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ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.

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Anti-SARS Mouse Monoclonal Antibody

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RIP3 Antibody: Certain serine/threonine protein kinases, such as ASK1, RIP, DAP, and ZIP kinases, are mediators of apoptosis. Receptor interacting proteins including RIP and RIP2/RICK mediate apoptosis induced by TNFR1 and Fas, two prototype members in the death receptor family. A novel member in the RIP kinase family was recently identified and designated RIP3. RIP3 contains N-terminal kinase domain but, unlike RIP or RIP2, lacks the C-terminal death or CARD domain. RIP3 binds to RIP and TNFR1, mediates TNFR1 induced apoptosis, and attenuates RIP and TNFR1 induced NF-kappa B activation. Overexpression of RIP3 induces apoptosis and NF-kappa B activation. The messenger RNA of RIP3 is expressed in a subset of adult tissues.

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STEAP1 Antibody: The six-transmembrane epithelial antigen of prostate 1 (STEAP1) was the first member of a family of metalloreductases identified as cell-surface antigens in prostate tissue. The normal function of STEAP is still uncertain; unlike other members of the STEAP family, STEAP1 does not promote iron or copper reduction or uptake and lacks the FNO-like reductase domain critical for activity. However, its expression is highly increased in multiple cancer cell lines, including prostate, bladder, colon, and ovarian cancers. Supporting this is evidence that STEAP1 peptides can be used to stimulate CD8+ T cells from healthy donors, enabling them to recognize STEAP1-positive human tumor cells, suggesting that STEAP1 may a potential target for cancer immunotherapy. At least three isoforms of STEAP1 are known to exist.

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LRRC15 may contribute to regulation of cell-matrix adhesion interactions with respect to astrocyte recruitment around senile plaques in Alzheimer's disease brain. LRRC15 is induced by EWS-WT1 (+KTS) in the tumor DSRCT and may play a role in cellular invasion.

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AIM Antibody: Apoptosis inhibitor of macrophages (AIM) is a member of the scavenger receptor cysteine-rich domain superfamily (SRCR-SF) initially identified as an inducible cell surface ligand of CD5. It was shown that AIM functions in the thymus as the inducer of resistance to apoptosis within CD4+/CD8+ thymocytes and as the supporter of the viability of these cells before thymic selection. AIM was also shown to support macrophage survival and enhance their phagocytic function. More recent experiments using recombinant AIM significantly inhibited apoptosis of NKT and T cells obtained from C. parvum-stimulated livers in vitro, suggesting that AIM functions to induce resistance to apoptosis in these cells and supports host defense against inflammation during infection.

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PUMA Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse. PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMA-alpha and PUMA-beta. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.

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TTC5 Antibody: Tetratricopeptide repeat protein 5 (TTC5) is a member of a diverse group of functionally distinct proteins that are characterized by containing one or more tetratricopeptide repeats. Each motif consists of two anti-parallel a-helices such that tandem arrays of TPR motifs generate a right-handed helical structure with an amphipathic channel that may serve to accommodate the complementary region of a target protein. While the exact function of TTC5 remains unclear, it is thought that the TPR motifs serve to mediate protein-protein interactions such as those seen with protein chaperones HSP70 and HSP90 and some proteins involved in cell stress response signaling pathways such as protein phosphatase 5, suggesting that TTC5 may also function via protein-protein interactions mediated by its TPR motifs.

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MDA5 Antibody: The innate immune system detects viral infection by recognizing various viral components and triggers antiviral responses. Like the toll-like receptor 3 (TLR3), the melanoma differentiation-associated protein 5 (MDA5) recognizes double-stranded (ds) RNA, a molecular pattern associated with viral infection. MDA5, a member of the DEAD/DEAH-box RNA helicase family, consists of an amino-terminal caspase recruitment domain (CARD) and a carboxyl-terminal RNA helicase domain similar to that of the related protein RIG-1. When stimulated by dsRNA, MDA5 recruits the adaptor protein VISA and ultimately causes the activation of IRF-3 and NF-kappa B. MDA5 and RIG-1 recognize different types of dsRNA, with MDA5 recognizing poly (I:C). MDA5-null mice were highly susceptible to infection with picornaviruses, which possess such sequences, demonstrating the importance of MDA5 in innate immunity.

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STIM1 Antibody: In T lymphocytes, the sole pathway for Ca++ entry following antigen-receptor binding is through store-operated Ca++-release-activated Ca++ (CRAC) channels. These channels are made up of the pore-forming subunit ORAI1 and the stromal interaction molecule 1 (STIM1), a protein that functions as a Ca++ sensor and activates the CRAC channels, migrating to the plasma membrane from endoplasmic reticulum (ER)-like sites which act as the Ca++ store. A related molecule, STIM2, acts to inhibit the STIM1-mediated store-operated Ca++ entry, and can form complexes with STIM1, suggesting they may play a coordinated role in controlling Ca++ entry. At least two isoforms of STIM1 are known to exist; this antibody will detect only the larger form. This STIM1 antibody is predicted to have no cross-reactivity to STIM2.

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Immunoblotting: 1/5000 - 1/50000, ELISA: 1/5000 - 1/50000, Immunohistochemistry: 1/100 - 1/1000

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TXNDC15, which is short for oredoxin domain-containing protein 15, is encoded by FAM172A gene. It is also known as C5orf14. TXNDC15 is a 360 aa. protein, and has 2 isoforms produced by alternative splicing. There is a natural variant location which is S248P and it has a 18 aa. signal peptide. TXNDC15 contains 1 thioredoxin domain. This protein is a Single-pass type I membrane protein and locates at membrane.

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LIGHT (HVEML; CD258) is a cytokine that binds to TNFRSF3/LTBR. It activates NF-kappaB, stimulates the proliferation of T cells, and inhibits growth of the adenocarcinoma HT-29. Acts as a receptor for Herpes simplex virus.

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Beta-NGF is a neurotrophic factor structurally related to BDNF, NT-3 and NT-4. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Beta-NGF is a potent neurotrophic factor that signals through its receptor Beta-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. Beta-NGF also acts as a growth and differentiation factor for B lymphocytes and enhances B-cell survival. The functional form of human Beta-NGF is a noncovalently disulfide-linked homodimer, of two 13.5 kDa polypeptide monomers (238 total amino acid residues). The three disulfide bonds are required for biological activity.Manufactured using all non-animal reagents.

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Retinol binding protein 4 (RBP4; RBP) is a 21kDa secreted protein, a member of the lipocalin family and is known as the primary transporter of retinol (vitamin A) to tissues. A recent report revealed RBP4 as an adipokine linking glucose transporter 4 (GLUT4) suppression in adipose tissue to insulin. Elevated human and mouse serum RBP4 levels are associated with insulin resistance and its severity, obesity, and certain components of metabolic syndrome. Furthermore, human serum RBP4 levels are closely related to renal function.

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CD99 Antigen-Like Protein 2 (CD99L2) belongs to the CD99 family. CD99L2 is a single-pass type I membrane protein and expressed in many tissues, with low expression in thymus. CD99L2 plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. CD99L2 and CD99 are involved in trans-endothelial migration of neutrophils in vitro and in the recruitment of neutrophils into inflamed peritoneum. A similar protein in mouse functions as an adhesion molecule during leukocyte extravasation. Alternate splicing results in multiple transcript variants.

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Dectin-1 and dectin-2 are type II transmembrane proteins of the C-type lectin family. They contain single carbohydrate recognition domains (CRDs) in their extracellular region. Dectin-1 and dectin-2 are expressed in macrophages and dendritic cells. Dectin-1 recognises beta-glucans with its CRD and signals through its immunoreceptor tyrosine-based activation motif (ITAM)-like motif in the cytoplasmic domain, whereas dectin-2 recognises alpha-mannans and transduces its signal through association with the ITAM-containing Fc receptor gamma-chain.

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CD134 (OX40) is a T cell activation antigen structurally belonging to a lymphocyte-specific subgroup of the nerve growth factor and tumour necrosis factor receptor superfamily, which also includes the T cell antigen CD27, B cell antigen CD40, FAS antigen and the T cell activation antigen 4-1BB. The human CD134 protein is expressed only on activated CD4 + T blasts, and its ligand has been identified as gp34. Interactions between CD134 and its ligand in vivo are necessary for the differentiation of activated B cells into highly immunoglobulin-producing cells, however not involved in other pathways of antigen-driven differentiation of B cells such as development of memory cells in the germinal centers. In addition, the CD134 and gp34 system directly mediate adhesion of activated T cells to vascular endothelial cells, and contribute to growth stimulation of the virus-infected T cells.

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alpha-Galactosidase A is a homodimeric glycoprotein that belongs to the glycosyl hydrolase 27 family. It is a lysosomal enzyme and used as a long-term enzyme replacement therapy in patients with a confirmed diagnosis of Fabry disease. alpha-Galactosidase A can hydrolyze terminal alpha-galactosyl moieties from glycolipids and glycoproteins and catalyze the hydrolysis of melibiose into galactose and glucose. Defects alpha-Galactosidase A are the cause of Fabry disease (FD) which is a rare X-linked sphingolipidosis disease with glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaoslyceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease.

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Irisin is a recently described exercise-induced hormone secreted by skeletal muscle in mice and humans. Irisin activates beige fat cells (beige cells have a gene expression pattern distinct from either white or brown fat and are preferentially sensitive to the polypeptide hormone Irisin). Irisin is cleaved from the type I membrane protein FNDC5 and improves systemic metabolism by increasing energy expenditure.

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SARS matrix peptide is used for blocking the activity of the SARS matrix antibody.

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Alpha-2-HS-glycoprotein (AHSG) is a glycoprotein that is composed of two subunits, the A and B chains, belongs to the Cystatin family of proteases inhibitors. It is highly expressed in embryonic cells and adult hepatocytes, and is expressed to a lesser extent in monocytes/macrophages. AHSG is an important circulating inhibitor of calcification in vivo, and is downregulated during the acute-phase response. It is involved in several functions, such as endocytosis, brain development and the formation of bone tissue. In addition, AHSG may influence the resolution of inflammation by modulating the phagocytosis of apoptotic cells by macrophages. ASHG blocks TGF-beta-dependent signalling in osteoblastic cells.

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Semaphorin-4D is also known as A8,BB18, GR3, CD100. Semaphorin-4D belongs to the semaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domain. It is the cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. It promotes the migration of cerebellar granule cells and of endothelial cells, regulates dendrite and axon branching and morphogenesis. Semaphorin-4D Plays a role in the immune system; Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade.

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Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells, and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils, and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important hemeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens.

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DCLK1 pepide is used for blocking the activity of DCLK1 antibody.

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CD99 is a type I transmembrane glycoprotein and the founding member of the CD99 family of molecules. The extracellular domain of CD99 contains no identifiable motifs, its cytoplasmic region, although short, does have signal transduction capability. Cells known to express CD99 include fibroblasts, neutrophils, T cells, double positive thymocytes, CD34+ stem cells, monocytes and endothelial cells. Two types of CD99 isoforms have been classified. Native human CD99 is referred to as the long, or type I isoform. The best studied type II isoform shows an Asp-Gly substitution for the C terminal 27 amino acids. The type I and II isoforms have distinctive signal transduction pathways (FAKsrc for type I PI3K plus srcERK1/2 for type II), and mediate clearly different biological outcomes. Homophilic interaction between CD99 on the neutrophil and CD99 on the endothelial cell regulates the transendothelial migration of neutrophils during inflammation. Human CD99 has 48% aa sequence identity to mouse CD99.

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OGFOD2 peptide is used for blocking the activity of OGFOD2 antibody.

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19 amino acids near the center of human TRIM24.

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MettL7B peptide is used for blocking the activity of MettL7B antibody.

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Gankyrin is a multicatalytic proteinase oncoprotein consists of 7 ankyrin repeats. Gankyrin overexpressed in most hepatocellular carcinomas. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4 to enhance the ubiquitinylation of p53 by MDM2. Gankyrin is also involved in progression of esophageal squamous cell carcinoma. Gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis.