SAMHD1 Antibody (Center)
Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)
|Application ||WB, E|
|Calculated MW||H=72,69,64,68 KDa|
|Antigen Region||204-230 aa|
|Other Names||Deoxynucleoside triphosphate triphosphohydrolase SAMHD1, dNTPase, 315-, Dendritic cell-derived IFNG-induced protein, DCIP, Monocyte protein 5, MOP-5, SAM domain and HD domain-containing protein 1, SAMHD1, MOP5|
|Target/Specificity||This SAMHD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 204-230 amino acids from the Central region of human SAMHD1.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SAMHD1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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:23602554, PubMed:23601106, PubMed:22056990, 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:23602554, PubMed:23601106, PubMed:23364794, PubMed:25038827, PubMed:26101257, PubMed:22056990, PubMed:24336198, PubMed:28229507, PubMed:26294762, PubMed:26431200). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:24035396, PubMed:29610582, PubMed:24217394). 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:23602554, PubMed:23601106, 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).|
|Cellular Location||Nucleus Chromosome. Note=Localizes to sites of DNA double-strand breaks in response to DNA damage|
|Tissue Location||Expressed in heart, skeletal muscle, spleen, liver, small intestine, placenta, lung and peripheral blood leukocytes (PubMed:11064105). No expression is seen in brain and thymus (PubMed:11064105).|
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Provided below are standard protocols that you may find useful for product applications.
This gene may play a role in regulation of the innate immune response. The encoded protein is upregulated in response to viral infection and may be involved in mediation of tumor necrosis factor-alpha proinflammatory responses. Mutations in this gene have been associated with Aicardi-Goutieres syndrome. [provided by RefSeq].
Tomkova, H., et al. Eur J Dermatol 20(3):411-413(2010)
Dale, R.C., et al. Am. J. Med. Genet. A 152A (4), 938-942 (2010) :
Davila, S., et al. Genes Immun. 11(3):232-238(2010)
Rice, G.I., et al. Nat. Genet. 41(7):829-832(2009)
Liao, W., et al. Proteomics 8(13):2640-2650(2008)
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