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Mouse Anti-ACTN1 Recombinant Antibody (V2-12507) (CBMAB-0997-CN)


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Published Data
Mouse Anti-ACTN1 Recombinant Antibody (910301) (CBMAB-0997-CN) in Simple Western
Detection and quantification of SI protein. (Panels A) and (Panels B) show the concentration-dependence of SI and α-actinin signals (Panel C) using automated capillary Western blotting of Caco-2/TC7 lysates. (Panel D) shows Caco-2/TC7 cell surface protein fraction purified after biotinylation from cells cultured on 6-well Transwell filters in glucose or sucrose for 21 days and treated on the apical side for the final 3 days with 1.5 mg/mL OLE. (Panel E) shows the total cellular SI, relative to α-actinin with data normalised to the glucose control and presented as mean ± SEM with n = 12, analysed in duplicate runs. The size was determined relative to a protein standard ladder for SI in the total lysate relative to α-actinin (F), normalised and presented as mean ± SEM with n = 24. * p < 0.05, ** p < 0.01, *** p < 0.001 from ANOVA followed by Tukey's post-hoc test. There was no change in the α-actinin loading control between the groups. ...View More
Pyner, A., Chan, S. Y., Tumova, S., Kerimi, A., & Williamson, G. (2019). Indirect chronic effects of an oleuropein-rich olive leaf extract on sucrase-isomaltase in vitro and in vivo. Nutrients, 11(7), 1505.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
V2-12507
Antibody Isotype
IgG2b
Application
WB

Basic Information

Immunogen
E. coli-derived recombinant human alpha -Actinin 1 Asn272-Thr500.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB0.2 µg/ml
Simple Western2 µg/ml

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

Format
Lyophilized
Buffer
PBS, trehalose
Preservative
None
Concentration
LYOPH
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
Actinin Alpha 1
Introduction
Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. This is a bundling protein. F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures.
Entrez Gene ID
Human83
Mouse109711
Rat81634
UniProt ID
HumanP12814
MouseQ7TPR4
RatQ9Z1P2
Alternative Names
Actinin Alpha 1; Alpha-Actinin Cytoskeletal Isoform; F-Actin Cross-Linking Protein; Non-Muscle Alpha-Actinin-1; Actinin 1 Smooth Muscle; Alpha-Actinin-1; BDPLT15;
Function
F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
Biological Process
Actin filament bundle assembly
Actin filament network formation
Actin filament organization
Focal adhesion assembly
Negative regulation of cellular component movement
Platelet degranulation
Platelet formation
Platelet morphogenesis
Regulation of apoptotic process
Cellular Location
Cytoskeleton; Cell membrane; Z line; Cell junction. Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures.
Involvement in disease
Bleeding disorder, platelet-type 15 (BDPLT15): An autosomal dominant form of macrothrombocytopenia. Affected individuals usually have no or only mild bleeding tendency, such as epistaxis. Laboratory studies show decreased numbers of large platelets and anisocytosis, but the platelets show no in vitro functional abnormalities.
More Infomation

O'Sullivan, L. R., Ajaykumar, A. P., Dembicka, K. M., Murphy, A., Grennan, E. P., & Young, P. W. (2020). Investigation of calmodulin‐like and rod domain mutations suggests common molecular mechanism for α‐actinin‐1‐linked congenital macrothrombocytopenia. FEBS letters, 594(1), 161-174.

Xie, G. F., Zhao, L. D., Chen, Q., Tang, D. X., Chen, Q. Y., Lu, H. F., ... & Chen, Z. (2020). High ACTN1 is associated with poor prognosis, and ACTN1 silencing suppresses cell proliferation and metastasis in Oral squamous cell carcinoma. Drug Design, Development and Therapy, 14, 1717.

Cetinkaya, A., Berge, B., Sen-Hild, B., Troidl, K., Gajawada, P., Kubin, N., ... & Richter, M. (2020). Radixin relocalization and nonmuscle α-Actinin expression are features of remodeling cardiomyocytes in adult patients with dilated cardiomyopathy. Disease Markers, 2020.

Blondelle, J., Tallapaka, K., Seto, J. T., Ghassemian, M., Clark, M., Laitila, J. M., ... & Lange, S. (2019). Cullin-3–dependent deregulation of ACTN1 represents a pathogenic mechanism in nemaline myopathy. JCI insight, 4(10).

Eich, F., Nonis, D. F., Sen, N. E., Nowock, J., & Auburger, G. (2019). Ataxin-2 Binds Alpha-Actinin-1.

Yang, X., Pang, Y., Zhang, J., Shi, J., Zhang, X., Zhang, G., ... & Fu, L. (2019). High expression levels of ACTN1 and ACTN3 indicate unfavorable prognosis in acute myeloid leukemia. Journal of Cancer, 10(18), 4286.

Faleschini, M., Melazzini, F., Marconi, C., Giangregorio, T., Pippucci, T., Cigalini, E., ... & Noris, P. (2018). ACTN 1 mutations lead to a benign form of platelet macrocytosis not always associated with thrombocytopenia. British journal of haematology, 183(2), 276-288.

Kanhai, D., Mulder, R., Ploos van Amstel, H. K., Schutgens, R., Lukens, M., & Tamminga, R. Y. (2018). Familial macrothrombocytopenia due to a double mutation in cis in the alpha‐actinin 1 gene (ACTN1), previously considered to be chronic immune thrombocytopenic purpura. Pediatric blood & cancer, 65(12), e27418.

Milanini, J., Fayad, R., Partisani, M., Lecine, P., Borg, J. P., Franco, M., & Luton, F. (2018). EFA6 proteins regulate lumen formation through α-actinin 1. Journal of cell science, 131(3), jcs209361.

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For research use only. Not intended for any clinical use.

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