|Application ||IHC-P, IF, E|
|Other Accession||NP_002456, 45976288|
|Calculated MW||128294 Da|
|Application Notes||MYBPC1 antibody can be used for detection of MYBPC1 by immunohistochemistry at 5 µg/mL. For immunofluorescence start at 5 µg/mL.|
|Reconstitution & Storage||MYBPC1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||MYBPC1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.|
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
MYBPC1 Antibody: Myosin binding protein C (MYBPC) is a component of the thick filament of striated muscle, with the slow-type isoform designated MYBPC1. Both the fast-type (MYBPC2) and slow-type MYBPC protein contains seven immunoglobulin C2 motifs and three fibronectin type-III repeats. Multiple isoforms of MYBPC1 are known to exist, and are present in varying amounts in different skeletal muscles. It is thought that the MYBPC1 slow subfamily may play important roles in the assembly and stabilization of sarcomeric M- and A-bands and regulate the contractile properties of the actomyosin filaments.
Furst DO, Vinkemeir U and Weber K. Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full-length human cDNA. J. Cell Sci. 1992; 102:769-78.
Weber FE, Vaughan KT, Reiach FC, et al. Complete sequence of human fast-type and slow-type muscle myosin-binding-protein C (MyBP-C). Differential expression, conserved domain structure and chromosome assignment. Eur. J. Biochem. 1993; 216:661-9.
Ackermann MA and Kontrogianni-Konstantopoulous A. Myosin binding protein-C slow: an intricate subfamily of proteins. J. Biomed. Biotech. 2010; 2010:652065
If you have any additional inquiries please email technical services at firstname.lastname@example.org.