Recombinant Proteins

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LBP
CEA
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Bax
BID

S100A8 Human, His

S100 Calcium Binding Protein A8 Human Recombinant, His Tag

Recombinant Human S100A8, expressed in E. coli, has a molecular weight of 12.08 kDa. It comprises 103 amino acids of the human S100A8 protein with a 10-amino acid His tag fused at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT587
Source
Escherichia Coli.

S100A8 Human, His-Myc

S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant

Recombinantly produced in E. coli, the human S100A8 protein is a single, non-glycosylated polypeptide chain comprising 127 amino acids (residues 1-93), with a molecular weight of 14.5 kDa. The protein features a 24 amino acid His-tag at the N-terminus and a 10 amino acid Myc-tag at the C-terminus.
Shipped with Ice Packs
Cat. No.
BT672
Source
Escherichia Coli.
Appearance
The appearance of this sterile filtered solution is colorless.

S100P Human, His

S100 Calcium Binding Protein P Human Recombinant, His Tag

Recombinantly produced in E. coli, S100P Human is a single, non-glycosylated polypeptide chain comprising 115 amino acids (1-95a.a.) with a molecular weight of 12.6 kDa. This S100P protein features a 20 amino acid His tag at the N-terminus and is purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT1920
Source
Escherichia Coli.
Appearance
A clear, colorless, and sterile-filtered solution.

S100Z Human

S100 Calcium Binding Protein Z Human Recombinant

Recombinant Human S100Z, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 119 amino acids (1-99 a.a.). With a molecular weight of 13.7 kDa, it includes a 20 amino acid His-Tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2004
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SNTN Human

Sentan Cilia Apical Structure Protein Human Recombinant

Recombinant Human SNTN, with a 20 amino acid His tag attached at the N-terminus, is produced in E. coli. This single, non-glycosylated polypeptide chain comprises 167 amino acids (1-147a.a.) and has a molecular weight of 18.6 kDa. The purification of SNTN is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2043
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

S100B Human, His

S100 Calcium Binding Protein B Human Recombinant, His Tag

Recombinant human S100B, produced in E. coli, is a non-glycosylated polypeptide chain containing 112 amino acids. This includes an S100B fragment (amino acids 1-92) with a 20 amino acid N-terminal His tag. The total molecular mass is 12.8kDa. S100B is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1122
Source
Escherichia Coli.
Appearance
A clear solution, sterilized by filtration.

S100b Mouse

S100 Calcium Binding Protein B Mouse Recombinant

Recombinant Mouse s100b, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 92 amino acids (1-92 a.a.) with a molecular mass of 10.7 kDa. The s100b protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1245
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

S100b Mouse, His

S100 Calcium Binding Protein B Mouse Recombinant, His Tag

Recombinant Mouse S100B, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 92 amino acids (1-112 a.a.) with a molecular weight of 12.8 kDa. A 20 amino acid His-Tag is fused to the N-terminus of the Mouse S100B protein. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1332
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

S100b Rhesus Macaque

S100 Calcium Binding Protein B Rhesus Macaque Recombinant

S100B Rhesus Macaque Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 91 amino acids with a molecular weight of 10.7 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1428
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder

S100A6 Mouse

S100 Calcium Binding Protein A6 Mouse Recombinant

Produced in E. coli, S100A6 is a single, non-glycosylated polypeptide chain consisting of 109 amino acids (amino acids 1-89). It has a molecular weight of 12.2 kDa.
This S100A6 protein is fused to a 20 amino acid His-tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT198
Source
Escherichia Coli.
Appearance
Sterile Filtered, clear solution.
Definition and Classification

Calcium binding proteins (CaBPs) are a diverse group of proteins that have the ability to bind calcium ions (Ca²⁺) through specific domains known as EF-hand motifs. These proteins play crucial roles in various cellular processes by regulating calcium signaling pathways. CaBPs can be classified into several families based on their structure and function, including calmodulins, troponins, S100 proteins, and annexins.

Biological Properties

Key Biological Properties:

  • Calcium Binding: CaBPs have high affinity for calcium ions, which allows them to act as calcium sensors and buffers.
  • Conformational Changes: Binding of calcium induces conformational changes in CaBPs, enabling them to interact with target proteins.
  • Versatility: CaBPs are involved in a wide range of cellular functions due to their ability to bind calcium and interact with various proteins.

Expression Patterns:

  • CaBPs are ubiquitously expressed in many tissues, but their expression levels can vary significantly depending on the tissue type and physiological conditions.

Tissue Distribution:

  • Calmodulins: Found in almost all eukaryotic cells.
  • Troponins: Predominantly present in cardiac and skeletal muscles.
  • S100 Proteins: Expressed in the brain, heart, and other tissues.
  • Annexins: Widely distributed in various tissues, including the lungs, liver, and kidneys.
Biological Functions

Primary Biological Functions:

  • Signal Transduction: CaBPs play a key role in translating calcium signals into cellular responses.
  • Muscle Contraction: Troponins regulate muscle contraction by controlling the interaction between actin and myosin.
  • Cell Cycle Regulation: Calmodulins are involved in cell cycle progression and division.
  • Neurotransmitter Release: S100 proteins modulate neurotransmitter release in the nervous system.

Role in Immune Responses:

  • CaBPs are involved in the activation and regulation of immune cells, such as T cells and macrophages, by modulating calcium-dependent signaling pathways.

Pathogen Recognition:

  • Certain CaBPs, like S100 proteins, can recognize and bind to pathogen-associated molecular patterns (PAMPs), playing a role in the innate immune response.
Modes of Action

Mechanisms with Other Molecules and Cells:

  • CaBPs interact with a variety of target proteins, including enzymes, ion channels, and structural proteins, to modulate their activity.

Binding Partners:

  • Calmodulins: Bind to and regulate kinases, phosphatases, and other signaling proteins.
  • Troponins: Interact with actin and myosin in muscle fibers.
  • S100 Proteins: Bind to receptors on immune cells and other target proteins.
  • Annexins: Interact with phospholipids and membrane proteins.

Downstream Signaling Cascades:

  • CaBPs initiate and regulate various signaling pathways, such as the calcium/calmodulin-dependent protein kinase (CaMK) pathway, which is involved in processes like memory formation and muscle contraction.
Regulatory Mechanisms

Regulatory Mechanisms that Control Expression and Activity:

  • Transcriptional Regulation: The expression of CaBPs is regulated by transcription factors that respond to cellular signals and environmental cues.
  • Post-Translational Modifications: CaBPs can undergo modifications such as phosphorylation, acetylation, and ubiquitination, which can alter their activity, stability, and interactions with other proteins.
Applications

Biomedical Research:

  • CaBPs are used as markers to study calcium signaling pathways and their role in various diseases, including cancer and neurodegenerative disorders.

Diagnostic Tools:

  • Elevated levels of certain CaBPs, such as troponins, are used as biomarkers for diagnosing myocardial infarction and other cardiac conditions.

Therapeutic Strategies:

  • Targeting CaBPs and their interactions with other proteins is being explored as a potential therapeutic approach for treating diseases like cancer, heart disease, and inflammatory disorders.
Role in the Life Cycle

Role Throughout the Life Cycle:

  • Development: CaBPs are essential for proper embryonic development, particularly in the formation of the nervous system and muscles.
  • Aging: Changes in the expression and function of CaBPs are associated with aging and age-related diseases, such as Alzheimer’s disease and sarcopenia.
  • Disease: Dysregulation of CaBPs is implicated in various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.
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