Recombinant Human CROT Protein (474 Leu/Val, His Tag)

Name: Recombinant Human CROT Protein (474 Leu/Val, His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1437
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	Q9UKG9
Synonym	COT
Background	Carnitine octanoyltransferase (CROT or COT), also known as octanoyl-CoA: L-carnitine O-octanoyltransferase, medium-chain/long-chain carnitine acyltransferase, and carnitine medium-chain acyltransferase, is a carnitine acyltransferase belonging to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups that catalyzes the reversible transfer of fatty acyl groups between CoA and carnitine. Carnitine octanoyltransferase (CROT or COT) facilitate the transport of medium- and long-chain fatty acids through the peroxisomal and mitochondrial membranes. It is physiologically inhibited by malonyl-CoA. COT also has functions in efficiently converting one of the end products of the peroxisomal beta-oxidation of pristanic acid, 4, 8-dimethylnonanoyl-CoA, to its corresponding carnitine ester.
Description	A DNA sequence encoding the human CROT (Q9UKG9) (Met 1-Leu 612, 474 Leu/Val) was fused with a His tag at the C-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met 1
AA Sequence	Met 1-Leu 612, 474 Leu/Val
Molecular Weight	The recombinant human CROT consists of 623 a.a. and predicts a molecular mass of 71.5 kDa. The apparent molecular mass of rhCROT is approximately 65 kDa in SDS-PAGE under reducing conditions.
Purity	>93% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0, 10% glycerol.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl-CoA, to its corresponding carnitine ester.
Subcellular Location	Peroxisome.
Protein Families	Carnitine/choline acetyltransferase family
Database References	HGNC: 2366 OMIM: 606090 KEGG: hsa:54677 STRING: 9606.ENSP00000413575 UniGene: Hs.125039

Gene Functions References

These results suggest that CROT activity, by controlling the peroxisomal amount of medium chain acyls, may control the peroxisomal oxidative pathway. PMID: 21619872
Selected 'Tpl2/Cot-YL ribozyme' efficiently cleaves its target sequence in cis and in trans; furthermore, the ribozyme efficiently cleaves a longer target sequence of 54 nucleotides in trans, as well as the full-length mRNA. PMID: 19054068
Human CPT1A, CPT1B, CPT2, CROT and CRAT are known to encode active carnitine acyltransferases. Earlier pfam annotations refer to the non-existing compound CARNITATE. In 2000 this has been changed to CARNITINE. PMID: 11001805
CROT encodes carnitine octanoyltransferase, an enzyme known from rat studies to act on products of peroxisomal fatty acid oxidation. Medium-chain acylcarnitines are thought to be transported from peroxisomes to mitochondria. PMID: 11001805

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.