Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations
- Immunocytochemistry [1]
- Other assay [1]
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Validation data
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- Product number
- 33-3700 - Provider product page
- Provider
- Invitrogen Antibodies
- Product name
- Ankyrin B Monoclonal Antibody (2.2)
- Antibody type
- Monoclonal
- Antigen
- Synthetic peptide
- Reactivity
- Human, Mouse, Rat
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- 2.2
- Vial size
- 100 µg
- Concentration
- 0.5 mg/mL
- Storage
- -20°C
Submitted references PERM1 interacts with the MICOS-MIB complex to connect the mitochondria and sarcolemma via ankyrin B.
Coupling of the Na+/K+-ATPase to Ankyrin B controls Na+/Ca2+ exchanger activity in cardiomyocytes.
Activation of glial FGFRs is essential in glial migration, proliferation, and survival and in glia-neuron signaling during olfactory system development.
Roles of specific membrane lipid domains in EGF receptor activation and cell adhesion molecule stabilization in a developing olfactory system.
Structural requirements for interaction of sodium channel beta 1 subunits with ankyrin.
Bock T, Türk C, Aravamudhan S, Keufgens L, Bloch W, Rozsivalova DH, Romanello V, Nogara L, Blaauw B, Trifunovic A, Braun T, Krüger M
Nature communications 2021 Aug 12;12(1):4900
Nature communications 2021 Aug 12;12(1):4900
Coupling of the Na+/K+-ATPase to Ankyrin B controls Na+/Ca2+ exchanger activity in cardiomyocytes.
Skogestad J, Aronsen JM, Tovsrud N, Wanichawan P, Hougen K, Stokke MK, Carlson CR, Sjaastad I, Sejersted OM, Swift F
Cardiovascular research 2020 Jan 1;116(1):78-90
Cardiovascular research 2020 Jan 1;116(1):78-90
Activation of glial FGFRs is essential in glial migration, proliferation, and survival and in glia-neuron signaling during olfactory system development.
Gibson NJ, Tolbert LP, Oland LA
PloS one 2012;7(4):e33828
PloS one 2012;7(4):e33828
Roles of specific membrane lipid domains in EGF receptor activation and cell adhesion molecule stabilization in a developing olfactory system.
Gibson NJ, Tolbert LP, Oland LA
PloS one 2009 Sep 29;4(9):e7222
PloS one 2009 Sep 29;4(9):e7222
Structural requirements for interaction of sodium channel beta 1 subunits with ankyrin.
Malhotra JD, Koopmann MC, Kazen-Gillespie KA, Fettman N, Hortsch M, Isom LL
The Journal of biological chemistry 2002 Jul 19;277(29):26681-8
The Journal of biological chemistry 2002 Jul 19;277(29):26681-8
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Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Immunofluorescent analysis of Ankyrin B was done on 70% confluent log phase SHSY5Y cells. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.25% Triton™ X-100 for 10 minutes, and blocked with 5% BSA for 1 hour at room temperature. The cells were labeled with Ankyrin B Mouse monoclonal Antibody (Product # 33-3700) at 1 µg/mL in 1% BSA and incubated for 3 hours at room temperature and then labeled with Alexa Fluor 488 Rabbit Anti-Mouse IgG Secondary Antibody (Product # A-11059) at a dilution of 1:400 for 30 minutes at room temperature (Panel a: green). Nuclei (Panel b: blue) were stained with SlowFade® Gold Antifade Mountant with DAPI (Product # S36938). F-actin (Panel c: red) was stained with Alexa Fluor 594 Phalloidin (Product # A12381). Panel d is a merged image showing cytoplasmic localization. Panel e shows no primary antibody control. The images were captured at 20X magnification.
Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Fig. 6 PERM1 associates with ankyrin B and the interaction with the MICOS-MIB complex is dependent on the transmembrane helix. a PERM1 interacts with ANKB, as indicated by immunoprecipitation of FLAG-tagged Perm1 and HA-tagged ankyrin-B in TREx-293 cells stably expressing Perm1 -FLAG. Protein lysates were immunoprecipitated with anti-FLAG beads and anti-HA beads and immunoblotted with anti-FLAG and anti-HA antibodies. b Immunohistochemical staining of soleus muscle revealed co-localization of PERM1 (red) with ANKB (green). Scale, 50 um. c Mean fractional intensity of ANKB signals in bins 1-6 from Perm1 -/- and wild-type soleus muscle fibers. ANKB staining intensity was reduced at subsarcolemmal sites and increased within interfibrillar mitochondria in Perm1 -/- muscles compared to wild-type controls ( n = 4 mice per group, 2299 quantified fibers). Box plot (c) represents the median, 25th, and 75th percentiles, maximum and minimum are connected through whiskers. Outliers are defined as Q 1 -1.8 IQR and Q 3 +1.8 IQR. (c) unpaired two-sided Mann-Whitney U -test. Source data are provided as Source Data file.