MAX Human

MYC Associated Factor X Human Recombinant

Cat. No.

BT22885

Source

Escherichia Coli.

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.

Appearance

Sterile filtered colorless solution.

Purity

Greater than 90% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

MAX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

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.

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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MAX Human

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