Recombinant Human SAMHD1 protein is a Human Full Length protein, in the 1 to 626 aa range, expressed in Wheat germ, with >=80% purity and suitable for ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:26294762, PubMed:26431200, PubMed:28229507, PubMed:28834754, PubMed:29670289). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses, such as HIV-1: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23364794, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:25038827, PubMed:26101257, PubMed:26294762, PubMed:26431200, PubMed:28229507). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:24035396, PubMed:24217394, PubMed:29610582). Not able to restrict infection by HIV-2 virus; because restriction activity is counteracted by HIV-2 viral protein Vpx (PubMed:21613998, PubMed:21720370). In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (PubMed:23858451). Phosphorylation at Thr-592 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (PubMed:23601106, PubMed:23602554, PubMed:29610582, PubMed:29670289). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (PubMed:29670289). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (PubMed:27477283, PubMed:29670289). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (PubMed:29670289). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation (By similarity).
MOP5, SAMHD1, Deoxynucleoside triphosphate triphosphohydrolase SAMHD1, dNTPase, Dendritic cell-derived IFNG-induced protein, Monocyte protein 5, SAM domain and HD domain-containing protein 1, DCIP, MOP-5, hSAMHD1
Recombinant Human SAMHD1 protein is a Human Full Length protein, in the 1 to 626 aa range, expressed in Wheat germ, with >=80% purity and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Glutathione Sepharose
Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:26294762, PubMed:26431200, PubMed:28229507, PubMed:28834754, PubMed:29670289). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses, such as HIV-1: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (PubMed:19525956, PubMed:21613998, PubMed:21720370, PubMed:22056990, PubMed:23364794, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:25038827, PubMed:26101257, PubMed:26294762, PubMed:26431200, PubMed:28229507). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:24035396, PubMed:24217394, PubMed:29610582). Not able to restrict infection by HIV-2 virus; because restriction activity is counteracted by HIV-2 viral protein Vpx (PubMed:21613998, PubMed:21720370). In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (PubMed:23858451). Phosphorylation at Thr-592 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (PubMed:23601106, PubMed:23602554, PubMed:29610582, PubMed:29670289). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (PubMed:29670289). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (PubMed:27477283, PubMed:29670289). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (PubMed:29670289). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation (By similarity).
Belongs to the SAMHD1 family.
Phosphorylation at Thr-592 by CDK1 acts as a switch to control deoxynucleoside triphosphate (dNTPase)-dependent and -independent functions (PubMed:29670289). Phosphorylation at Thr-592 takes place in cycling cells: it reduces the stability of the homotetramer, impairing the dNTPase activity and subsequent ability to restrict infection by viruses (PubMed:23601106, PubMed:23602554, PubMed:26294762, PubMed:26431200, PubMed:31291580). It also inhibits ability to suppress LINE-1 retrotransposon activity (PubMed:29610582). In contrast, phosphorylation at Thr-592 promotes DNA end resection at stalled replication forks in response to DNA damage (PubMed:29670289).
SAMHD1 also known as Sterile Alpha Motif and HD-Domain Containing Protein 1 functions mechanically as a dGTP-dependent deoxynucleotide triphosphohydrolase. It has a molecular mass of approximately 72 kDa. This protein is expressed in various cell types most notably in immune cells such as macrophages and dendritic cells. SAMHD1 operates by hydrolyzing deoxynucleoside triphosphates (dNTPs) into deoxynucleosides and inorganic triphosphates controlling the intracellular pool of dNTPs.
SAMHD1 serves as a modulator of cellular proliferation and DNA repair processes. It forms part of a larger complex that regulates DNA replication through its influence on dNTP levels. By modulating these levels the protein prevents excess dNTP buildup which can result in inefficient replication and genomic instability. Moreover SAMHD1 contributes to the innate immune response by restricting viral replication particularly that of retroviruses like HIV-1 in non-dividing cells.
SAMHD1 participates in nucleotide metabolism and DNA damage response pathways. For effective dNTP pool regulation it interacts with proteins involved in dNTP synthesis and degradation such as RRM2B. Additionally SAMHD1 is relevant in pathways connected to the restriction of viral infections working alongside proteins like TREX1 that degrade excess DNA and sustain genomic integrity during infection.
SAMHD1 mutations associate with autoimmune disorders and certain types of cancers. Aicardi-Goutières syndrome a rare genetic inflammatory disorder shows links to defective SAMHD1 activity where impaired DNA damage response leads to chronic inflammation. Furthermore altered SAMHD1 expression relates to chronic lymphocytic leukemia where it influences both the proliferation and survival of malignant cells. Interaction with proteins such as DNA-PK is significant in linking SAMHD1 to these conditions demonstrating its role in maintaining immune system balance and genomic stability.
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ab153254 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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