Recombinant Mouse Deoxynucleoside Triphosphate Triphosphohydrolase Samhd1 (SAMHD1) Protein (His)

Name: Recombinant Mouse Deoxynucleoside Triphosphate Triphosphohydrolase Samhd1 (SAMHD1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10283P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Deoxynucleoside Triphosphate Triphosphohydrolase Samhd1 (SAMHD1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q60710
Target Symbol	SAMHD1
Synonyms	Samhd1; Mg21; Deoxynucleoside triphosphate triphosphohydrolase SAMHD1; dNTPase; EC 3.1.5.-; Interferon-gamma-inducible protein Mg11; SAM domain and HD domain-containing protein 1; mSAMHD1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DIMITDAFLKADPYVEITGTAGKKFRISTAIDDMEAFTKLTDNIFLEVLHSTDPQLSEAQSILRNIECRNLYKYLGETQPKREKIRKEEYERLPQEVAKAKPEKAPDVELKAEDFIVDVINVDYGMEDKNPIDRVHFYCKSNSKQAVRINKEQVSQLLPEKFAEQLIRVYCKKKDGKSLDAAGKHFVQWCALRDFTKPQDGDIIAPLITPLKWNNKTSSCLQEVSKVKTCLK
Expression Range	395-626aa
Protein Length	Partial
Mol. Weight	30.6kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: 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. Likewise, suppresses LINE-1 retrotransposon activity. In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools. Phosphorylation at Thr-634 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. 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. 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. Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity. Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation.
Subcellular Location	Nucleus. Chromosome.
Protein Families	SAMHD1 family
Database References	KEGG: mmu:56045 STRING: 10090.ENSMUSP00000059717 UniGene: Mm.248478

Gene Functions References

SAMHD1 inhibits NF-kappaB activation by interacting with NF-kappaB1/2 and reducing phosphorylation of the NF-kappaB inhibitory protein IkappaBalpha. SAMHD1 also interacts with the inhibitor-kappaB kinase epsilon (IKKepsilon) and IFN regulatory factor 7 (IRF7), leading to the suppression of the IFN-I induction pathway by reducing IKKepsilon-mediated IRF7 phosphorylation. SAMHD1 down-regulates innate immune responses to ... PMID: 29610295
SAMHD1's restriction of dNTP supply enhances AID's mutagenicity and that the evolution of Ig hypermutation included the repurposing of antiviral mechanisms based on dNTP starvation. PMID: 29669924
SAMHD1 crystal structure delineates the SAMHD1 allosteric activation process that governs SAMHD1 enzymatic activities. PMID: 29379009
provide genetic evidence that cell-autonomous control of lentivirus infection in myeloid cells by SAMHD1 limits virus-induced production of interferons and the induction of co-stimulatory markers PMID: 27477283
These data support a model in which SAMHD1 catalytic activity is regulated through tetramer stabilization by the carboxyl-terminal tail, phosphorylation destabilizing the complexes and inactivating the enzyme. ISF2 may serve to reduce the dNTP pool to very low levels as a means of restricting virus replication. PMID: 27920203
These observations suggest that heterozygous cancer-associated SAMHD1 mutations increase mutation rates in cancer cells. PMID: 27071091
SAMHD1 in the mouse blocks retroviral infection at the level of reverse transcription and is regulated through cell cycle-dependent phosphorylation. PMID: 26667483
phosphorylation of mSAMHD1 at T634 by CDK1/2 negatively regulates its HIV-1 restriction in differentiated cells, but does not affect its murine leukemia virus restriction in dividing cells. PMID: 26580513
SAMHD1 restricts HIV-1 replication and regulates interferon production in mouse myeloid cells. PMID: 24586870
Allosteric regulation by dATP and dTTP works similarly in human and mouse SAMHD1. PMID: 24828500
SAMHD1 decreases dNTP pool in murine cells, restricts retroviral replication and regulates type I IFN production. PMID: 23972988
SAMHD1 can restrict lentiviruses in vivo and that nucleotide starvation is an evolutionarily conserved antiviral mechanism. PMID: 23872947
there are several Vpx residues required for SAMHD1 degradation PMID: 23076149
Vpx targets SAMHD1 for degradation in a viral strategy to control cellular deoxynucleotide levels for efficient replication PMID: 22069334

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.