MAX Human

MYC Associated Factor X Human Recombinant
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Description

Introduction to the MAX Gene

The MAX gene in humans encodes the MAX transcription factor, which is crucial for various cellular processes. It belongs to the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. The MAX protein forms homodimers with itself and heterodimers with other transcription factors like Myc, Mad, Mxl1, and Mxd proteins .

Function of the MAX Gene

The MAX transcription factor plays a significant role in regulating gene expression by forming dimers that bind to specific DNA sequences known as E-boxes. These dimers can either activate or repress gene transcription, depending on the composition of the dimer. For instance, the Myc/Max heterodimer is involved in promoting cell proliferation, while the Mad/Max heterodimer can induce apoptosis .

Clinical Relevance of the MAX Gene

The MAX gene has been implicated in several diseases. Mutations in the MAX gene have been associated with hereditary pheochromocytoma and small cell lung cancer (SCLC). In SCLC, mutations in MAX are mutually exclusive with alterations in Myc and BRG1, suggesting a complex interplay between these genes in cancer development .

Research Findings on MAX Dimerization

Recent studies have focused on modulating MAX dimerization as a therapeutic strategy. For example, the compound KI-MS2-008 has been identified as a small molecule that stabilizes the MAX homodimer, reducing Myc protein levels and Myc-regulated transcripts. This approach shows promise in suppressing cancer cell growth and tumor formation .

Implications for Future Research

Understanding the role of MAX in transcriptional regulation and its interactions with other proteins can provide insights into developing targeted therapies for diseases involving MAX dysregulation. Further research is needed to explore the full potential of modulating MAX dimerization in a clinical context.

Data Table: Interactions of the MAX Protein

Interacting ProteinFunction
MycPromotes cell proliferation
MadInduces apoptosis
Mxl1Forms heterodimers with MAX
Mxd proteinsCompetes with Myc for MAX binding
MNTTranscriptional repressor
MSH2DNA mismatch repair protein
MXD1Transcriptional repressor
MXI1Transcriptional repressor
MYCL1Myc-like protein
N-MycNeuroblastoma-derived Myc protein
SPAG9Sperm-associated antigen 9
TEAD1Transcriptional enhancer factor

References

  1. MAX (gene) - Wikipedia. Available at: https://en.wikipedia.org/wiki/MAX_(gene)

  2. Stabilization of the Max Homodimer with a Small Molecule. Available at: https://pubmed.ncbi.nlm.nih.gov/30880155/

Product Specs

Introduction
MAX protein belongs to the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It forms both homodimers with itself and heterodimers with other proteins like Mad, Mxi1, and Myc. Myc, known for its role in cell proliferation, differentiation, and apoptosis, is considered an oncoprotein. Both MAX homodimers and heterodimers bind to a specific DNA sequence called the E box. The dynamic interplay between these different dimer forms allows for intricate control of gene expression. Unlike Myc, whose levels fluctuate significantly during the cell cycle, MAX remains stable and is present in higher amounts compared to Myc.
Description
Recombinant human MAX protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 168 amino acids (specifically, amino acids 1 to 160). It has a molecular weight of 19.3 kDa. An 8-amino acid His-Tag is fused to the C-terminus of the MAX protein to facilitate purification, which is achieved through standard chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
Human MAX protein is supplied in a solution containing 20mM Tris-HCl at a pH of 8, 1mM DTT (a reducing agent), and 10% glycerol (a cryoprotectant).
Stability
For short-term use (2-4 weeks), the solution can be stored at 4°C. For extended storage, it's recommended to freeze the solution at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein like HSA or BSA at a concentration of 0.1%. It's important to minimize repeated cycles of freezing and thawing to maintain protein integrity.
Purity
The purity of the MAX protein is greater than 90%, as assessed by SDS-PAGE analysis.
Synonyms
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
Source
Escherichia Coli.
Amino Acid Sequence
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH.

Q&A

What is the MAX gene and how does it function in human cells?

The MAX gene (myc-associated factor X) encodes the MAX transcription factor in humans. This protein contains basic helix-loop-helix and leucine zipper motifs, placing it in the bHLHZ family of transcription factors .

Methodological approach:
Researchers studying MAX typically employ a combination of techniques:

  • Chromatin immunoprecipitation (ChIP) to identify DNA binding patterns

  • Co-immunoprecipitation to detect protein-protein interactions

  • Gene expression analysis following MAX manipulation

  • Structural biology approaches to characterize binding domains

MAX functions by forming homodimers with other MAX proteins or heterodimers with transcription factors including Mad, Mxl1, and Myc. These dimers compete for binding to E-box sequences in gene promoters, creating a sophisticated regulatory system affecting diverse gene targets .

What protein interactions does MAX participate in and how do these regulate transcription?

MAX engages in multiple protein interactions that collectively regulate gene transcription through competitive binding mechanisms.

Methodological approach:
To identify and characterize these interactions, researchers should:

  • Employ proteomics approaches including mass spectrometry

  • Conduct sequential ChIP experiments to determine co-occupancy

  • Use fluorescence-based interaction assays in live cells

  • Perform domain mapping to identify critical interaction surfaces

Research findings demonstrate that MAX interacts with numerous proteins including:

  • Myc family proteins (c-Myc, N-Myc, MYCL1)

  • MNT and MXD1 transcriptional regulators

  • MSH2 DNA repair protein

  • MXI1 transcriptional repressor

  • SPAG9 scaffold protein

  • TEAD1 transcription factor

  • Transformation/transcription domain-associated protein

These interactions regulate transcription through competition for MAX binding, differential cofactor recruitment, and altered DNA binding specificity. The rearrangement of dimers (switching between Mad:Max, Max:Myc, etc.) enables precise control over diverse gene expression programs .

How do MAX gene mutations contribute to cancer development and progression?

MAX gene mutations play significant roles in multiple cancer types, particularly hereditary pheochromocytoma and small cell lung cancer (SCLC), through distinct molecular mechanisms.

Methodological approach:
Investigating MAX's role in cancer requires integrated approaches:

  • Whole-genome or targeted sequencing of patient samples

  • CRISPR-engineered cell lines modeling specific mutations

  • Patient-derived xenografts for in vivo studies

  • Transcriptome and proteome profiling before/after MAX restoration

Research findings indicate that:

  • In hereditary pheochromocytoma, MAX mutations act as tumor suppressor mutations

  • In SCLC, MAX gene inactivation occurs mutually exclusively with alterations in MYC and BRG1 genes

  • BRG1 regulates MAX expression through direct recruitment to the MAX promoter region

  • Depletion of BRG1 significantly impairs growth specifically in MAX-deficient cells, creating a synthetic lethal interaction

Genetic AlterationCancer TypeMutual ExclusivityFunctional Consequence
MAX inactivationSCLCMutually exclusive with MYC and BRG1 alterationsDisrupts transcriptional regulation
MAX mutationPheochromocytomaN/AActs as tumor suppressor
BRG1 depletion in MAX-deficient cellsSCLCCreates synthetic lethalitySeverely impairs cell growth

What methodologies best capture the dual role of MAX in cell proliferation versus apoptosis?

Studying MAX's opposing roles in cell proliferation and apoptosis requires sophisticated approaches that can distinguish between these cellular outcomes.

Methodological approach:
Researchers should consider:

  • Temporal gene expression systems:

    • Inducible MAX expression (Tet-On/Off)

    • Time-course transcriptomics

    • Pulse-chase experiments tracking protein dynamics

  • Functional genomics approaches:

    • CRISPR-engineered MAX variants

    • Pooled genetic screens identifying synthetic interactions

    • Systematic partner protein manipulation

  • Single-cell techniques:

    • scRNA-seq to capture transcriptional heterogeneity

    • Live-cell imaging with proliferation/apoptosis reporters

    • Mass cytometry for multi-parameter cellular analysis

Research findings demonstrate that MAX homodimers and different heterodimers can promote either cell proliferation or apoptosis depending on cellular context and available partners . MAX must dimerize to be biologically active, and its transcriptionally active forms can drive opposing cellular fates, highlighting the need for context-specific experimental designs.

How do organizational members anthropomorphize AI systems in workplace settings?

Anthropomorphization involves attributing human characteristics and social roles to AI technologies, significantly influencing how they are integrated into organizational settings.

Methodological approach:
Researchers should employ:

  • Semi-structured interviews capturing language used to describe AI

  • Ethnographic observation of human-AI interactions

  • Discourse analysis examining pronoun usage and descriptions

  • Analysis of written and verbal communications about AI systems

Research findings from a workplace case study of an anthropomorphized AI called "Max" reveal:

  • Managers referred to Max using human terms like "junior colleague," "team member," and attributed learning capabilities: "He is learning"

  • Employees also anthropomorphized Max but with more negative human attributes: "Max is quite stupid," "a beginner," "needing supervision"

  • Anthropomorphization occurred despite Max being merely "an algorithm without physical or visual form"

This anthropomorphization creates expectations that influence technology adoption and can amplify existing organizational dynamics.

How does hierarchical position influence perception of and interaction with AI systems?

Organizational hierarchy significantly shapes how individuals perceive and interact with AI systems, creating distinct patterns of engagement and resistance.

Methodological approach:
To investigate this phenomenon, researchers should:

  • Conduct comparative analysis across organizational tiers

  • Employ power-sensitive research designs

  • Analyze decision-making processes about AI implementation

  • Examine resource allocation for AI training and integration

Research findings demonstrate clear hierarchical differences:

  • Managers viewed AI positively, focusing on future potential: "Max is our junior colleague. He does these [booking] tasks faster. And our employees can do something else in the meantime"

  • Employees emphasized present limitations: "Max is quite stupid, and he is just a beginner"

  • Managers expressed frustration with employee resistance: "I'm amazed that people just won't do this small thing"

  • Employees asserted their expertise: "We are knowledgeable and can recommend how to work with robots"

These hierarchical differences create fundamental tensions in AI implementation that require careful management and inclusive design processes.

What theoretical frameworks best explain collective affects around anthropomorphized AI?

Understanding collective affects around anthropomorphized AI requires sophisticated frameworks that capture the interplay between technology, human emotions, and organizational dynamics.

Methodological approach:
Researchers should consider:

  • Affect theory frameworks:

    • Concepts like "affective atmospheres" and "circulation"

    • Tracking affects across organizational boundaries

    • Analyzing non-verbal emotional expressions

  • Socio-material theoretical approaches:

    • Actor-network theory for human-AI assemblages

    • Boundary object analysis of AI mediation

    • Material agency alongside human agency

  • Longitudinal research designs:

    • Tracking affective shifts through implementation phases

    • Analyzing critical incidents and turning points

    • Documenting evolving anthropomorphization practices

Research findings from the Max case study led to the conceptualization of a "circle of mixed collective affects" where "human affects were extended to include an artificially intelligent 'colleague'" . This theoretical innovation explains how affectively charged organizational groups extend affects to include affectively inert technology, creating group-level patterns that transcend individual responses.

How can researchers measure AI systems as amplifiers of existing organizational tensions?

AI systems frequently function as amplifiers of pre-existing organizational tensions rather than simply creating new conflicts, requiring specialized methodologies to capture this amplification effect.

Methodological approach:
Effective research designs include:

  • Pre-post implementation comparative analyses

  • Multi-stakeholder tension mapping across organizational levels

  • Critical discourse analysis of communications about AI systems

  • Process tracing methodologies documenting tension amplification

Research findings demonstrate how the AI system "Max" amplified pre-existing tensions:

  • Researchers identified conflicts between managers and employees that predated AI implementation

  • The AI system made these tensions more visible: "conflicts... were hidden from view"

  • Max became a focal point for expressing broader dissatisfaction: "Now, with the introduction of all these Maxes, our voices need to be heard"

Analytical CategoryInductively Generated MeaningsHermeneutic Principles ApplicationCross-checkingResearcher Reflexivity
AI as amplifier of human discontentManagers and employees expressed different views of Max, reflecting deeper organizational conflictsInitially hidden tensions became visible through discussions about MaxExpanded analysis to include views across management levelsTeam discussions about interpretations of circulating affects

By conceptualizing AI as an "amplifier of human discontent," researchers can better understand how these technologies surface and intensify existing organizational tensions .

Product Science Overview

Structure and Classification

MAX contains a basic helix-loop-helix (bHLH) domain, which is essential for its function as a transcription factor. This domain allows MAX to form homodimers and heterodimers with other family members, including Mad, Mxi1, and Myc . The protein is highly conserved across species, indicating its fundamental role in cellular processes.

Expression Patterns and Tissue Distribution

MAX is ubiquitously expressed in various tissues, with high levels observed in the brain, heart, and lung. Lower levels are found in the liver, kidney, and skeletal muscle . This widespread expression pattern underscores its importance in multiple physiological processes.

Biological Functions

MAX primarily functions as a transcriptional regulator. It forms dimers that bind to specific DNA sequences known as E-boxes, influencing the transcription of target genes . The interaction between MAX and Myc is particularly significant, as Myc is an oncoprotein involved in cell proliferation, differentiation, and apoptosis . By forming heterodimers with Myc, MAX modulates the transcriptional activity of Myc, thereby impacting various cellular processes.

Modes of Action

The homodimers and heterodimers formed by MAX compete for binding to E-box sequences in the DNA . This competition creates a complex system of transcriptional regulation, where the balance between different dimer forms determines the transcriptional outcome. Additionally, MAX may repress transcription by recruiting chromatin remodeling complexes that contain histone methyltransferase activity .

Regulatory Mechanisms

The activity of MAX is regulated at multiple levels, including its expression, dimerization, and interaction with other proteins. Unlike Myc, which is tightly regulated throughout the cell cycle, MAX is relatively stable and abundant . This stability allows MAX to serve as a consistent regulatory partner for Myc and other bHLHZ family members.

Recombinant Production

Recombinant human MAX protein is typically produced in Escherichia coli (E. coli) or baculovirus-insect cells . The recombinant protein is often fused with tags such as polyhistidine or GST to facilitate purification. These recombinant forms are used in various research applications to study the function and regulation of MAX.

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