Recombinant Human CKMT1A Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1290

Recombinant Human CKMT1A Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1290
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His
Host Species Human
Accession P12532
Background CKMT1A belongs to the ATP:guanido phosphotransferase family. It contains 1 phosphagen kinase C-terminal domain and 1 phosphagen kinase N-terminal domain. CKMT1A gene is one of two genes which encode the ubiquitous mitochondrial creatine kinase (CKMT1). CKMT1 is responsible for the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. It belongs to the creatine kinase isoenzyme family. It exists as two isoenzymes, sarcomeric MtCK (CKMT2) and ubiquitous MtCK, encoded by separate genes. CKMT1 occurs in two different oligomeric forms: dimers and octamers, in contrast to the exclusively dimeric cytosolic creatine kinase isoenzymes. Ubiquitous mitochondrial creatine kinase has 8% homology with the coding exons of sarcomeric CKMT1.
Description A DNA sequence encoding human CKMT1A (P12532-1) (Ala40-His417) was expressed, with a His tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal His
AA Sequence Ala40-His417
Molecular Weight The recombinant human CKMT1A consists of 396 a.a. and predicts a molecular mass of 45.3 KDa. It migrates as an approximately 43 KDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Supplied as sterile 20mM Tris, 500mM NaCl, pH 8.5, 10% gly.
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 Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
Subcellular Location Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Protein Families ATP:guanido phosphotransferase family
Database References

Gene Functions References

  1. The highly conserved residue E227 acts as the catalytic base to accept the guanidinium proton transferred from creatine in UMTCK. PMID: 27909311
  2. Mitochondrial creatine kinase CKMT1 is necessary for survival of EVI1-expressing cells in subjects with EVI1-positive AML. PMID: 28191887
  3. LRRK2 can interact directly with uMtCK to block its entry into mitochondria and its subsequent processing. PMID: 21370995
  4. CKMT1 is a key regulator of the permeability transition pore through a complex that is distinct from the classical permeability transition pore. PMID: 24522192
  5. mitochondrial creatine kinase expression in hepatocellular carcinoma may be caused by hepatocarcinogenesis per se but not by loss of mitochondrial integrity, of which ASB9 could be a negative regulator PMID: 24174293
  6. The results indicated that uMtCK expression is associated with a poor prognosis in breast cancer and might serve as a tumor marker. PMID: 22982673
  7. Significantly greater creatine kinase carbonylation is associated with chronic obstructive pulmonary disease PMID: 16166745
  8. Because creatine kinase temporally buffers ATP, these observations support the hypothesis that a deficit in myofibrillar energy delivery contributes to chronic heart failure pathophysiology in human left ventricular hypertrophy. PMID: 16952984


Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed