Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

CALM2 Human

Calmodulin-2 Human Recombinant

Recombinant CALM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 16 kDa.
CALM2 is purified by conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT2268
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CALM2 Human 135 a.a

Calmodulin-2 135 a.a. Human Recombinant

CALM2 Human Recombinant full length protein expressed in E.coli, containing 135 amino acids and having a Molecular Weight of approximately 16 kDa. 

Shipped with Ice Packs
Cat. No.
BT2383
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

CALML3 Human

Calmodulin Like 3 Human Recombinant

CALML3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-149 a.a.) and having a molecular mass of 19kDa.
CALML3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2498
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CALML5 Human

Calmodulin Like 5 Human Recombinant

CALML5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-146) containing 155 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 17.0kDa (calculated). 

Shipped with Ice Packs
Cat. No.
BT2593
Source
Escherichia Coli.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

Calmodulin, also known as calcium-modulated protein, is a highly conserved, multifunctional calcium-binding messenger protein found in the cytoplasm of all eukaryotic cells . It belongs to a family of proteins that includes troponin C, another essential calcium-binding protein involved in muscle contraction . Calmodulin is encoded by multiple genes in humans: CALM1, CALM2, and CALM3, located on chromosomes 14, 2, and 19, respectively .

Biological Properties

Calmodulin is a small protein composed of 148 amino acid residues and has a molecular weight of approximately 16.7 kDa . It consists of two globular domains connected by a flexible central linker, with each domain containing a pair of EF-hand motifs that bind calcium ions . Calmodulin can bind up to four calcium ions, which induces a conformational change that allows it to interact with various target proteins .

Expression Patterns and Tissue Distribution: Calmodulin is ubiquitously expressed in all eukaryotic cells and is highly conserved across species . It is abundant in the cytoplasm and plays a critical role in numerous cellular processes .

Biological Functions

Calmodulin mediates a wide range of calcium-dependent cellular processes, including inflammation, metabolism, apoptosis, smooth muscle contraction, intracellular movement, short-term and long-term memory, and the immune response . It acts as an intermediary protein that senses calcium levels and relays signals to various calcium-sensitive enzymes, ion channels, and other proteins .

Role in Immune Responses and Pathogen Recognition: Calmodulin is involved in the regulation of immune responses by modulating the activity of various immune cells and signaling pathways . It plays a role in pathogen recognition by interacting with proteins involved in the immune response .

Modes of Action

Calmodulin functions by binding to calcium ions, forming a Ca2+/calmodulin complex that interacts with target proteins . This interaction can activate or inhibit the target proteins, leading to downstream signaling cascades . Calmodulin can bind to a wide variety of proteins, including kinases, phosphatases, and ion channels, due to its structural flexibility and the predominantly hydrophobic nature of its binding sites .

Binding Partners and Downstream Signaling Cascades: Calmodulin interacts with over 300 target proteins, including Ca2+/calmodulin-dependent protein kinases (CAMKs), myosin light chain kinase, and other enzymes involved in cellular processes . These interactions regulate various signaling pathways and cellular functions .

Regulatory Mechanisms

The expression and activity of calmodulin are regulated by multiple mechanisms, including transcriptional regulation and post-translational modifications .

Transcriptional Regulation: The genes encoding calmodulin (CALM1, CALM2, and CALM3) are regulated by various transcription factors that respond to cellular signals .

Post-Translational Modifications: Calmodulin can undergo several post-translational modifications, such as phosphorylation, acetylation, methylation, and proteolytic cleavage, which modulate its activity and interactions with target proteins .

Applications in Biomedical Research

Calmodulin plays a critical role in numerous physiological processes, making it a valuable target for biomedical research .

Diagnostic Tools and Therapeutic Strategies: Calmodulin antagonists are used in research to study calcium signaling pathways and their role in diseases . These antagonists have potential therapeutic applications in conditions such as hypertension, congestive heart failure, arrhythmia, and gastrointestinal disorders .

Protein Purification: Calmodulin is used in affinity purification techniques to isolate calmodulin-binding proteins, facilitating the study of protein-protein interactions and cellular signaling pathways .

Role in the Life Cycle

Calmodulin is essential throughout the life cycle, from development to aging and disease .

Development: During development, calmodulin mediates processes such as cell cycle progression, cytoskeletal assembly, and cell motility .

Aging and Disease: Calmodulin continues to play a critical role in maintaining cellular functions and responding to physiological changes throughout life . Dysregulation of calmodulin activity is associated with various diseases, including neurodegenerative disorders, cardiovascular diseases, and cancer .

© Copyright 2024 Thebiotek. All Rights Reserved.