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Calumenin Human

Calumenin Human Recombinant

Calumenin Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (20-315) and having a molecular mass of 35kDa. Calumenin is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT3650
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Calumenin Human, His

Calumenin Human Recombinant, His Tag

Recombinant Human Calumenin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (20-315 a.a) and having a molecular mass of 37.2 kDa. Calumenin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3713
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
Definition and Classification

Calumenin, encoded by the CALU gene, is a calcium-binding protein localized in the endoplasmic reticulum (ER). It is a member of the EF-hand superfamily, specifically the CREC family, which includes Cab45, reticulocalbin, Erc-55, and calumenin .

Biological Properties

Key Biological Properties: Calumenin is involved in calcium ion binding and protein folding within the ER. It contains six EF-hand motifs, one potential N-glycosylation site, and a C-terminal ER retention signal .

Expression Patterns: Calumenin mRNA is ubiquitously expressed in human tissues, including the endometrium, smooth muscle tissue, and various arteries .

Tissue Distribution: It is highly expressed in stromal cells of the endometrium, smooth muscle tissue, and various arteries, indicating its widespread role in different tissues .

Biological Functions

Primary Biological Functions: Calumenin functions as a molecular chaperone, assisting in protein folding and sorting within the ER. It also plays a role in calcium cycling, vascular calcification, thrombosis, cell migration, and apoptosis .

Role in Immune Responses and Pathogen Recognition: Calumenin has been implicated in immune responses, particularly in the regulation of interferon signals and inflammatory pathways .

Modes of Action

Mechanisms with Other Molecules and Cells: Calumenin interacts with various ER proteins, including sarco-endoplasmic reticulum calcium ATPase (SERCA) pumps, and regulates ER stress by modulating the expression of ER-stress proteins .

Binding Partners: It binds to proteins involved in calcium signaling and γ-carboxylation processes .

Downstream Signaling Cascades: Calumenin influences signaling pathways such as MYC and KRAS, while activating interferon and inflammatory pathways .

Regulatory Mechanisms

Transcriptional Regulation: The expression of calumenin is regulated at the transcriptional level, with increased expression observed in various cancers .

Post-Translational Modifications: Calumenin undergoes post-translational modifications, including glycosylation, which may affect its function and localization .

Applications

Biomedical Research: Calumenin is studied for its role in cancer progression, particularly in lung adenocarcinoma and clear cell renal cell carcinoma .

Diagnostic Tools: Its expression levels can serve as biomarkers for certain cancers, aiding in diagnosis and prognosis .

Therapeutic Strategies: Targeting calumenin may offer therapeutic potential in treating cancers and other diseases associated with ER stress and calcium dysregulation .

Role in the Life Cycle

Development to Aging and Disease: Calumenin plays a crucial role throughout the life cycle, from development to aging. It is involved in muscle contraction-relaxation processes and has been linked to various diseases, including cancer and cardiovascular diseases .

Calumenin’s multifaceted roles in cellular processes and disease mechanisms make it a significant protein of interest in biomedical research and therapeutic development.

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