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Mouse Anti-CAPZB Recombinant Antibody (CBYY-C0944) (CBMAB-C2381-YY)


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Published Data
CBMAB-C2381-YY-1
Mouse Anti-CAPZB Recombinant Antibody (CBYY-C0944) (CBMAB-C2381-YY) in WB
Western blot of wild type (WT) G1E cell lysates after retroviral infection with control shRNA (shControl) or shRNA targeting Capzb mRNA (shCapzb2) stained with anti-sterile alpha motif domain 14 (Samd14), anti-Capzα1, anti-Capzβ, or anti-Hsc70 antibodies. ...View More
Ray, S., Chee, L., Zhou, Y., Schaefer, M. A., Naldrett, M. J., Alvarez, S., ... & Hewitt, K. J. (2022). Functional requirements for a Samd14-capping protein complex in stress erythropoiesis. Elife, 11, e76497.
CBMAB-C2381-YY-2
Mouse Anti-CAPZB Recombinant Antibody (CBYY-C0944) (CBMAB-C2381-YY) in WB
Western blot of WT G1E cell lysates following pulldown with anti-Samd14 or anti-rabbit IgG control antibody. Input corresponds to 5% of immunoprecipitation (IP) lysate. ...View More
Ray, S., Chee, L., Zhou, Y., Schaefer, M. A., Naldrett, M. J., Alvarez, S., ... & Hewitt, K. J. (2022). Functional requirements for a Samd14-capping protein complex in stress erythropoiesis. Elife, 11, e76497.
CBMAB-C2381-YY-3
Mouse Anti-CAPZB Recombinant Antibody (CBYY-C0944) (CBMAB-C2381-YY) in IF
The distribution of phalloidin stained F-actin (red) and of CP visualized by HA-Tag antibody labelling (green) in fixed cells is shown: In the top cells overexpressed CP after induction with 1 µg/ml Doxycyclin (CP Dox, N = 21). In the middle cells were not overexpressing CP but treated with 1 µg/ml Doxycyclin (no CP Dox, N = 10) and in bottom cells contained the expression plasmids but were not treated with Doxycyclin (CP no Dox, N = 21). ...View More
Dürre, K., Keber, F. C., Bleicher, P., Brauns, F., Cyron, C. J., Faix, J., & Bausch, A. R. (2018). Capping protein-controlled actin polymerization shapes lipid membranes. Nature communications, 9(1), 1630.
CBMAB-C2381-YY-4
Mouse Anti-CAPZB Recombinant Antibody (CBYY-C0944) (CBMAB-C2381-YY) in IF
Confocal images of the equatorial vesicle's plane showed the interactions of the contractile actin network (red hot) with the membrane (cyan). At 20 nM CP the network detached from the membrane and was pulled towards the bulk of the vesicle. At 60 nM CP membrane invaginations (insets) emerged from the membrane. At 120 nM CP membrane invaginations (left inset) and fission events (right insets) could be observed. Scale bars are 20 µm. ...View More
Dürre, K., Keber, F. C., Bleicher, P., Brauns, F., Cyron, C. J., Faix, J., & Bausch, A. R. (2018). Capping protein-controlled actin polymerization shapes lipid membranes. Nature communications, 9(1), 1630.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat, Dog, Chicken
Clone
CBYY-C0944
Antibody Isotype
IgG1, κ
Application
IP, WB

Basic Information

Immunogen
Amino acids 162-267 of CapZ-β of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat, Dog, Chicken
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
capping protein (actin filament) muscle Z-line, beta
Entrez Gene ID
832
UniProt ID
P47756
Alternative Names
Caspase 3; Caspase 3, Apoptosis-Related Cysteine Peptidase; Caspase 3, Apoptosis-Related Cysteine Protease; SREBP Cleavage Activity 1; Cysteine Protease CPP32; Protein Yama; EC 3.4.22.56; Apopain; CASP-3;
Function
F-actin-capping proteins bind in a Ca2+-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization.
Biological Process
Actin cytoskeleton organization Source: InterPro
Antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
Barbed-end actin filament capping Source: GO_Central
Blood coagulation Source: Reactome
Cell morphogenesis Source: GO_Central
Cytoskeleton organization Source: UniProtKB
Endoplasmic reticulum to Golgi vesicle-mediated transport Source: Reactome
Negative regulation of filopodium assembly Source: GO_Central
Regulation of cell morphogenesis Source: UniProtKB
Regulation of lamellipodium assembly Source: GO_Central
Cellular Location
Cytoskeleton; Sarcomere
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For research use only. Not intended for any clinical use.

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