This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This STOML2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 161-189 amino acids from the Central region of human STOML2.
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C,-20 °C
Haltbarkeit
6 months
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Da Cruz, De Marchi, Frieden, Parone, Martinou, Demaurex: "SLP-2 negatively modulates mitochondrial sodium-calcium exchange." in: Cell calcium, Vol. 47, Issue 1, pp. 11-8, (2010) (PubMed).
Grass, Preuss, Ahlgrimm, Fadle, Regitz, Pfoehler, Murawski, Pfreundschuh: "Association of a dominantly inherited hyperphosphorylated paraprotein target with sporadic and familial multiple myeloma and monoclonal gammopathy of undetermined significance: a case-control study." in: The lancet oncology, Vol. 10, Issue 10, pp. 950-6, (2009) (PubMed).
Kirchhof, Chau, Lemke, Vardhana, Darlington, Márquez, Taylor, Rizkalla, Blanca, Dustin, Madrenas: "Modulation of T cell activation by stomatin-like protein 2." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 181, Issue 3, pp. 1927-36, (2008) (PubMed).
STOML2 is similar in sequence to stomatin. It is a 356 amino acid protein with a calculated molecular mass of 38.5 kDa. STOML2 has 3 potential initiator sites, all sharing the same open reading frame. The STOML2 protein contains the cognate stomatin family consensus sequence, but it lacks the characteristic N-terminal hydrophobic domain and palmitoylation consensus sequence. STOML2 shares greatest sequence homology with stomatin and SLP1 in a region predicted to contain beta sheet and alpha helix structures. Northern blot analysis detected a 1.5 kb STOML2 transcript in all tissues examined, with highest levels in heart, liver, and pancreas. Western blot analysis detected STOML2 at apparent molecular masses of 45.5 kDa or 44.6 kDa in all human and mammalian cell lines and tissues examined, including red blood cells. Some cells also showed a faint band at about 34.3 kDa, which may represent translation from an alternate initiation site.