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M5948

Sigma-Aldrich

Anti-MIB1 (C-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-DAPK-interacting protein 1, Anti-DIP-1, Anti-KIAA1323, Anti-Mindbomb homolog 1, Anti-Ubiquitin ligase mind bomb

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~110 kDa

species reactivity

rat, mouse, human

concentration

~1.0 mg/mL

technique(s)

western blot: 0.5-1 μg/mL using lysates of A549 or PC12 cells.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MIB1(57534)
mouse ... Mib1(225164)
rat ... Mib1(307594)

General description

MIB1 (Mindbomb homology 1) are E3 ubiquitin ligases. It is abundantly expressed in both embryos and adult tissues, whereas MIB2 is highly expressed in adult tissues.
Mindbomb homolog 1 (MIB1) is an ubiquitin ligase which possesses two substrate recognition domains, ankyrin repeats and an amino terminal zinc finger domain.

Immunogen

synthetic peptide corresponding to amino acids 924-939 of human MIB1, conjugated to KLH. The corresponding sequence is identical in rat and mouse.

Application

Anti-MIB1 (C-terminal) antibody produced in rabbit has been used in:immunofluorescence, immunoprecipitation , western blotting immunohistochemistry
Anti-MIB1 (N-terminal) antibody produced in rabbit has been used for immunofluorescence.

Biochem/physiol Actions

MIB1 is critical for mammalian development and cellular differentiation. It also plays a role in neuronal morphogenesis partially through physical interaction with cyclin-dependent kinase 5 (CDK5)/p35. Knockout of MIB1 in mice results in embryonic mortality with many defects observed in somitogenesis, neurogenesis, vasculogenesis and cardiogenesis.
Mindbomb homolog 1 (MIB1) aids in the ubiquitination and internalization of Notch ligands such as the protein δ. It also acts as a positive regulator in the activation of nuclear factor-κB (NF-κB).

Physical form

Solution in 0.01 M phosphate buffered saline, pH7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Differential routing of mindbomb1 via centriolar satellites regulates asymmetric divisions of neural progenitors
Tozer S, et al.
Neuron, 93(3), 542-551 (2017)
Mindbomb 1, an E3 ubiquitin ligase, forms a complex with RYK to activate Wntbeta-catenin signaling
Berndt JD, et al.
The Journal of Cell Biology, 194(5), 737-750 (2011)
Neuronal morphogenesis is regulated by the interplay between cyclin-dependent kinase 5 and the ubiquitin ligase mind bomb 1
Choe EA, et al.
The Journal of Neuroscience, 27(35), 9503-9512 (2007)
Samuel Tozer et al.
Neuron, 93(3), 542-551 (2017-01-31)
Unequal centrosome maturation correlates with asymmetric division in multiple cell types. Nevertheless, centrosomal fate determinants have yet to be identified. Here, we show that the Notch pathway regulator Mindbomb1 co-localizes asymmetrically with centriolar satellite proteins PCM1 and AZI1 at the
Orhi Barroso-Gomila et al.
Nature communications, 14(1), 7656-7656 (2023-11-24)
Hundreds of E3 ligases play a critical role in recognizing specific substrates for modification by ubiquitin (Ub). Separating genuine targets of E3s from E3-interactors remains a challenge. We present BioE3, a powerful approach for matching substrates to Ub E3 ligases

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