Recombinant Proteins

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HMGA1 Human

High Mobility Group AT-Hook 1 Human Recombinant

Recombinant HMGA1, of human origin, is produced in E. coli. This results in a single, non-glycosylated polypeptide chain composed of 115 amino acids (specifically, amino acids 1-107). The protein has a molecular mass of 12.7 kDa. However, the molecular weight observed on SDS-PAGE will be higher due to the presence of an 8 amino acid His-tag fused to the C-terminus of HMGA1. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20897
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

HMGA2 Human

High Mobility Group AT-Hook 2 Human Recombinant

Recombinant HMGA2, of human origin, is produced in E.Coli. This non-glycosylated polypeptide chain comprises 117 amino acids (amino acids 1-109), resulting in a molecular weight of 12.8kDa. The HMGA2 protein is fused to an 8 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20980
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

HMGB1 Human

High-Mobility Group Box 1 Human Recombinant

Recombinant human HMG1, fused with a 6X His tag, is produced in E. coli. This non-glycosylated polypeptide chain contains 223 amino acids, resulting in a molecular weight of 26 kDa. The purification of HMGB-1 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21059
Source
Escherichia Coli.
Appearance
White, sterile-filtered powder, lyophilized (freeze-dried).

HMGB1 Human, Sf9

High-Mobility Group Box 1 Human Recombinant, Sf9

Recombinant human HMGB1 protein, expressed in baculovirus-infected insect cells (Sf9), is a single, glycosylated polypeptide chain with a His-tag at the C-terminus. It encompasses amino acids 1-215, resulting in a protein of 223 amino acids with a molecular weight of 25 kDa. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21124
Source

Sf9 Insect Cells.

Appearance
Clear, colorless, and sterile-filtered solution.

HMGB2 Human

High-Mobility Group Box 2 Human Recombinant

This segment details the recombinant production process of HMGB2 protein using Baculovirus, specifying its structure, molecular weight, and purification method.
Shipped with Ice Packs
Cat. No.
BT21199
Source
Baculovirus.
Appearance
This describes the visual characteristics of the supplied HMGB2 protein solution, indicating it as a clear and colorless liquid that has been sterilized through filtration.

HMGB3 Human

High-Mobility Group Box 3 Human Recombinant

Recombinant human HMGB3, expressed in E.coli, is a non-glycosylated polypeptide chain with a molecular weight of 22.8kDa. It consists of 203 amino acids, including a 23 amino acid His-tag at the N-terminus (amino acids 1-180). Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21267
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.

HMGN1 Human

High-Mobility Group Nucleosome Binding Domain 1 Human Recombinant

Recombinant human HMGN1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 108 amino acids. This includes the full HMGN1 sequence (1-100 amino acids) and an 8 amino acid His-tag fused at the C-terminus. The protein has a molecular weight of 11.7 kDa and is purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21335
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

HMGN3 Human

High Mobility Group Nucleosomal Binding Domain 3 Human Recombinant

Recombinant human HMGN3, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 100 amino acids (residues 1-77) with a molecular mass of 10.8 kDa. It includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21391
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.
Definition and Classification

High-Mobility Group (HMG) proteins are a family of non-histone chromosomal proteins that play a crucial role in the regulation of DNA-dependent processes such as transcription, replication, recombination, and DNA repair. They are characterized by their ability to bind to the minor groove of DNA and induce structural changes. HMG proteins are classified into three main subfamilies based on their functional domains:

  • HMGA (High-Mobility Group A): Contains AT-hook motifs that bind to the minor groove of AT-rich DNA sequences.
  • HMGB (High-Mobility Group B): Contains HMG-box domains that facilitate DNA bending and looping.
  • HMGN (High-Mobility Group N): Contains nucleosome-binding domains that interact with nucleosomes and modulate chromatin structure.
Biological Properties

Key Biological Properties: HMG proteins are highly conserved across species and are known for their dynamic interaction with chromatin. They are involved in the regulation of gene expression by altering chromatin structure and facilitating the binding of transcription factors.

Expression Patterns: HMG proteins are ubiquitously expressed in various tissues, with some subtypes showing tissue-specific expression patterns. For example, HMGA proteins are highly expressed in embryonic tissues and rapidly dividing cells.

Tissue Distribution: HMG proteins are found in the nucleus of almost all eukaryotic cells. Their distribution within the nucleus can vary depending on the cell type and the physiological state of the cell.

Biological Functions

Primary Biological Functions: HMG proteins play a pivotal role in the regulation of gene expression by modulating chromatin structure and facilitating the access of transcription factors to DNA. They are also involved in DNA repair, replication, and recombination.

Role in Immune Responses: HMG proteins, particularly HMGB1, act as damage-associated molecular patterns (DAMPs) that are released by stressed or damaged cells. They play a crucial role in the activation of the immune system and the recognition of pathogens.

Pathogen Recognition: HMGB1 can bind to pathogen-associated molecular patterns (PAMPs) and enhance the recognition of pathogens by the immune system. This interaction is essential for the initiation of immune responses against infections.

Modes of Action

Mechanisms with Other Molecules and Cells: HMG proteins interact with a variety of molecules, including DNA, histones, transcription factors, and other chromatin-associated proteins. These interactions are essential for their role in chromatin remodeling and gene regulation.

Binding Partners: HMG proteins have multiple binding partners, including transcription factors such as p53, NF-κB, and steroid hormone receptors. These interactions facilitate the recruitment of transcriptional machinery to specific gene promoters.

Downstream Signaling Cascades: HMG proteins can influence downstream signaling pathways by modulating the expression of target genes. For example, HMGB1 can activate the NF-κB signaling pathway, leading to the production of pro-inflammatory cytokines.

Regulatory Mechanisms

Regulatory Mechanisms that Control Expression and Activity: The expression and activity of HMG proteins are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications.

Transcriptional Regulation: The transcription of HMG genes is regulated by various transcription factors and signaling pathways. For example, the expression of HMGA1 is regulated by the Wnt/β-catenin signaling pathway.

Post-Translational Modifications: HMG proteins undergo various post-translational modifications, such as phosphorylation, acetylation, and methylation. These modifications can influence their DNA-binding affinity, subcellular localization, and interaction with other proteins.

Applications

Biomedical Research: HMG proteins are widely studied in biomedical research due to their role in gene regulation and chromatin dynamics. They are used as markers for studying chromatin structure and function.

Diagnostic Tools: HMG proteins, particularly HMGA and HMGB, are used as diagnostic markers for various cancers. Their expression levels are often correlated with tumor progression and prognosis.

Therapeutic Strategies: Targeting HMG proteins has therapeutic potential in various diseases, including cancer, inflammation, and autoimmune disorders. Inhibitors of HMGB1, for example, are being developed as potential treatments for sepsis and inflammatory diseases.

Role in the Life Cycle

Role Throughout the Life Cycle: HMG proteins play essential roles throughout the life cycle, from development to aging and disease. During development, they regulate the expression of genes involved in cell differentiation and proliferation.

Development: HMG proteins are critical for embryonic development and the regulation of genes involved in cell fate determination. HMGA proteins, for example, are essential for the development of the nervous system and other tissues.

Aging and Disease: The expression and function of HMG proteins can change with aging, leading to alterations in chromatin structure and gene expression. Dysregulation of HMG proteins is associated with various age-related diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases.

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