IHC-P:0.5-1ug/ml for 30 minutes at RT.
This MAb reacts with MUC1, a large transmembrane glycoprotein expressed on the ductal surface of normal glandular epithelia. The dominant epitope of this MAb involves both amino acids as well as sugar moieties. Neuraminidase treatment destroys the antigen. It is a very good tracer agent in CA15.3 assays. The extracellular domain of MUC1 largely consists of a highly conserved, O-glycosylated 20 amino acids tandem repeat which can occur 30-100 times per molecule depending on the length of the allele involved. In the vast majority of human carcinomas this protein is up-regulated and poorly glycosylated and appears on the cell surface in a non-polarized fashion.
Prepared in 10mM PBS with 0.05% BSA and 0.05% azide.
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Human milk-fat globule membranes (HMFGM)
Ab purified from Bioreactor Concentrate by Protein A/G
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Mucin 1, Cell Surface Associated,Admckd,Admckd1,Ca 15-3,Cd227,Ema,H23Ag,Kl-6,Mam6,Mcd,Mckd,Mckd1,Muc-1,Muc-1/Sec,Muc-1/X,Muc1/Zd,Pem,Pemt,Pum,Muc1
This gene encodes a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach and pancreas. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. This gene is known to contain a highly polymorphic variable number tandem repeats (VNTR) domain. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Feb 2011]