Anti-Human Creatine Phosphokinase (BB) Antibody, clone BGN/2ba6
Mouse Anti-Human Monoclonal Antibody
|Calculated MW||42644 Da|
|Purification||Purified IgG prepared by affinity chromatography on Protein G|
|Shelf Life||18 months from date of despatch.|
|Other Names||Creatine kinase B-type, 22.214.171.124, B-CK, Creatine kinase B chain, CKB, CKBB|
|Target/Specificity||Mouse anti-human creatine phosphokinase, clone BGN/2ba6 recognizes creatine phosphokinase. Also known as creatine kinase (CK), it is a dimer with a molecular weight of approximately 80,000 kDa. In vertebrate cells, the cytosolic CK enzymes consist of two different subunits, either B (brain type) or M (muscle type). They combine to produce three different isoenzymes: CKMM, CKBB and CKMB. CKBB is the major CK isoenzyme of the brain (Eppenbergeret al, 1967,Dawsonet al, 1967).Creatine phosphokinase is an enzyme expressed in tissues and cell types with high energy requirements and is involved in cellular energy homeostasis. CK reversibly catalyzes the conversion of creatine and consumes adenosine triphosphate (ATP) to create phosphocreatine and adenosine diphosphate (ADP) (Wallimannet al, 1992,2011).Mouse anti-human creatine phosphokinase is specific for the CKBB isoenzyme and does not react with the B subunit in CKMB. There is minimal reactivity with other human serum proteins.|
|Preservative & Stabilisers||0.09% Sodium Azide (NaN3)|
|Storage||Store at +4℃ or at -20 ℃.|
|Precautions||Anti-Human Creatine Phosphokinase (BB) Antibody, clone BGN/2ba6 is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
1. Wallimann, T. et al. (2011) The creatine kinase system and pleiotropic effects of creatine.Amino Acids. 40(5):1271-96.2. Wallimann, T. et al. (1992) Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis.Biochem J. 281: 21-40.3. Eppenberger, H.M. et al. (1967) The comparative enzymology of creatine kinases. I. Isolation and characterization from chicken and rabbit tissues.J Biol Chem. 242: 204-209.4. Dawson, D.M. et al. (1967) The comparative enzymology of creatine kinases. II. Physical and chemical properties.J Biol Chem. 242: 210-217.
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