This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogène
This MPZL2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 67-94 amino acids from the Central region of human MPZL2.
MPZL2
Reactivité: Humain
Hôte: Lapin
Polyclonal
FITC
Indications d'application
For WB starting dilution is: 1:1000
Restrictions
For Research Use only
Format
Liquid
Concentration
0.5 mg/mL
Buffer
Supplied in PBS with 0.09 % (W/V) sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C,-20 °C
Stockage commentaire
Store at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
anticorps cb837, anticorps eva1, anticorps mpzl2, anticorps wu:fb07b02, anticorps EVA1, anticorps EVA, anticorps Eva, anticorps Eva1, anticorps myelin protein zero-like 2b, anticorps myelin protein zero like 2, anticorps myelin protein zero-like 2, anticorps mpzl2b, anticorps MPZL2, anticorps Mpzl2
Sujet
Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain, a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq].