Protein kinases comprise a large group of encoded factors that regulate cellular processes by catalyzing the transfer of a phosphate group to a hydroxyl acceptor in serine, threonine or tyrosine residues. SRMS (src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites), also known as SRM, is a 488 amino acid nonreceptor tyrosine-protein kinase that may play a role in the differentiation/proliferation of keratinocytes. SRMS consists of one Src homology 3 (SH3) domain, one Src homology 2 (SH2) domain and one protein kinase domain. The SH3 region is a small protein domain present in a large group of proteins, generally existing in association with catalytic domains. SH3 domains are also often accompanied by SH2 domains which bind to tyrosine-phosphorylated regions of target proteins, frequently linking activated growth factors to putative signal transduction proteins. Deletion or mutation of SH3 domains generally activate the transforming potential of nonreceptor tyrosine kinases, suggesting that SH3 mediates negative regulation of an intrinsic transforming activity.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of SRMS of human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-143 mapping at the N-terminus of SRMS of human origin
Tissue Specificity
epitope corresponding to amino acids 1-143 mapping at the N-terminus of SRMS of human origin