Alternative Name(s):

Class E basic helix-loop-helix protein 36 ;bHLHe36Transcriptional activator MondoA

Species: (Organism)

Homo sapiens (Human)

Gene Names:

MLXIP

Tag info:

N-terminal 6xHis-SUMO-tagged

Target Protein AA Sequence:

MDEQGCEHTSRTEDPFIQPTDFGPSEPPLSVPPPISPVLPLVPPPATALNPPAPPTFHQPQKFAGVNKAPSVITHTASATLTHDAPATTFSQSQGLVITTHHPAPSAAPCGLALSPVTRPPQPRLTFVHPKPVSLTGGRPKQPHKIVPAPKPEPVSLVLKNARIAPGEPGGETQCGAPPDPEGCFPIPKAFKLVTTTTTLVCTCMRTHIHLNETKVS

Expression Region:

1-217aa

Subcellular Location:

Cytoplasm, Nucleus, Mitochondrion outer membrane

Tissue Specificity:

Widely expressed in adult tissues. Most abundant in skeletal muscle.

Protein Length:

Full Length of Isoform 5

Pathway:

Mol. Weight:

38.8 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Transcription

Function:

Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation.

Involvement in disease:

Relevance:

Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Reference:

A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex.Eilers A.L., Sundwall E., Lin M., Sullivan A.A., Ayer D.E.Mol. Cell. Biol. 22:8514-8526(2002)