Catalog# |
CA43 |
Source |
HEK293 |
Description |
Recombinant Human Calumenin/CALU is produced by our mammalian expression system in human cells. The target protein is expressed with sequence (Lys20-Phe315) of Human CALU fused with a polyhistidine tag at the C-terminus. |
Names |
Calumenin, Crocalbin, IEF SSP 9302, CALU |
Accession # |
O43852 |
Formulation |
Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4 |
Shipping |
The product is shipped at ambient temperature. |
Reconstitution |
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in 1X PBS.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
Storage |
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
Purity |
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. |
Endotoxin |
Less than 0.1 ng/µg (1 IEU/µg). |
Amino Acid Sequence |
KPTEKKDRVHHEPQLSDKVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDK DGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNY KQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQETMEDIDKNADGFIDLEEYI GDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQ NKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEFVDHHHHHH
|
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 γ-carboxylase GGCX. |