Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

HMGA1 Human

High Mobility Group AT-Hook 1 Human Recombinant

HMGA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-107 a.a.) and having a molecular mass of 12.7kDa (Molecular weight on SDS-PAGE will appear higher).
HMGA1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20897
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

HMGA2 Human

High Mobility Group AT-Hook 2 Human Recombinant

HMGA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (1-109 a.a) and having a molecular mass of 12.8kDa.
HMGA2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20980
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

HMGB1 Human

High-Mobility Group Box 1 Human Recombinant

HMG1 Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 223 amino acids and having a molecular mass of 26 kDa.
The HMGB-1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21059
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

HMGB1 Human, Sf9

High-Mobility Group Box 1 Human Recombinant, Sf9

HMG1 Human Recombinant fused to an 8 aa His-Tag at C-terminus produced in baculovirus insect cells is a single, glycosylated, polypeptide chain (amino acids 1-215) containing 223 amino acids and having a molecular mass of 25kDa. The HMGB1 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21124
Source

Sf9 Insect Cells.

Appearance
Sterile Filtered colorless solution.

HMGB2 Human

High-Mobility Group Box 2 Human Recombinant

HMGB2 Human Recombinant produced in Baculovirus is a single polypeptide chain containing 232 amino acids (1-209) and having a molecular mass of 26.4 kDa.
The HMGB2 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21199
Source
Baculovirus.
Appearance
Sterile Filtered colorless solution.

HMGB3 Human

High-Mobility Group Box 3 Human Recombinant

HMGB3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-180) and having a molecular mass of 22.8kDa.
HMGB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21267
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

HMGN1 Human

High-Mobility Group Nucleosome Binding Domain 1 Human Recombinant

HMGN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids (1-100 a.a.) and having a molecular mass of 11.7 kDa. HMGN1 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Shipped with Ice Packs
Cat. No.
BT21335
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

HMGN3 Human

High Mobility Group Nucleosomal Binding Domain 3 Human Recombinant

HMGN3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77 a.a) and having a molecular mass of 10.8 kDa.
HMGN3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21391
Source
Escherichia Coli.
Appearance
Sterile filtered 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.

© Copyright 2024 Thebiotek. All Rights Reserved.