Human

The thromboxane A2 (TxA2) receptor (TP) is a member of the G protein-coupled receptor (GPCR) superfamily which mediates TxA2-induced platelet aggregation and vasoconstriction. Dysregulation of TxA2 synthesis and function has been implicated in the pathogenesis of a number of disease states including myocardial ischemia, asthma, pregnancy-induced hypertension, and a variety of kidney diseases. TP receptors (Thromboxane A2 receptors) are widely distributed among different organ systems and localized on both cell membranes and in intracellular structures. Two isoforms of human TPs have been cloned from placenta (TPα) and endothelium (TPβ) that differ in their mechanisms and kinetics of desensitization and internalization. The TPs are linked via the Gq/G11 class of G proteins to phospholipase C (PLC), which hydrolyzes phosphoinositides to two potent second messengers: inositol 1,4,5-trisphosphate, which leads to an increase in cytoplasmic free calcium, and diacylglycerol (DAG), which activates protein kinase C (PKC).

Camelid VHH Antibody (also called single-domain antibody, sdAb or Nanobody by Ablynx) is a peptide chain about 110 amino acids in length, containing one variable domain of a heavy-chain antibody (a VHH fragment). Like a whole antibody, the camelid VHH antibody is able to bind selectively to a specific antigen. This single-domain antibody has a broad range of applications in biotechnical and therapeutic research fields due to its small size, simple production and high affinity. GenScript’s MonoRab™ Anti-Camelid VHH Affinity Resin (Cat. No. L00905) is designed for purification of Camelid VHH single domain antibody from commonly used protein expression systems such as bacteria, yeast and mammalian cells. The VHH single domain antibody in cell lysate can specifically bind to the Anti-Camelid VHH monoclonal antibody coupled to the resin. Nonspecific binding reactions are eliminated by stringent washing steps, and the purified target protein is eluted with a high recovery rate. Table 1 lists the main characteristics of GenScript’s MonoRab™ Anti-Camelid VHH Affinity Resin.

ELISA; WB;

Mouse IgG2a,κ

Horseradish peroxidase (HRP)

V5 tag peptide conjugated to KLH

Human

Prostaglandin D(2) (PGD(2)) is derived from arachidonic acid and binds with high affinity to the G-protein coupled receptors prostanoid DP(1) and DP(2). Interaction with DP(2) results in cell chemotaxis, eosinophil degranulation, eosinophil shape change, adhesion molecule upregulation and Th2 cytokine production. In allergic rhinitis and allergic asthma PGD(2) is released from mast cells in response to allergen challenge and may trigger symptoms such as sneezing, rhinorrhea, pruritus, mucus hypersecretion and pulmonary inflammation. GenScript's cloned human DP2-expressing cell line co-expressing Gα15 is made in the CHO-K1 host.

Mouse

HEK 293

MIP-1α (Ala24-Ala92) Accession # Q5QNW0

Macrophage Inflammatory Protein-1α; CCL-3; LD78α; LD78 alpha

Human

HEK 293

B7-1/CD80 (Val35-Asn242) Accession # P33681	hFc
N-term	C-term

CD80; B7; B7-1; B7.1; BB1; CD28LG; CD28LG1; LAB7

Human

Proteinase-activated receptors (PAR) are a subfamily of G-protein coupled, seven-transmembrane domain receptors, which are cleaved within the aminoterminal exodomain by certain serine proteinases at a specific peptide bond. Trypsin and mast cell tryptase, and more recently, the activated coagulation factors VIIa and Xa, have been identified as serine proteinases able to activate mammalian PAR-2. As already indicated, PAR-2 is believed to be involved in inflammation. This role for PAR-2 implies that elastase and cathepsin G would paradoxically display an anti-inflammatory property by disarming PAR-2.

Bovine

Reconstitute lyophilized EK powder in sterile deionized water at 1mg/ml, then dilute in EK Dilution/Storage Buffer according to your requirement.

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys(DDDDK↑). Enterokinase will not work if the recognition site is followed by a proline. rbEKhas the highest activity than EK of other species and is used wildly in biochemical applications. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system. Recombinant Bovine Enterokinase (His-tagged) (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 × His at C-terminus. A fully biologically active molecule, rbEK has a molecular mass of 40 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Human

Human Cells

IL-5RA (Asp21-Glu335) Accession # Q01344	Poly-His
N-term	C-term

Interleukin-5 receptor subunit alpha; IL-5 receptor subunit alpha; IL-5R subunit alpha; IL-5R-alpha; CDw125; CD125; IL5RA; IL5R

Human

HEK 293

B7-H3 (Leu29-Pro245) Accession # Q5ZPR3-2	Poly-His
N-term	C-term

B7H3; B7-H3; B7H34Ig-B7-H3; B7-H3B7; CD276ss