CKM Human, Native

Creatine Kinase Muscle Human

Human Creatine Kinase M-Type derived from Human Cardiac Tissue.

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 produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.
The CKMB is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT50
Source

Escherichia Coli.

Appearance

Sterile Filtered colorless liquid formulation.

CKMB Human S.Chain

Creatine Kinase MB Single Chain Human Recombinant

Recombinant Human Creatine Kinase MB Single Chain produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.
The CKMB is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT81
Source

Escherichia Coli.

Appearance

Sterile Filtered colorless liquid formulation.

CKMBITI Human

Creatine Kinase MB Isoenzyme Type-I Human Recombinant

CKMBITI Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain and a full length Creatine Kinase MB isoenzyme, which is missing the C-terminal Lysine on the M subunit. CKMBITI is a dimeric protein comprised of M and B subunits, having a total Mw of ~44kDa.
The CKMBITI is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT108
Source
Pichia Pastoris.
Appearance
Sterile Filtered colorless liquid formulation.

CKMBITII Human

Creatine Kinase MB Isoenzyme Type-II Human Recombinant

CKMBITII Human Recombinant produced in Pichia Pastoris reacts with polyclonal antibodies to MB Isoenzyme in ELISA.
Shipped with Ice Packs
Cat. No.
BT151
Source
Pichia Pastoris.
Appearance
Sterile Filtered colourless liquid formulation.

CKMT1 Human

Creatine Kinase Muscle Type-1 Human Recombinant

CKMT1 Human Recombinant without C-terminal Lysine on both chains produced in Pichia Pastoris is a glycosylated 47kDa polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA. The CKMT1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT240
Source
Pichia Pastoris.
Appearance
Sterile Filtered colourless liquid formulation.

CKMT1A Human

Creatine Kinase, Mitochondrial 1A Human Recombinant

CKMT1A Human Recombinant produced in E. coli is a single polypeptide chain containing 403 amino acids (40-417) and having a molecular mass of 45.0 kDa.
CKMT1A is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT337
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

CKMT2 Human

Creatine Kinase, Mitochondrial 2 Human Recombinant

CKMT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 405 amino acids (40-419) and having a molecular mass of 46.1 kDa.
CKMT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT382
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

CKMT3 Human

Creatine Kinase Muscle Type-3 Human Recombinant

CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT451
Source
Pichia Pastoris.
Appearance
Sterile Filtered colorless liquid formulation.

CKB Human His

Creatine Kinase Brain Human Recombinant, His Tag

CKB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 44.8 kDa. The CKB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30946
Source
Escherichia Coli.
Appearance
Sterile filtered colorless 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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