SRP2101
Myc-associated factor X (MAX) human
recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
Synonyme(s) :
MGC10775, MGC11225, MGC18164, MGC34679, bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8
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10 μG
540,00 $
540,00 $
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Changer de vue
10 μG
540,00 $
About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.26
540,00 $
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Devis pour commande en gros
Source biologique
human
Produit recombinant
expressed in E. coli
Essai
≥80% (SDS-PAGE)
Forme
frozen liquid
Poids mol.
~19.6 kDa
Conditionnement
pkg of 10 μg
Concentration
250 μg/mL
Couleur
clear colorless
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... MAX(4149)
Description générale
The gene encoding this protein is localized on human chromosome 14q23.[1]
Actions biochimiques/physiologiques
The MAX gene encodes a protein that interacts specifically with the Myc protein to form a heterodimer with high affinity for the specific cognate DNA-binding site of Myc. The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include MAD, MXI1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Substantial evidence has been accumulated over the last years that support the model that Myc/MAX/MAD proteins affect different aspects of cell behavior, including proliferation, differentiation, and apoptosis, by modulating distinct target genes. The unbalanced expression of these genes, e.g. in response to deregulated Myc expression, is most likely an important aspect of Myc`s ability to stimulate tumor formation. It is reported that in vivo transactivation assays suggest that Myc-MAX and MAD-MAX complexes have opposing functions in transcription and that MAX plays a central role in this network of transcription factors. High levels of MAX and stress-induced NFkappaB activation may result in elevated expression of Fas ligand in human lung cancer cells and possibly contribute to Fas ligand-associated immune escape mechanisms.
Forme physique
Clear and colorless frozen liquid solution
Notes préparatoires
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Hypoxia reduces MAX expression in endothelial cells by unproductive splicing
Katrin Kemmerer
Febs Letters, 588 (2014)
Complex MAX Rearrangement in a Family With Malignant Pheochromocytoma, Renal Oncocytoma, and Erythrocytosis
Esther Korpershoek
The Journal of Clinical Endocrinology and Metabolism, 101(2), 453-460 (2016)
Zoltan Wiener et al.
Experimental cell research, 299(1), 227-235 (2004-08-11)
Fas (CD95/APO-1) ligand is a member of the Tumor Necrosis Factor family and a potent inducer of apoptosis. Fas ligand is expressed in activated T cells and represents a major cytotoxic effector mechanism by which T cells kill their target
B Lüscher
Gene, 277(1-2), 1-14 (2001-10-17)
The members of the Myc/Max/Mad network function as transcriptional regulators. Substantial evidence has been accumulated over the last years that support the model that Myc/Max/Mad proteins affect different aspects of cell behavior, including proliferation, differentiation, and apoptosis, by modulating distinct
E M Blackwood et al.
Science (New York, N.Y.), 251(4998), 1211-1217 (1991-03-08)
The myc protooncogene family has been implicated in cell proliferation, differentiation, and neoplasia, but its mechanism of function at the molecular level is unknown. The carboxyl terminus of Myc family proteins contains a basic region helix-loop-helix leucine zipper motif (bHLH-Zip)
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