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anti-Mouse (Murine) Antibodies:
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Mouse (Murine) Monoclonal RSAD2 Primary Antibody for FACS, IF - ABIN2191757
Lackman, Jamieson, Griffith, Geuze, Cresswell: Innate immune recognition triggers secretion of lysosomal enzymes by macrophages. in Traffic (Copenhagen, Denmark) 2007
Viperin N-terminal is necessary for the interaction with Junin viral nucleoprotein.
viperin also reduced the stability of several other viral proteins in a NS3-dependent manner, suggesting a central role of NS3 in viperin's antiflavivirus activity.
RSAD2 and AIM2 Modulate Coxsackievirus A16 and Enterovirus A71 Replication in Neuronal Cells in Different Ways That May Be Associated with Their 5' Nontranslated Regions.
Data suggest that CIA2B and MMS19 (show MMS19 Antibodies) physically interact with C-terminus of viperin/RSAD2; CIAO1 (show CIAO1 Antibodies) appears to function as primary viperin-interacting protein; CIA2A binds to N-terminus of viperin in CIAO1 (show CIAO1 Antibodies)-, CIA2B-, and MMS19 (show MMS19 Antibodies)-independent fashion. (CIA2B = metallochaperone CIA2B/FAM96B (show FAM96B Antibodies); MMS19 (show MMS19 Antibodies) = transcription factor MMS19 (show MMS19 Antibodies); CIAO1 (show CIAO1 Antibodies) = cytosolic iron-sulfur assembly component 1; CIA2A = metallochaperone CIA2A/Fam96a (show FAM96A Antibodies))
Data suggest that human viperin exerts "ancient radical" SAM (show TTN Antibodies)-dependent activity in invading bacteria such as Escherichia coli; here, expression of recombinant viperin induces dramatically elongated morphology of "host"/pathogen cells. (SAM (show TTN Antibodies) = S-adenosylmethionine)
Exposure to hepatitis B virus up-regulates viperin expression in vivo and in vitro in placental trophoblast, and lack of this up-regulation is associated with intrauterine transmission of hepatitis B virus.
Viperin was localized in trophoblast cells. HCMV IE1 mRNA expression was significantly inhibited by viperin RNA interference.
data suggested that viperin impaired respiratory syncytial virus (RSV) transmission by inhibiting virus filament formation, providing a basis for its anti-virus activity in RSV-infected cells
Viperin inhibits viral replication by interactiing with host cell proteins and viral proteins. [review]
These data suggest that viperin requires CIAO1 (show CIAO1 Antibodies) for [4Fe-4S] cluster assembly, and acts through an enzymatic, Fe-S cluster- and SAM (show TTN Antibodies)-dependent mechanism to inhibit viral RNA synthesis.
The viperin putative active site contains several conserved positively charged residues, and a portion of the active site shows structural similarity to the GTP-binding (show RND2 Antibodies) site of MoaA, suggesting that the viperin substrate may be a nucleoside triphosphate of some type.
miR (show MLXIP Antibodies)-200 family may potentially promote podocyte differentiation through repression of RSAD2 expression.
data support the therapeutic potential for viperin to inhibit RABV replication, which appears to involve upstream regulation by TLR4 (show TLR4 Antibodies).
A relatively high level of viperin protein expression was detected in infected RAW 264.7 cells, and it was extensively localized throughout the cytoplasm of infected cells
The data indicate that viperin is the major effector underlying the ability of HCMV to regulate cellular lipid metabolism.
The viperin-deficient mouse model indicated that absence of viperin enhanced neither the viral load nor pulmonary damage in the lungs.
Viperin(-/-) adult mice infected with West Nile virus via the subcutaneous or intracranial route showed increased lethality and/or enhanced viral replication in central nervous system (CNS) tissues.
study shows human cytomegalovirus (HCMV)-induced viperin disrupts cellular metabolism to enhance infectious process; viperin interaction with vMIA resulted in viperin relocalization from endoplasmic reticulum to mitochondria
Viperin may play a central role in bacterial or parasitic infections and may protect neutrophils and macrophages from infection.
Vesicular stomatitis virus (VSV)-mediated viperin induction occurs independently of interferon (show IFNA Antibodies) (IFN), through IFN regulatory factor (IRF)-1 (show IRF1 Antibodies); the transcriptional upregulation of viperin is sufficient to reduce VSV replication.
protein involved in bone formation
radical S-adenosyl methionine domain-containing protein 2
, inflammatory response gene 6 protein
, virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible
, cytomegalovirus-induced gene 5 protein
, VHSV-induced-like protein
, viral hemorrhagic septicemia virus (VHSV)-induced gene 1
, bone-expressed sequence tag 5 protein