signal-regulatory protein a-1

Expression system: HEK293 Cells
Length: 32-373, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-373, Partial
Activity: Not Tested

Signal-regulatory protein beta-1 (SIRPB1, CD172b) is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins known to be involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. This protein was found to interact with TYROBP DAP12, a protein bearing immunoreceptor tyrosine-based activation motifs. This protein was also reported to participate in the recruitment of tyrosine kinase SYK.

Expression system: HEK293 Cells
Length: 33-287, Extracellular Domain
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-373, Partial
Activity: Not Tested

Signal regulatory protein α (SIRPα) is a regulatory membrane glycoprotein from SIRP family expressed mainly by myeloid cells and also by stem cells or neurons.SIRPα acts as inhibitory receptor and interacts with a broadly expressed transmembrane protein CD47 also called the don´t eat me signal.Cancer cells highly expressed CD47 that activate SIRP α and inhibit macrophage-mediated destruction. SIRP alpha Protein, Human, Recombinant (aa 31-370, hFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-hFc-Avi tag. The predicted molecular weight is 66.1 kDa and the accession number is P78324-1.

CD47 (Cluster of Differentiation 47) also known as integrin associated protein (IAP) is a transmembrane protein that in humans is encoded by the CD47 gene. CD47 belongs to the immunoglobulin superfamily and partners with membrane integrins and also binds the ligands thrombospondin-1 (TSP-1) and signal-regulatory protein alpha (SIRPα).CD-47 acts as a don't eat me signal to macrophages of the immune system which has made it a potential therapeutic target in some cancers.

Hydroxyacid oxidase 1, also known as Glycolate oxidase, HAO1, and GOX1, is a member of the FMN-dependent alpha-hydroxy acid dehydrogenase family. HAO1 GOX1 has 2-hydroxyacid oxidase activity. It is most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate. HAO1 GOX1 is a liver-specific peroxisomal enzyme that oxidizes glycolate to glyoxylate with the concomitant production of H2O2. In Hao1 messenger RNA (mRNA), an iron-responsive element (IRE) homologous to the sequence recognized by iron regulatory proteins (IRP), key regulators of iron homeostasis, is present. Mammalian HAO1 GOX1 is a peroxisomal protein and that the C-terminal sequence SKI acts as the targeting signal. Down-regulation of HAO1 GOX1 expression during oxidative stress may provide a mechanism to prevent excessive H2O2 formation in liver peroxisomes and may represent the prototype of a poorly recognized but potentially relevant response to an oxidative injury involving down-regulation of ROS-producing enzymes.

Expression system: HEK293 Cells
Length: 1-363, Partial
Activity: Not Tested

Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen, heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.

Expression system: Baculovirus Insect Cells
Length: 1-416, Full Length
Activity: Enzyme activity

Serine threonine-protein kinase 1, also known as Lymphocyte-oriented kinase, STK1 and LOK, belongs to the protein kinase superfamily, STE Ser Thr protein kinase family and STE2 subfamily. Protein kinases constitute a large superfamily of enzymes with key regulatory functions in nearly all signal transmission processes of eukaryotic cells. The Ste2 family of serine threonine kinases plays an important role in numerous cellular functions such as growth, apoptosis, and morphogenesis. STK1 is similar to several known polo-like kinase kinases. It can associate with and phosphorylate polo-like kinase 1, and overexpression of a kinase-dead version of the protein interferes with normal cell cycle progression. STK1 can also negatively regulate interleukin 2 expression in T-cells via the mitogen activated protein kinase kinase 1 pathway. Stk1 can associate with Plk1 in cells and furthermore can phosphorylate Plk1. It can also act on substrates such as myelin basic protein and histone 2A on serine and threonine residues.