions) Pericentrin, by Abcam (1 mentions) Centrin, by Santa Cruz Biotechnology (1 mentions) Gt335, by Adipogen (1 mentions) Yl1 2, by Bio-Rad (1 mentions) Ab4448, by Abcam (1 mentions) Fluorescein isothiocyanate (fitc), by Jackson ImmunoResearch (1 mentions) Gtu 88, by Merck Group (1 mentions)

Spelling variants of this product

Mouse anti-centrin (8 citations) Anti-centrin (4 citations) Mouse α-Centrin (CrCen clone 20H5, (2 citations) Centrin 1 (2 citations) Anti-centrin 20H5 (2 citations) Mouse anti-centrin clone 20H5 (2 citations)

8 protocols using centrin

1

Immunofluorescence Microscopy of Cytoskeletal Proteins

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Primary antibodies used were against glutamylated tubulin (1:800 [tissue sections] and 1:500 [cell lines]; mouse; GT335; AdipoGen), pericentrin (1:250; rabbit; ab4448; Abcam), centrin (1:500; rabbit; N-17; Santa Cruz Biotechnology, Inc.), centrin (1:500; mouse; 20H5; EMD Millipore), A647-conjugated centrin (1:500; mouse; 20H5; EMD Millipore), γ-tubulin (1:500; mouse; GTU88; Sigma-Aldrich), α-tubulin (1:50; rat; YL1/2; AbD Serotec), p53 (1:100; mouse; DO-1; EMD Millipore), E-cadherin (1:30; rabbit; Cell Signaling Technology), and CP110 (1:250; rabbit; Jiang et al., 2012 (link)). The secondary antibodies FITC, Cy5, and rhodamine red (1:50 [tissue sections] and 1:200 [cell lines]; Jackson ImmunoResearch Laboratories, Inc.) as well as Alexa Fluor 488 and 647 (1:500 [cell lines]; Thermo Fisher Scientific) were also used.
Lopes C.A., Mesquita M., Cunha A.I., Cardoso J., Carapeta S., Laranjeira C., Pinto A.E., Pereira-Leal J.B., Dias-Pereira A., Bettencourt-Dias M, & Chaves P. (2018). Centrosome amplification arises before neoplasia and increases upon p53 loss in tumorigenesis. The Journal of Cell Biology, 217(7), 2353-2363.
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2

Immunofluorescence Staining of Centrosomal Proteins

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The following commercial antibodies were used: CEP290 (C-terminus), Bethyl Laboratory, A301-659A; acetylated α-tubulin, Santa Cruz, sc-23950; Centrin, pan-Centrin antibody from EMD Millipore, 04-1624, raised against Chlamydomonas Centrin and reported to recognize all mouse Centrin isoforms 1-4 (41, 84); CEP164, Proteintech, 22227-1-AP; CEP164, Santa Cruz, sc-515403; MKS3 (cultured cells) Proteintech, 13975-1-AP; Atto488-Tuba1, Antibodies-online.com, ABIN1169085. Antibodies were used at a concentration of 10 μg/mL, with the exception of Atto488-Tuba1 which was used at a concentration of 7.5 μg/mL. Secondary antibodies used were F(ab’)2-goat anti-rabbit IgG Alexa 488, F(ab’)2-goat anti-mouse IgG Alexa 555, and F(ab’)2-goat anti-mouse IgG Alexa 647 (Thermo Fisher, 8 μg each).
Boulton I.C., Yost M.K., Anderson J.E, & Cornelissen C.N. (2000). Identification of Discrete Domains within Gonococcal Transferrin-Binding Protein A That Are Necessary for Ligand Binding and Iron Uptake Functions. Infection and Immunity, 68(12), 6988-6996.
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3

Immunofluorescence Staining Protocols

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The following commercial antibodies were used CEP290, Bethyl Laboratory, A301-659A; acetylated a-tubulin, Santa Cruz, sc-23950; NPHP5, Proteintech, 15747-1-AP; Centrin, EMD Millipore, 04-1624; CEP164, Proteintech, 22227-1-AP; CEP164, Santa Cruz, sc-515403; wheat germ agglutinin (WGA)-A647, Molecular Probes, W32466; Atto488-Tuba1, Antibodies-online.com, ABIN1169085. Rat anti-CEP290 antibody was a gift from the Swaroop laboratory. Mouse anti-1D4 was generated in house. For SIM and confocal imaging, antibodies were used at a concentration of 1 μg/150 μL. For STORM, antibodies were used at a concentration of 10 μg/mL, with the exception of rat anti-CEP290 antibody and Atto488-Tuba1 which were used at concentrations of 5 μg/mL and 7.5 μg/mL, respectively.
Potter V.L., Moye A.R., Robichaux M.A., & Wensel T.G. (2020). Superresolution microscopy reveals photoreceptor-specific subciliary location and function of Cep290.
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4

Immunofluorescence Imaging of Centrosomal Proteins

Cited 3 times
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Antibodies used included: Mib1 (M5948; Sigma-Aldrich, St. Louis, MO), PCM1 (H262; Santa Cruz, Santa Cruz, CA), Cep131 (A301-415A; Bethyl Laboratories, Montgomery, TX), Cep90 (Kim and Rhee, 2011 (link)), Ki-67 (ab15580; Abcam, Cambridge, MA), GT335 (AG-20B-0020-C100; Adipogen, Switzerland), BBS4 (Kim et al., 2012 (link)), Rab11 (71–5300; Life Technologies, Carlsbad, CA), Rab8 (a gift from J. Peranen, University of Helsinki, Helsinki, Finland and 610844; BD Biosciences, San Jose, CA), α-tubulin (T5168; Sigma-Aldrich), Cep290 (A301-659A; Bethyl Laboratories), Ofd1 (a gift from J. Reiter, University of California, San Francisco, USA; Singla et al., 2010 (link)), Talpid3 (Kobayashi et al., 2014 (link)), Myc (sc-40; Santa Cruz), Flag (F3165; Sigma-Aldrich), centrin (04–1624; Millipore, Billerica, MA), GFP (G1544; Santa Cruz), Cep164 (a gift from Eva Lee, University of California, USA), IFT88 (13967-1-AP; Proteintech, Chicago, IL).
Wang L., Lee K., Malonis R., Sanchez I, & Dynlacht B.D. (2016). Tethering of an E3 ligase by PCM1 regulates the abundance of centrosomal KIAA0586/Talpid3 and promotes ciliogenesis. eLife, 5, e12950.
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5

Immunofluorescence Staining of Cellular Components

Cited 1 time
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Cells were fixed in ice-cold methanol for 3 min, permeabilized in
blocking buffer (2.5% BSA or FBS, 0.1% TritonX-100,
0.03% NaN3 in DPBS). Primary and secondary antibodies were
diluted in blocking buffer and incubated for 2 h at RT. Coverslips were mounted
using Gelvatol, or Prolong Diamond (ThermoFisher Scientific) and imaged with the
inverted confocal microscope Zeiss LSM700. Images were processed with
ImageJ/FIJI. For 3D-structured illumination microscopy (SIM) (Fig. 1e), WT and KO FEFs were plated on 1.5-mm
coverslips and immunostained as above. Coverslips were mounted with Vectashield
(Vectorlabs). 3D-SIM imaging was performed on a Zeiss Elyra PS.1 microscope
equipped with a 100x/1.40 oil objective lens. Exciting light was directed
through a movable optical grating to generate a fine-striped interference
pattern on the same plane. Z-stacks of 15 optical sections with a step size of
0.1 μm were acquired to generate images in maximum intensity projection.
The epitope of the ASPM (216-1) antibody43 (link), NDNYGLNQDLESES, is located prior to the TALEN target
site. The following antibodies were used at 1:100 – 1:2000: Centrin
(Millipore 20H5), Par6α (SCBT sc-14405), Par6α (Abcam ab180159),
β-actin (Proteintech 20536-1-AP), ASPM (SCBT sc-98903), ASPM (gift from
J. Bond, 216-1), Ninein (Biolegend Poly6028), aPKCζ (SCBT sc-216).
Johnson M.B., Sun X., Kodani A., Borges-Monroy R., Girskis K.M., Ryu S.C., Wang P.P., Patel K., Gonzalez D.M., Woo Y.M., Yan Z., Liang B., Smith R.S., Chatterjee M., Coman D., Papademetris X., Staib L.H., Hyder F., Mandeville J.B., Grant P.E., Im K., Kwak H., Engelhardt J.F., Walsh C.A, & Bae B.I. (2018). Aspm knockout ferret reveals an evolutionary mechanism governing cerebral cortical size. Nature, 556(7701), 370-375.
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6

Immunofluorescence Staining of Cellular Components

Cited 1 time
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Cells were fixed in ice-cold methanol for 3 min, permeabilized in
blocking buffer (2.5% BSA or FBS, 0.1% TritonX-100,
0.03% NaN3 in DPBS). Primary and secondary antibodies were
diluted in blocking buffer and incubated for 2 h at RT. Coverslips were mounted
using Gelvatol, or Prolong Diamond (ThermoFisher Scientific) and imaged with the
inverted confocal microscope Zeiss LSM700. Images were processed with
ImageJ/FIJI. For 3D-structured illumination microscopy (SIM) (Fig. 1e), WT and KO FEFs were plated on 1.5-mm
coverslips and immunostained as above. Coverslips were mounted with Vectashield
(Vectorlabs). 3D-SIM imaging was performed on a Zeiss Elyra PS.1 microscope
equipped with a 100x/1.40 oil objective lens. Exciting light was directed
through a movable optical grating to generate a fine-striped interference
pattern on the same plane. Z-stacks of 15 optical sections with a step size of
0.1 μm were acquired to generate images in maximum intensity projection.
The epitope of the ASPM (216-1) antibody43 (link), NDNYGLNQDLESES, is located prior to the TALEN target
site. The following antibodies were used at 1:100 – 1:2000: Centrin
(Millipore 20H5), Par6α (SCBT sc-14405), Par6α (Abcam ab180159),
β-actin (Proteintech 20536-1-AP), ASPM (SCBT sc-98903), ASPM (gift from
J. Bond, 216-1), Ninein (Biolegend Poly6028), aPKCζ (SCBT sc-216).
Johnson M.B., Sun X., Kodani A., Borges-Monroy R., Girskis K.M., Ryu S.C., Wang P.P., Patel K., Gonzalez D.M., Woo Y.M., Yan Z., Liang B., Smith R.S., Chatterjee M., Coman D., Papademetris X., Staib L.H., Hyder F., Mandeville J.B., Grant P.E., Im K., Kwak H., Engelhardt J.F., Walsh C.A, & Bae B.I. (2018). Aspm knockout ferret reveals an evolutionary mechanism governing cerebral cortical size. Nature, 556(7701), 370-375.
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7

Cell Cycle Regulation Assay

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The following chemicals were used: RO3306 (Axon MedChem), Okadaic Acid sodium salt (A.G. Scientifix), Thymidine and 2’-Deoxycytidine hydrate (Santa Cruz Biotechnology). The following antibodies were used; BUB1B (BubR1) (#4116), Cyclin B1 (#12231), Phospho-(Ser) CDK Substrate (#2324), pCdc2-Tyr15 (CDK1-Y15) (#9111), Plk1 (#4535), Aurora B (#3094) and Lamin A/C (#4777) (Cell Signaling Technologies), Securin (ab3306) (Abcam), Cyclin A (sc-596), Cdc2 (CDK1) (sc-137034), Mad2 (sc-47747), Cdc25C (sc-327) (Santa Cruz Biotechnology), centrin (#04–1624) (Millipore) and β-actin (A5441) (Sigma-Aldrich). Anti-Greatwall was obtained as previously described (Vigneron et al., 2009), and monoclonal β-Tubulin hybridoma antibody was a generous donation from Dr Natalie Morin (CRBM, France).
McCloy R.A., Rogers S., Caldon C.E., Lorca T., Castro A, & Burgess A. (2014). Partial inhibition of Cdk1 in G2 phase overrides the SAC and decouples mitotic events. Cell Cycle, 13(9), 1400-1412.
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8

Antibody-Based Protein Detection Techniques

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Antibodies against the following were used for western blotting (WB), immunofluorescence (IF) and immunoprecipitation (IP):
• α-tubulin (DM1A; Sigma-Aldrich, T6199 mouse; 1:2500 IF, methanol; 1:5000 WB)
• β-actin (Sigma-Aldrich, clone AC-15 mouse; 1:10,000 WB)
• Centrin (Millipore, (20H5) Mouse;1:5000 IF, methanol)
• CREST (Europa Bioproducts, FZ90C-CS1058, Human, 1:2000, methanol)
• HA tag (Roche Diagnostics, 3F10 rat; 1:200 IF, formaldehyde; 1:1000 WB)
• PCNA (Abcam, ab18197, rabbit, 1:2000 IF, methanol)
• PeriCentrin (Covance, PRB-432C; rabbit, 1:2000 IF, methanol)
• PLK4 (Sigma-Aldrich, clone 6H5 mouse, 1:1000 IF, methanol; 1:500 WB)
• Tiam1 (Bethyl Laboratories, rabbit, A300-099A, 1:1000 WB)
Porter A.P., White G., Ogg E., Whalley H.J., & Malliri A. (2020). The RAC1 activator Tiam1 regulates centriole duplication through controlling PLK4 levels.
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