All CAMKV reagents are produced in house and quality controlled, including 1 CAMKV Antibody, 30 CAMKV Gene, 1 CAMKV Lysate, 1 CAMKV Protein, 2 CAMKV qPCR. All CAMKV reagents are ready to use.
Recombinant CAMKV proteins are expressed by Baculovirus-Insect Cells with fusion tags as N-GST & His.
CAMKV antibodies are validated with different applications, which are ELISA, IHC-P, ICC/IF, IF.
CAMKV cDNA clones are full length sequence confirmed and expression validated. There are 13 kinds of tags for each CAMKV of different species, especially GFP tag, OFP tag, FLAG tag and so on. There are three kinds of vectors for choice, cloning vector, expression vector and lentivrial expression vector.
CaM kinase-like vesicle-associated protein, also known as CAMKV, is a peripheral membrane protein and Cytoplasmic vesicle membrane protein which belongs to the protein kinase superfamily and CAMK Ser/Thr protein kinase family. CAMKV contains one protein kinase domain. It is predominantly observed in association with the plasma membrane of soma and in neurites, both axons and dendrites. CAMKV may be associated with vesicular structures. It does not appear to have detectable kinase activity. Protein kinases are a group of enzymes that move a phosphate group onto proteins, in a process called phosphorylation. Protein kinases function as an on/off switch for many cellular processes, including metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. They also function in embryonic development, physiological responses, and in the nervous and immune system. Abnormal phosphorylation causes many human diseases, including cancer, and drugs that affect phosphorylation can treat those diseases. The protein kinase domain is a structurally conserved protein domain containing the catalytic function of protein kinases. Protein kinases play a role in a mulititude of cellular processes, including division, proliferation, apoptosis, and differentiation. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins.
Hunter T, et al.,1988, Science. 241 (4861): 42-51.
Wiemann S., et al., 2001, Genome Res. 11:422-435.
G. Manning, et al., 2002, Science 6. 298:1912-1934.
Manning G, et al.,2002, Science. 298 (5600): 1912-34.