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This gene encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasa

bs-0194P is one synthetic peptide derived from human GRP94. Glucose regulated protein 94 (GRP 94) is a resident protein of the endoplasmic reticulum (ER) and is induced by the accumulation of unfolded proteins suggesting that it might associate transiently with a variety of newly synthesized secretory and membrane proteins or permanently with mutant or defective proteins. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the C terminus of GRP 94 and other resident ER protei

Noggin is a secreted protein involved at multiple stages of vertebrate embryonic development including neural induction and is known to exert its effects by inhibiting the bone morphogenetic protein (BMP)-signaling pathway. It binds several BMPs with very high (picomolar) affinities, with a marked preference for BMP2 and BMP4 over BMP7. By binding tightly to BMPs, Noggin prevents BMPs from binding their receptors. Noggin binds the bone morphogenetic proteins (BMP) such as BMP-4 and BMP-7, ａ

The Ca2+/calmodulin-dependent protein kinases (CaM kinases) are a structurally related subfamily of serine/threonine kinases that includes CaMKI, CaMKII, CaMKIV and Myosin light chain kinases (MYLKs, also designated MLCKs). The MYLK kinases phosphorylate Myosin regulatory light chains to catalyze Myosin interaction with Actin filaments, resulting in contractile activity. MYLK3 (Myosin light chain kinase 3) is a 795 amino acid cardiac-specific protein that contains one protein kinase domain ａn

Myosin heavy chains are ubiquitous Actin-based motor proteins that convert the chemical energy derived from ATP hydrolysis into the mechanical energy that drives diverse motile processes in eukaryotic cells, including cytokinesis, vesicular transport and cellular locomotion. Muscle myosin is a heterohexamer consisting of two myosin heavy chains and two associated nonidentical pairs of myosin light chains. The seven myosin heavy chain isoforms that predominate in mammalian skeletal muscles inc

Myosin heavy chains are ubiquitous Actin-based motor proteins that convert the chemical energy derived from ATP hydrolysis into the mechanical energy that drives diverse motile processes in eukaryotic cells, including cytokinesis, vesicular transport and cellular locomotion. Muscle myosin is a heterohexamer consisting of two myosin heavy chains and two associated nonidentical pairs of myosin light chains. The seven myosin heavy chain isoforms that predominate in mammalian skeletal muscles inc