CKMT1 Human

Creatine Kinase Muscle Type-1 Human Recombinant

Produced in Pichia Pastoris, recombinant human CKMT1, devoid of the C-terminal Lysine on both chains, is a glycosylated polypeptide weighing 47kDa. This protein shares an identical amino acid sequence with the native enzyme. Purified in non-denaturing conditions, it exhibits reactivity with polyclonal antibodies specific to MM Isoenzyme in ELISA. The purification of CKMT1 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT240
Source
Pichia Pastoris.
Appearance
Clear, colorless liquid solution, sterile-filtered.

CKMT1A Human

Creatine Kinase, Mitochondrial 1A Human Recombinant

Recombinant human CKMT1A, produced in E. coli, is a single polypeptide chain consisting of 403 amino acids (residues 40-417) with a molecular weight of 45.0 kDa. It includes a 25 amino acid His-tag fused at the N-terminus and is purified through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT337
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CKMT2 Human

Creatine Kinase, Mitochondrial 2 Human Recombinant

Recombinant human CKMT2, produced in E. coli, is a single polypeptide chain with a molecular weight of 46.1 kDa. The protein consists of 405 amino acids (residues 40-419) and includes a 25 amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT382
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CKMT3 Human

Creatine Kinase Muscle Type-3 Human Recombinant

CKMT3 Human Recombinant is a glycosylated polypeptide chain produced in Pichia Pastoris. This recombinant protein exhibits an identical amino acid sequence to the native CKMT3 enzyme. Purified under non-denaturing conditions, it demonstrates reactivity with polyclonal antibodies specific to the MM isoenzyme in ELISA assays. The purification process for CKMT3 involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT451
Source
Pichia Pastoris.
Appearance
Sterile Filtered colorless liquid.

CKM Human, Native

Creatine Kinase Muscle Human

Human Creatine Kinase M-Type is a protein naturally found in the heart muscle of humans.

Shipped with Ice Packs
Cat. No.
BT29
Source

Human Cardiac Tissue.

Appearance

Lyophilized Powder

CKMB Human

Creatine Kinase MB Human Recombinant

Recombinant Human Creatine Kinase MB, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of approximately 44 kDa. The purification of CKMB is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT50
Source

Escherichia Coli.

Appearance

Sterile Filtered colorless liquid.

CKMB Human S.Chain

Creatine Kinase MB Single Chain Human Recombinant

Recombinant Human Creatine Kinase MB Single Chain, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of approximately 44 kDa. It is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT81
Source

Escherichia Coli.

Appearance

Sterile Filtered colorless liquid.

CKMBITI Human

Creatine Kinase MB Isoenzyme Type-I Human Recombinant

Recombinant human CKMBITI, produced in Pichia Pastoris, is a fully glycosylated polypeptide chain encompassing the complete sequence of the Creatine Kinase MB isoenzyme, except for the C-terminal lysine residue on the M subunit. This dimeric protein consists of M and B subunits, resulting in a total molecular weight of approximately 44 kDa. CKMBITI is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT108
Source
Pichia Pastoris.
Appearance
Sterile, colorless liquid.

CKMBITII Human

Creatine Kinase MB Isoenzyme Type-II Human Recombinant

Recombinantly produced in Pichia Pastoris, CKMBITII Human effectively reacts with polyclonal antibodies specific to MB Isoenzyme in ELISA assays.
Shipped with Ice Packs
Cat. No.
BT151
Source
Pichia Pastoris.
Appearance
Sterile Filtered, clear and colorless liquid.

CKB Human His

Creatine Kinase Brain Human Recombinant, His Tag

Recombinant Human CKB, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 401 amino acids (with amino acids 1-381 present) and has a molecular weight of 44.8 kDa. A 20 amino acid His-Tag is fused to the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30946
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.
Definition and Classification

Creatine kinases (CK), also known as creatine phosphokinases (CPK), are enzymes that catalyze the conversion of creatine and adenosine triphosphate (ATP) to phosphocreatine (PCr) and adenosine diphosphate (ADP). This reversible reaction plays a crucial role in cellular energy homeostasis . CK enzymes are classified into three main isoenzymes based on their tissue distribution: CK-MM (muscle type), CK-BB (brain type), and CK-MB (hybrid type found in the heart) . Additionally, there are two mitochondrial isoforms: ubiquitous mitochondrial CK (u-mtCK) and sarcomeric mitochondrial CK (s-mtCK) .

Biological Properties

Key Biological Properties: CK enzymes are essential for maintaining ATP levels in cells with high energy demands, such as muscle cells, brain cells, and spermatozoa . They facilitate the rapid regeneration of ATP from PCr, ensuring a constant energy supply .

Expression Patterns and Tissue Distribution: CK-MM is predominantly found in skeletal muscle, CK-BB in the brain and smooth muscle, and CK-MB in the myocardium (heart muscle) . Mitochondrial CK isoforms are present in tissues with high metabolic rates, such as the heart and skeletal muscle .

Biological Functions

Primary Biological Functions: CK enzymes play a pivotal role in cellular energy metabolism by maintaining ATP homeostasis . They act as an energy buffer, storing and regenerating ATP as needed .

Role in Immune Responses and Pathogen Recognition: Recent studies suggest that creatine metabolism, including CK activity, may influence immune cell function and pathogen recognition . CK enzymes help regulate energy supply during immune responses, supporting the high energy demands of activated immune cells .

Modes of Action

Mechanisms with Other Molecules and Cells: CK enzymes interact with various molecules, including ATP, ADP, and creatine, to facilitate the reversible transfer of a phosphoryl group . This interaction is crucial for maintaining cellular energy balance .

Binding Partners and Downstream Signaling Cascades: CK enzymes bind to creatine and ATP to form phosphocreatine and ADP . This reaction is part of the phosphocreatine shuttle, which transports high-energy phosphate groups within cells . CK activity also influences downstream signaling pathways involved in energy metabolism and cellular stress responses .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: CK expression and activity are regulated at multiple levels, including transcriptional and post-translational modifications . Transcription factors and signaling pathways modulate CK gene expression in response to cellular energy demands .

Transcriptional Regulation and Post-Translational Modifications: CK genes are regulated by transcription factors that respond to changes in cellular energy status . Post-translational modifications, such as phosphorylation, can also modulate CK enzyme activity and stability .

Applications

Biomedical Research: CK enzymes are widely studied in biomedical research for their role in energy metabolism and muscle physiology . They serve as biomarkers for muscle damage and cardiac events .

Diagnostic Tools: Elevated CK levels in the blood are used as diagnostic markers for conditions such as myocardial infarction, rhabdomyolysis, and muscular dystrophy . CK assays are commonly performed in clinical settings to assess tissue damage .

Therapeutic Strategies: Understanding CK function and regulation has potential therapeutic implications for metabolic disorders, muscle diseases, and cardiovascular conditions . Targeting CK pathways may offer new treatment approaches for these diseases .

Role in the Life Cycle

Role Throughout the Life Cycle: CK enzymes play a critical role in energy metabolism throughout the life cycle, from development to aging . During development, CK activity supports rapid cell growth and differentiation . In aging, CK function may decline, contributing to reduced muscle mass and strength .

Development to Aging and Disease: CK enzymes are essential for maintaining energy homeostasis during periods of high metabolic demand, such as growth, exercise, and stress . Dysregulation of CK activity is associated with various diseases, including muscular dystrophy, heart failure, and neurodegenerative disorders .

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