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Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.

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For WB starting dilution is: 1:1000.

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Anti-STYX Rabbit Polyclonal Antibody

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FREM1 peptide is used for blocking the activity of FREM1 antibody.

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NBEAL1 belongs to the WD repeat neurobeachin family. It contains 1 BEACH domain and 2 WD repeats. NBEAL1 is highly expressed in brain, kidney, prostate and testis and weakly expressed in ovary, small intestine, colon and peripheral blood leukocytes. It may be correlative to several tumors, such as ovary serous adenocarcinoma and metastasis mammary gland carcinoma breast.

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KLF1 is a transcription factor, originally identified in this laboratory, which plays a crucial role as a transcriptional activator at the adult beta-globin locus.

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cIAP Antibody: Apoptosis, or programmed cell death, is related to many diseases, such as cancer. Apoptosis is triggered by a variety of stimuli including members in the TNF family and can be prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. The two isoforms of c-IAP (c-IAP1 and c-IAP2) are structurally related to XIAP, containing 3 baculoviral IAP repeat (BIR) motifs that are essential and sufficient for the binding and inhibition of caspases-3, -7. The c-IAPs can associate with the death receptor TNF-R2, and mediate the ubiquitinization of TRAF2 following the binding of TNF-alpha by its receptor. Omi, a negative regulator of c-IAP, inhibits its activity by catalytically cleaving c-IAP. Another negative regulator, Smac/DIABLO, acts by enhancing the auto-ubiquitization activity of c-IAP.

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Anti-MKL1 Rabbit Polyclonal Antibody

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FEZ2 peptide is used for blocking the activity of FEZ2 antibody.

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Anti-SECISBP2 Goat Polyclonal Antibody

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Anti-REG1A Rabbit Polyclonal Antibody

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ARL13B has an evolutionarily conserved role mediating cilia function in multiple organs. N and C domains of ARL13B cooperatively regulate its ciliary localization and that N domain-dependent self-association of Arl13b may be important for its function in cilia biogenesis.

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FAM119A is a multi-pass membrane protein. It belongs to the FAM119 family. The function of the FAM119A protein remains unknown.

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Anti-CD80 Recombinant Antibody [Clone: 16C10]

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BCMA Antibody: Members in the TNF superfamily regulate immune responses and induce apoptosis. Two novel members in the TNF family were recently identified and designated BAFF/BLyS/TALL-1/THANK/zTNF4 and April/TALL-2, respectively. BAFF was characterized as a B cell activator since it induced B cell proliferation and immunoglobulin secretion. April regulates immunological and non-immunological cell growth. Three receptors, BCMA (for B cell maturation protein), TACI, and BAFF-R, for BAFF were recently identified. BCMA, like TACI, binds BAFF and April. BAFF and its receptors induce B cell development and survival, activate NF-kappa B and c-jun N-terminal kinase, and are involved in B cell associated autoimmune diseases.

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EXOC3 is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and functions of exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. The complex is also essential for the biogenesis of epithelial cell surface polarity.The protein encoded by this gene is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and functions of exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. The complex is also essential for the biogenesis of epithelial cell surface polarity.