Product: Phospho-SAMHD1 (Thr592) Antibody
Catalog: DF2986
Description: Rabbit polyclonal antibody to Phospho-SAMHD1 (Thr592)
Application: WB
Reactivity: Human, Mouse
Mol.Wt.: 72KD; 72kD(Calculated).
Uniprot: Q9Y3Z3
RRID: AB_2840965

View similar products>>

   Size Price Inventory
 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

Source:
Rabbit
Application:
WB 1:1000-3000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse
Clonality:
Polyclonal
Specificity:
Phospho-SAMHD1 (Thr592) Antibody detects endogenous levels of SAMHD1 only when phosphorylated at Thr592.
RRID:
AB_2840965
Cite Format: Affinity Biosciences Cat# DF2986, RRID:AB_2840965.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

CHBL2; DCIP; Dendritic cell derived IFNG induced protein; Dendritic cell-derived IFNG-induced protein; Deoxynucleoside triphosphate triphosphohydrolase SAMHD1; dNTPase; HD domain containing 1; HDDC1; Mg11; Monocyte protein 5; MOP 5; MOP-5; MOP5; OTTHUMP00000030889; SAM domain and HD domain 1; SAM domain and HD domain containing protein 1; SAM domain and HD domain-containing protein 1; SAMH1_HUMAN; Samhd1; SBBI88;

Immunogens

Immunogen:

A synthesized peptide derived from human SAMHD1 around the phosphorylation site of Thr592.

Uniprot:
Gene(ID):
Expression:
Q9Y3Z3 SAMH1_HUMAN:

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).

Sequence:
MQRADSEQPSKRPRCDDSPRTPSNTPSAEADWSPGLELHPDYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQIHVDTMKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPELQISERDVLCVQIAGLCHDLGHGPFSHMFDGRFIPLARPEVKWTHEQGSVMMFEHLINSNGIKPVMEQYGLIPEEDICFIKEQIVGPLESPVEDSLWPYKGRPENKSFLYEIVSNKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARVCEVDNELRICARDKEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKADDYIEITGAGGKKYRISTAIDDMEAYTKLTDNIFLEILYSTDPKLKDAREILKQIEYRNLFKYVGETQPTGQIKIKREDYESLPKEVASAKPKVLLDVKLKAEDFIVDVINMDYGMQEKNPIDHVSFYCKTAPNRAIRITKNQVSQLLPEKFAEQLIRVYCKKVDRKSLYAARQYFVQWCADRNFTKPQDGDVIAPLITPQKKEWNDSTSVQNPTRLREASKSRVQLFKDDPM

PTMs - Q9Y3Z3 As Substrate

Site PTM Type Enzyme
M1 Acetylation
S6 Phosphorylation
K11 Ubiquitination
S18 Phosphorylation
T21 Phosphorylation
S23 Phosphorylation
T25 Phosphorylation
S27 Phosphorylation
S33 Phosphorylation
K66 Ubiquitination
S93 Phosphorylation
K98 Ubiquitination
K99 Ubiquitination
S102 Phosphorylation
Y103 Phosphorylation
T138 Phosphorylation
Y146 Phosphorylation
K148 Ubiquitination
Y155 Phosphorylation
S278 Phosphorylation
K288 Ubiquitination
K294 Acetylation
K294 Ubiquitination
K304 Ubiquitination
K312 Ubiquitination
Y315 Phosphorylation
K332 Sumoylation
T384 Phosphorylation
T387 Phosphorylation
K405 Ubiquitination
Y419 Phosphorylation
Y432 Phosphorylation
K446 Ubiquitination
K455 Ubiquitination
K467 Ubiquitination
K469 Sumoylation
K478 Ubiquitination
S482 Phosphorylation
K486 Ubiquitination
Y507 Phosphorylation
S519 Phosphorylation
K534 Ubiquitination
K544 Ubiquitination
Y553 Phosphorylation
K560 Ubiquitination
T579 Phosphorylation
T592 Phosphorylation P24941 (CDK2) , P06493 (CDK1)
K595 Sumoylation
K596 Ubiquitination
S601 Phosphorylation
T608 Phosphorylation
S616 Phosphorylation
K622 Sumoylation

Research Backgrounds

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, 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. Likewise, suppresses LINE-1 retrotransposon activity. Not able to restrict infection by HIV-2 virus; because restriction activity is counteracted by HIV-2 viral protein Vpx. In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools. 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. 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 (By similarity).

PTMs:

Phosphorylation at Thr-592 by CDK1 acts as a switch to control deoxynucleoside triphosphate (dNTPase)-dependent and -independent functions. 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. It also inhibits ability to suppress LINE-1 retrotransposon activity. In contrast, phosphorylation at Thr-592 promotes DNA end resection at stalled replication forks in response to DNA damage.

(Microbial infection) Ubiquitinated following interaction with HIV-2 viral protein Vpx; Vpx promotes interaction and with a DCX (DDB1-CUL4-X-box) E3 ubiquitin ligase, leading to proteasomal degradation.

Subcellular Location:

Nucleus. Chromosome.
Note: Localizes to sites of DNA double-strand breaks in response to DNA damage.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in heart, skeletal muscle, spleen, liver, small intestine, placenta, lung and peripheral blood leukocytes. No expression is seen in brain and thymus.

Subunit Structure:

Homodimer; in absence of GTP and dNTP. Homotetramer; in GTP- and dNTP-bound form. Interacts with MRE11; leading to stimulate the exonuclease activity of MRE11. Interacts with RBBP8/CtIP. Interacts (via its C-terminus) with CD81.

(Microbial infection) Interacts with HIV-2 viral protein Vpx; promoting interaction with a E3 ubiquitin-protein ligase complex containing DCAF1, leading to subsequent ubiquitination and degradation of SAMHD1.

Family&Domains:

In human, and in contrast to mouse protein, the SAM domain is not required for deoxynucleoside triphosphate (dNTPase) activity and ability to restrict infection by viruses.

Belongs to the SAMHD1 family.

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.