Recombinant Human PRSS8 Protein(His tag) (HH0106PL)

Cat.No.

HH0106PL

Synonyms

PRSS8; prostasin; CAP1; PROSTASIN;

Accession

PRSS8

Predicted N Terminal

Ala 30

Form

Lyophilized from sterile PBS, pH 7.4, 5 % trehalose and 5 % mannitol.

Bio-activity

Measured by its ability to cleave the fluorogenic peptide substrate Boc-QAR-AMC. The specific activity is>10 pmoles/min/μg.

Molecular Mass

Recombinant Human Prss8 consists of 304 amino acids and predicts a molecular mass of 32.8 kDa. By SDS-PAGE under reducing conditions, the apparent molecular mass of rhPrss8 is approximately 40 kDa due to glycosylation.

Endotoxin

< 1.0 EU per 1 microgram of protein (determined by LAL method).

Purity

> 97 % by SDS-PAGE.

Storage

In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C). Avoid repeated freeze/thaw cycles.

Reconstitution

Reconstitute in sterile distilled water to a concentration of 0.1-1.0 mg/mL.

Warning

For research use only!

Background

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Tag

His

Species

Human

Source

HEK293

Background

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).