Anti-Hemopexin/HPX Antibody Picoband® fluoro550 Vervoeging

Hemopexin (or haemopexin; Hpx; Hx), also known as beta-1B-glycoprotein, is a glycoprotein that in humans is encoded by the HPX gene and belongs to hemopexin family of proteins. This gene encodes a plasma glycoprotein that binds heme with high affinity. The encoded protein is an acute phase protein that transports heme from the plasma to the liver and may be involved in protecting cells from oxidative stress.

T-cell surface glycoprotein CD8 alpha chain; CD8 antigen 32 kDa chain; OX-8 membrane antigen; CD8a

HPX

3263

P02790

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human Hemopexin/HPX recombinant protein (Position: V97-A447) .

Flow Cytometry

Immunology, T Cells

Immunogen affinity purified.

Liquid

Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs) . In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs) . This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells.

1. Altruda, F., Poli, V., Restagno, G., Argos, P., Cortese, R., Silengo, L. The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology. Nucleic Acids Res. 13: 3841-3859, 1985. 2. Altruda, F., Poli, V., Restagno, G., Silengo, L. Structure of the human hemopexin gene and evidence for intron-mediated evolution. J. Molec. Evol. 27: 102-108, 1988. 3. Cai, G.-Y., Law, M. L. Cloning and characterization of a human gene coding for hemopexin. (Abstract) Am. J. Hum. Genet. 39: A191 only, 1986.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

6

CD8a molecule

Cell membrane. Single-pass type I membrane protein.

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.