The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ELISA: Use at a concentration of 0.25 - 1 µg/ml. Allows the detection of at least 0.2 - 0.4 ng/well of recombinant human SCF.
sELISA: Use at a concentration of 0.25 - 1 µg/ml. Allows the detection of at least 0.2 - 0.4 ng/well of recombinant human SCF.
WB: Use at a concentration of 0.1 - 0.2 µg/ml. The detection limit for recombinant human SCF is 1.5 - 3.0 ng/lane, under either reducing or non-reducing conditions. Predicted molecular weight: 31 kDa.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.
Hyperpigmentation with or without hypopigmentation, familial progressive Deafness, congenital, unilateral or asymmetric
Belongs to the SCF family.
Acts in the early stages of hematopoiesis.
A soluble form (sKITLG) is produced by proteolytic processing of isoform 1 in the extracellular domain. Found in two differentially glycosylated forms, LMW-SCF and HMW-SCF. LMW-SCF is fully N-glycosylated at Asn-145, partially N-glycosylated at Asn-90, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97 or Asn-118. HMW-SCF is N-glycosylated at Asn-118, Asn-90 and Asn-145, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97. A soluble form exists as a cleavage product of the extracellular domain.