Anti-MAX Antibody Picoband®

Overview

This antibody is intended for detection of MAX in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.

Vendor notes: Boster Bio Anti-MAX Antibody Picoband® catalog # A03239. Tested in ELISA, Flow Cytometry, IF, ICC, WB applications. This antibody reacts with Human, Mouse. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Antibody format: Rabbit Polyclonal Rabbit IgG
• Immunogen / epitope context: E. coli-derived human MAX recombinant protein (Position: A30-R106). (reported region: A30-R106).
• Molecular weight context: reported MW: 19-21 kDa; calculated MW: nan
• Reactivity: Human,Mouse
• Applications: ELISA, Flow Cytometry, IF, ICC, WB

As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.

Biological background

MYC associated factor X. MAX (Max protein), also called Myc-associated factor x, is the most conserved dimerization component of the MYC-MAX-MXD1 network of basic helix-loop-helix leucine zipper (bHLHZ) transcription factors that regulate cell proliferation, differentiation, and apoptosis. The conservation of the MAX sequence is particularly high in the bHLHZ domain, which is involved in protein-protein interactions and DNA binding. The MAX gene is located on chromosome 14q23 by fluorescence in situ chromosomal hybridization. Both quasisymmetric heterodimers resemble the symmetric MAX homodimer, albeit with marked structural differences in the coiled-coil leucine zipper regions that explain preferential homo- and heteromeric dimerization of these 3 evolutionarily related DNA-binding proteins. MAX acts as a classic tumor suppressor gene. Normal lymphocytes from patients showed absence of methylation of the MAX promoter and biallelic expression of MAX, which ruled out an imprinting-mediated effect on MAX expression. The ability of these cells to divide, differentiate, and apoptose in the absence of Max demonstrated for the first time that these processes can occur via Max- and possibly Myc-independent mechanisms. Functional note: Transcription regulator. Forms a sequence-specific DNA- binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Reported localization: Nucleus. Cell projection, dendrite. Expression/tissue context: High levels found in the brain, heart and lung while lower levels are seen in the liver, kidney and skeletal muscle.

Research relevance and current trends

• Cancer Susceptibility: Researchers commonly examine how MAX relates to this theme using model systems and orthogonal readouts.
• 2339: Researchers commonly examine how MAX relates to this theme using model systems and orthogonal readouts.
• Domain Families: Researchers commonly examine how MAX relates to this theme using model systems and orthogonal readouts.

Common research applications

• Western blotting: compare relative MAX levels across conditions; band patterns may reflect isoforms and processing.
• IF/ICC: evaluate subcellular localization and co-localization patterns; signal can depend on fixation/permeabilization and epitope accessibility.
• Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.
• ELISA-compatible use: when applicable, interpret signal as relative abundance across sample sets with consistent handling and dilution strategy.

Notes for experimental interpretation

• Specificity notes: No cross reactivity with other proteins.
• Cross-reactivity: No cross-reactivity with other proteins.
• Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
• Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.