Vac14 Antibody

Cat. No.: HY-P810298: Data Sheet COA
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Vac14 Antibody is a Rabbit-derived and non-conjugated IgG polyclonal antibody, targeting to Vac14.

For research use only. We do not sell to patients.

Size	Stock	Quantity
20 μL	In-stock	Estimated Time of Arrival: December 31
50 μL	In-stock	Estimated Time of Arrival: December 31
100 μL	In-stock	Estimated Time of Arrival: December 31
250 μL	Get quote

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Vac14 Antibody Featured Recommendations:

WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Background
Documentation

Description

Vac14 Antibody is a Rabbit-derived and non-conjugated IgG polyclonal antibody, targeting to Vac14.

Host

Rabbit

Molecular Weight

Predicted band size: 86.2 kDa

Species Reactivity

Human, Mouse, Rat

SwissProt ID

O95786

Application &
Dilution Ratio

Application	Dilution Ratio
WB WB: Western Blot	1:1000-2000

Purity	Affinity purified	Conjugation	Non-conjugated
Isotype	IgG

Appearance

Solution

Formulation

Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05% BSA.

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

Shipping

Shipping with blue ice.

Background

Function：Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines (PubMed:15208624, PubMed:15708988, PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:17190814, PubMed:18636086, PubMed:19122199, PubMed:19211564, PubMed:24366338, PubMed:28469175, PubMed:29117565, PubMed:31006531, PubMed:34935440, PubMed:35263596, PubMed:36793726). Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments (PubMed:15208624, PubMed:15708988). The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms (PubMed:28469175, PubMed:31006531). Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons (PubMed:28469175, PubMed:31006531). Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length) (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV) (PubMed:21616437, PubMed:21884169). It also detects rotaviruses and reoviruses (PubMed:21616437, PubMed:21884169). Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.74). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV) (PubMed:19631370). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration

Subcellular Localization：Cytoplasm; Cell projection, ruffle membrane; Cytoplasm, cytoskeleton; Cell junction, tight junction

Expression：
Tissue_specificity:It exists in vascular smooth muscle cells (protein level) .

Induction:By bacterial lipopolysaccharides (LPS) in endothelial cells. By interferon (IFN)

Isoforms & Post-Translational Modification：O95786 has 2 isomers: O95786-1: 106600 Da (predicted); O95786-2: 101377 Da (predicted).
Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-770, Ser-854 and Ser-855 results in inhibition of its activity while dephosphorylation at these sites results in its activation;Ubiquitinated. 'Lys-63' ubiquitination by RNF135, which occurs after RNA-binding and homodimerization, releases the autoinhibition of the CARD domains by the RLR CTR domain, an essential step in the activation of the RIG-I signaling pathway (PubMed:23950712, PubMed:28469175, PubMed:31006531). Lys-172 is the critical site of ubiquitination for MAVS/IPS1 binding and to induce anti-viral signal transduction (PubMed:17392790, PubMed:30193849). Lys-154, Lys-164 and Lys-172 are shared sites for RNF135-mediated and TRIM4-mediated ubiquitination (PubMed:19017631, PubMed:19484123, PubMed:24755855). Also undergoes 'Lys-48' ubiquitination at Lys-181 by RNF125 that leads to proteasomal degradation (PubMed:17460044, PubMed:26471729). 'Lys-48' ubiquitination follows viral infection and is enhanced by 'Lys-63'-linked ubiquitination of the CARD domains that promotes interaction with VCP/p97 and subsequent recruitment of RNF125 (PubMed:17460044, PubMed:26471729). Within a negative feedback loop involving SIGLEC10 and PTPN11, 'Lys-48' ubiquitination at Lys-812 by CBL also elicits the proteasomal degradation of RIGI (By similarity). Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains (PubMed:18636086). Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'- and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor (PubMed:20368735). Ubiquitinated by TRIM40 via 'Lys-48'-linked ubiquitination; leading to proteasomal degradation (PubMed:29117565). Deubiquitinated by USP27X that cleaves 'Lys-63'-linked ubiquitin chains and inhibits the innate immune receptor activity (PubMed:32027733). Deubiquitinated by USP3 that also cleaves 'Lys-63'-linked ubiquitin chains and inhibits the innate immune receptor activity (PubMed:24366338). Undergoes 'Lys-48'-linked ubiquitination catalyzed by MARCHF5 at Lys-193 and Lys-203, leading to proteasomal degradation (PubMed:31881323);Phosphorylated at Ser-8 and Thr-170; these phosphorylations suppresse the TRIM25-mediated 'Lys-63'-linked ubiquitination of RIG-I and thereby prevents RIG-I downstream signaling. Dephosphorylated by phosphatases PPP1CA/PPP1CC; this step is essential to activate RIGI and initiate downstream signaling;ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response;Sumoylated, probably by MUL1; inhibiting its polyubiquitination;Acetylated in response to RNA virus infection (PubMed:26746851). Deacetylated by HDAC6 in the presence of viral mRNAs which is required for detection of viral RNA by RIGI (PubMed:26746851);(Microbial infection) Deamidated on Asn-495 and Asn-549 by herpes simplex virus 1 protein UL37. These modifications eliminate RIGI detection of viral RNA and restriction of viral replication;Degraded via selective autophagy following interaction with IRGM (PubMed:32715615). IRGM promotes RIGI recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagic degradation (PubMed:32715615);(Microbial infection) Cleaved by the protease 3C of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production;(Microbial infection) Phosphorylated at Ser-8 by herpes simplex virus 1 protein US3 leading to inhibition of critical RIGI activation steps

Subunit：Monomer; maintained as a monomer in an autoinhibited state. Upon binding of viral RNAs and conformational shift, homooligomerizes and forms filaments on these molecules (PubMed:26471729, PubMed:31881323).

Synonyms

DDX58, RIGI, Antiviral innate immune response receptor RIG-I, ATP-dependent RNA helicase DDX58, DEAD box protein 58, RIG-I-like receptor 1, RNA sensor RIG-I, Retinoic acid-inducible gene 1 protein, Retinoic acid-inducible gene I protein, RLR-1, RIG-1, RIG-I

Documentation

Select Batch:

Data Sheet (230 KB) SDS (251 KB)

COA (204 KB)

User Guide for Antibodies (1077 KB)

Vac14 Antibody Related Classifications

Help & FAQs

Do most proteins show cross-species activity?
Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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Vac14 Antibody

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Product Detail

Background

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Vac14 Antibody Related Classifications

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