Calumenin Human, His

Calumenin Human Recombinant, His Tag
Cat. No.
BT3713
Source
Escherichia Coli.
Synonyms
CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Calumenin, found in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR), is a calcium-binding protein vital for ER functions like protein folding and sorting in mammals. Part of the multiple EF-hand proteins (CERC) family, which includes reticulocalbin, ERC-55, and Cab45, calumenin binds seven calcium ions with low affinity and contributes to protein folding and sorting processes within the ER.
Description
Recombinant Human Calumenin, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 317 amino acids (20-315 a.a), has a molecular mass of 37.2 kDa, and features a 20 amino acid His Tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The Calumenin protein is supplied in a buffer of 20mM Tris-HCl at pH 8.0 with 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 90% as determined by SDS-PAGE analysis.
Synonyms
CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MKPTEKKDRV HHEPQLSDKV HNDAQSFDYD HDAFLGAEEA KTFDQLTPEE SKERLGKIVS KIDGDKDGFV TVDELKDWIK FAQKRWIYED VERQWKGHDL NEDGLVSWEE YKNATYGYVL DDPDPDDGFN YKQMMVRDER RFKMADKDGD LIATKEEFTA FLHPEEYDYM KDIVVQETME DIDKNADGFI DLEEYIGDMY SHDGNTDEPE WVKTEREQFV EFRDKNRDGK MDKEETKDWI LPSDYDHAEA EARHLVYESD QNKDGKLTKE EIVDKYDLFV GSQATDFGEA LVRHDEF.

Product Science Overview

Structure and Characteristics

Recombinant human calumenin, particularly the variant with a His tag, is produced using mammalian expression systems, such as HEK 293 cells . This recombinant protein typically has a high purity level, often exceeding 90% as determined by SDS-PAGE . The His tag, usually located at the C-terminus, facilitates purification and detection of the protein .

The recombinant human calumenin protein consists of 303 amino acids and has a predicted molecular mass of approximately 35.9 kDa. However, it migrates as a band of around 46-52 kDa in SDS-PAGE under reducing conditions .

Functional Role

Calumenin plays a crucial role in the calcium homeostasis within the ER. It contributes to the regulation of calcium levels, which is essential for various cellular functions, including muscle contraction, enzyme activity, and signal transduction . Additionally, calumenin is involved in the quality control of protein folding and sorting within the ER, ensuring that only properly folded proteins are transported to their final destinations .

Applications

Recombinant human calumenin with a His tag is widely used in research to study its function and role in cellular processes. It is also utilized in various biochemical assays and structural studies to understand its interaction with other proteins and its involvement in calcium signaling pathways .

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