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Calumenin Recombinant Protein | CALU recombinant protein
Recombinant Human Calumenin Protein
Purity
>95% as determined by reducing SDS-PAGE.
Synonyms
Calumenin; Recombinant Human Calumenin Protein; Crocalbin; IEF SSP 9302; CALU; CALU recombinant protein
Host
Human Cells
Purity/Purification
>95% as determined by reducing SDS-PAGE.
Form/Format
Lyophilized from a 0.2 mum filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Sequence Length
315
Species
Human
Endotoxin
<1.0 EU per ug as determined by LAL test.
Fragment
Lys20-Phe315
Fusion Tag
C-6His
Preparation and Storage
Lyophilized protein should be stored at < -20 degree C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7 degree C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20 degree C for 3 months.
Reconstituted protein solution can be stored at 4-7 degree C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20 degree C for 3 months.
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SDS-Page
Related Product Information for CALU recombinant protein
Protein Construction: Recombinant Human Calumenin is produced by our Mammalian expression system and the target gene encoding Lys20-Phe315 is expressed with a 6His tag at the C-terminus.
Background: Calumenin is a secreted calcium-binding protein that belongs to the CREC family. Calumenin contains six EF-hand domains and is expressed at high levels in the heart, placenta and skeletal muscle. Human Calumenin is synthesized as a 315 amino acid precursor that contains a 19 amino acid signal sequence, and a 296 amino acid mature chain. Calumenin localizes to the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin is involved in the regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. It seems to inhibit gamma-carboxylase GGCX.
Background: Calumenin is a secreted calcium-binding protein that belongs to the CREC family. Calumenin contains six EF-hand domains and is expressed at high levels in the heart, placenta and skeletal muscle. Human Calumenin is synthesized as a 315 amino acid precursor that contains a 19 amino acid signal sequence, and a 296 amino acid mature chain. Calumenin localizes to the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin is involved in the regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. It seems to inhibit gamma-carboxylase GGCX.
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
Molecular Mass: 36.0kDa
Actual Protein Molecular Mass: 54kDa
Actual Protein Molecular Mass: 54kDa
NCBI Official Full Name
calumenin isoform b
NCBI Official Synonym Full Names
calumenin
NCBI Official Symbol
CALU
NCBI Protein Information
calumenin
UniProt Protein Name
Calumenin
Protein Family
UniProt Gene Name
CALU
NCBI Description
The product of this gene is a calcium-binding protein localized in the endoplasmic reticulum (ER) and it is involved in such ER functions as protein folding and sorting. This protein belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Oct 2008]
Uniprot Description
Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity ().
Research Articles on CALU
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Product Notes
The CALU calu (Catalog #AAA2556599) is a Recombinant Protein produced from Human Cells and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Calumenin, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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