|Application ||WB, IHC-P, E|
|Other Accession||NP_003794.3, NP_062830.1|
|Calculated MW||187627 Da|
|Antigen Region||904-933 aa|
|Other Names||Myomesin-1, 190 kDa connectin-associated protein, 190 kDa titin-associated protein, Myomesin family member 1, MYOM1|
|Target/Specificity||This MYOM1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 904-933 amino acids from the Central region of human MYOM1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MYOM1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.|
|Cellular Location||Cytoplasm, myofibril, sarcomere, M line|
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Provided below are standard protocols that you may find useful for product applications.
The giant protein titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line, where it binds tightly to M-band constituents of apparent molecular masses of 190 kD (myomesin 1) and 165 kD (myomesin 2). This protein, myomesin 1, like myomesin 2, titin, and other myofibrillar proteins contains structural modules with strong homology to either fibronectin type III (motif I) or immunoglobulin C2 (motif II) domains. Myomesin 1 and myomesin 2 each have a unique N-terminal region followed by 12 modules of motif I or motif II, in the arrangement II-II-I-I-I-I-I-II-II-II-II-II. The two proteins share 50% sequence identity in this repeat-containing region. The head structure formed by these 2 proteins on one end of the titin string extends into the center of the M band. The integrating structure of the sarcomere arises from muscle-specific members of the superfamily of immunoglobulin-like proteins. Alternatively spliced transcript variants encoding different isoforms have been identified.
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Schoenauer, R., et al. J. Mol. Biol. 349(2):367-379(2005)
Hornemann, T., et al. J. Mol. Biol. 332(4):877-887(2003)
Porter, J.D., et al. J. Exp. Biol. 206 (PT 17), 3101-3112 (2003) :
Agarkova, I., et al. J. Biol. Chem. 275(14):10256-10264(2000)
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