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Recombinant Human immunodeficiency virus type 1 group M subtype B Nef protein (nef)

Recombinant Human immunodeficiency virus type 1 group M subtype B Nef protein (nef)

Code	CSB-YP356303HKP
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP356303HKP
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP356303HKP-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP356303HKP
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP356303HKP
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

nef

Uniprot No.

P04601

Alternative Names

nef; Protein Nef; 3'ORF; Negative factor; F-protein) [Cleaved into: C-terminal core protein]

Species

Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)

Expression Region

2-206

Target Protein Sequence

GGKWSKSSV IGWPTVRERM RRAEPAADRV GAASRDLEKH GAITSSNTAA TNAACAWLEA QEEEEVGFPV TPQVPLRPMT YKAAVDLSHF LKEKGGLEGL IHSQRRQDIL DLWIYHTQGY FPDWQNYTPG PGVRYPLTFG WCYKLVPVEP DKIEEANKGE NTSLLHPVSL HGMDDPEREV LEWRFDSRLA FHHVARELHP EYFKNC

Protein Length

Full Length of Mature Protein

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells.; In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impare the membrane fusion event necessary for subsequent virion penetration.; Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis.; Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad.; Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors.

Gene References into Functions

The authors find that both simian immunodeficiency virus and HIV-1 Nef proteins are present in affinity-purified extracellular vesicles derived from cultured cells, as well as in extracellular vesicles from simian immunodeficiency virus-infected macaques. PMID: 29437924
Nef regulates viral pathogenesis through interaction with POTEE and mTORC2 activation in macrophages. PMID: 30391463
Together these findings suggest a possible mechanism of host invasion by HIV-1 through the CAWLEAQ motif of Nef-mediated regulation of ENO1 and identify a potential therapeutic target for HIV-1 entry at mucosal barriers. PMID: 29404888
results demonstrate that HIV-1 Nef's inferior ability to downregulate MHC-B compared to that of MHC-A is conserved across primate lentiviruses and suggest that this property influences antiviral cellular immune responses. PMID: 29046444
These results provide direct evidence that Nef promotes cholesterol deposition in the liver aorta. PMID: 27649790
HIV-1 Nef protein physically interacts with host proteins that regulate protein trafficking [review]. PMID: 27161574
these data suggested that HIV-1 Nef can be a formidable contributor to neurotoxicity along with other factors, which leads to HAND in HIV-1-infected AIDS patients. PMID: 28079886
Data suggest that restriction of HIV-1 particle infectivity by host-cell SERINC5 (which is antagonized by viral Nef) does not depend on alterations in lipid composition and organization of HIV-1 particles and suggest that channeling serine into lipid biosynthesis may not be a cardinal cellular function of SERINC5. (SERINC5 = serine incorporator 5; Nef = nef gene product, HIV1gp9) PMID: 28659343
These results suggest the involvement of HIV-1 nef and human NKG2D-NKG2D ligand interactions in the enhanced susceptibility of HIV-1-infected cells from HIV elite controllers to antibody-dependent cellular cytotoxicity responses. PMID: 28615199
Depletion of the gamma2 or mu1A (AP1M1) subunits of AP-1, but not of gamma1 (AP1G1), precludes Nef-mediated lysosomal degradation of CD4. PMID: 27909244
AP-2alpha depletion enhanced apoptosis, demonstrating that disrupting the HIV-1 Nef:AP-2alpha interaction limits Nef-mediated apoptosis. PMID: 28577469
findings provide a mechanistic explanation for previous observations that dimerization-defective Nef mutants fail to down-regulate CD4 and validate the Nef dimerization interface as a target site for antiretroviral drug development PMID: 28031466
Inhibit interaction between HIV-1 Nef and Calnexin to reverse HIV-induced lipid accumulation and prevent atherosclerosis. PMID: 27470515
results suggest that the antagonism of HIV-1 Nef to SERINC5 restriction of virion infectivity is mediated by a dual mechanism that is related to CD4 downregulation PMID: 27681140
In light of existing report suggesting critical role of Nef-GCC185 interaction reveals valuable mechanistic insights affecting specific protein transport pathway in docking of late endosome derived Rab9 bearing transport vesicle at TGN elucidating role of Nef during viral pathogenesis. PMID: 27105913
The authors found that Akt interacts with HIV-1 Nef protein. In primary T cells treated with exogenous Nef or acutely infected with Nef-expressing HIV-1 in vitro, Akt became phosphorylated on serine(473) and threonine(308). PMID: 27076174
Nef exosomes isolated from the plasma of individuals with HIV-associated dementia (HAD) can induce amyloid beta (1-42) secretion in cultured neurons. PMID: 26407718
The results show that natural polymorphisms within HIV-1 Nef modulate its interaction with natural polymorphisms in the HLA cytoplasmic tails, thereby affecting the efficiency of HLA downregulation and consequent recognition by HIV-specific T cells. PMID: 26787826
HRB knock-down affected CD4 downregulation induced by Nef but not by HIV-1 Vpu. PMID: 26701340
The Nef-GPG motif is required for optimal infectivity of those viruses produced in T-cells. PMID: 26700863
show that HIV-1 promotes tunneling nanotube formation per se via its protein Nef PMID: 26773158
Nef exploits PAK2 in a stepwise mechanism in which its kinase activity cooperates with an adaptor function for the exocyst complex to inhibit host cell actin dynamics. PMID: 26350970
Differential signaling mechanism operates in HIV-1 Nef-mediated production of IL-6 and IL-8 in human astrocytes. PMID: 26075907
HIV-1 Nef down-regulated CD1a lipid antigen presentation in dendritic cells, and involved both Hck and PAK2. PMID: 26584215
TLR2 has a role in the synergistic effect of M. tuberculosis and HIV-1, and their antigens Rv3416 and Nef, respectively, in inhibiting apoptosis of macrophages PMID: 26132135
exosomes are unlikely involved in intercellular Nef transfer. PMID: 25919665
SERINC3 and SERINC5 together restricted HIV-1 replication, and this restriction was evaded by Nef PMID: 26416733
identification of the host transmembrane protein SERINC5, and to a lesser extent SERINC3, as a potent inhibitor of HIV-1 particle infectivity that is counteracted by Nef PMID: 26416734
this study reports the cryo-electron microscopy structures of the Nef- and Arf1-bound AP-1 trimer in the active and inactive states. PMID: 26494761
Nef expression was necessary for both systemic T cell activation and substantial CD4(+) T cell loss from blood and tissues. PMID: 26169178
AP-2 is the most important player for Nef-mediated CD4 downmodulation PMID: 26423947
These results lead to a model for the docking of the full AP-2 tetramer to membranes as bound to Nef, such that the cytosolic tail of CD4 is situated to interact with its binding site on Nef. PMID: 24473078
our study identifies selectively expressed mRNAs in Nef-expressing U937 cells and their exosomes and supports a new mode on intercellular regulation by the HIV-1 Nef protein. PMID: 25961023
unifying picture of Nef functions based on old and new experimental results evidencing that Nef also influence the cytokine network[review] PMID: 25529283
Overall study determines modulation of cellular protein expression in T cells by HIV-1 Nef PMID: 25874870
Results suggest that Nef protein expressed by transfected astrocytes implanted in rat hippocampus activates the immune system leading to neuronal damage and spatial and recognition memory deficits PMID: 22926191
HIV-1 Nef, a key factor for viral pathogenesis, downregulates functionally important molecules from the surface of infected cells, including the viral entry receptor CD4 and coreceptors CCR5 and CXCR4. PMID: 26178998
Ile-20 within HIV-1 subtype B Nef is associated with poorer disease outcome. PMID: 26060058
Altogether, the findings suggest that the mechanisms of infectivity enhancement by Nef are different between HIV-1 and SIVmac239. PMID: 25519983
Nef domains involved in CD4 downregulation were necessary for activation of plasmacytoid dendritic Cell. PMID: 25972534
These results support enhanced Nef-mediated HLA class II immune evasion activities in acute/early compared to chronic infection, highlighting the potential importance of these functions following HIV-1 transmission. PMID: 25998395
Together, these results suggested that HIV-1 preferential infection of CD4(+)CTLA-4(+) T cells in vivo was followed by Nef-mediated concomitant downregulation of both CD4 and CTLA-4 upon transition to productive infection. PMID: 25626682
Taken together, these data indicate that Nef is a critical viral protein for incorporating nascent proviral DNA into host chromosomes in resting peripheral mononuclear leukocytes and that this occurs through interaction with INI1. PMID: 25559666
Authors identified a cis element in the 5'UTR of Nef mRNA essential for efficient Nef translation, which was named the Nef-translation essential region (NER). PMID: 24981044
Nef-induced apoptosis is mediated through reactive oxygen species-dependent mechanisms. PMID: 24608713
Nef markedly activated TAK1 in M-CSF-derived M2-MPhi but not in GM-CSF-derived M1-MPhi. PMID: 24874739
Interaction with the Src homology (SH3-SH2) region of the Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment. PMID: 25122770
HIV-1 Nef impairs key functional activities in human macrophages through CD36 downregulation. PMID: 24705461
HIV-1 Nef interacts with Alix in late endosomes, and this is required for efficient lysosomal targeting of CD4. PMID: 25118280
These results demonstrate that early Nef clones from HIV controllers displayed lower HLA class I and CD4 downregulation activity, as well as a reduced ability to enhance virion infectivity. PMID: 24965469