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Merck
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SAB4200614

Sigma-Aldrich

Monoclonal Anti-SAMHD1 antibody produced in mouse

~1.0 mg/mL, clone SM1.1, purified immunoglobulin

Synonym(s):

Anti-CHBL2, Anti-DCIP, Anti-HDDC1, Anti-MOP-5, Anti-RP1-132F21.1, Anti-SAM domain and HD domain-containing protein 1, Anti-SBBI88, Anti-dendritic cell-derived IFNG-induced protein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

Key Documents

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biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

SM1.1, monoclonal

form

buffered aqueous solution

mol wt

antigen ~72 kDa

species reactivity

monkey, human

concentration

~1.0 mg/mL

technique(s)

immunoblotting: 0.5-1.0 μg/mL using HeLa total cell extracts
immunocytochemistry: suitable
immunofluorescence: 5-10 μg/mL using HeLa cells

isotype

IgG1

UniProt accession no.

Q9Y3Z3

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SAMHD1(25939)

General description

Monoclonal Anti-SAMHD1 (mouse IgG1 isotype) is derived from the hybridoma SM1.1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. SAM and HD domain-containing deoxynucleoside triphosphate triphosphohydrolase 1 (SAMHD1) is expressed at basal levels in a large number of tissues but is highly expressed in dendritic cells and other cells of the myeloid lineage. It is made up of sterile alpha motif (SAM) and an HD domain which occur in tandem. SAMDH1 is mapped on the human chromosome at 20q11.23.

Immunogen

synthetic peptide corresponding to a sequence at the C-terminal region of human SAMHD1

Application

Monoclonal Anti-SAMHD1 antibody produced in mouse may be used in:
  • immunoblotting
  • flow cytometry
  • immunocytochemistry

Biochem/physiol Actions

Monoclonal Anti-SAMHD1 recognizes human and monkey SAMHD1.
Mutations in SAM and HD domain-containing deoxynucleoside triphosphate triphosphohydrolase 1 (SAMHD1) are associated with Aicardi-Goutières syndrome (AGS), a severe genetic infantile encephalopathy characterized by chronic cerebrospinal fluid lymphocytosis, elevated levels of interferon-α. Lower levels of SAMHD1 leads to the accumulation of full-length human immunodeficiency virus (HIV) DNA.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Preparation Note

For extended storage, freeze at -20 °C in working aliquots. Repeated freezing and thawing,or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation beforeuse. Working dilution samples should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
098M4872V
093M4829V

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Mutations involved in Aicardi-Goutieres syndrome implicate SAMHD1 as regulator of the innate immune response
Rice G I, et al.
Nature Genetics, 41(7), 829-832 (2009)
How SAMHD1 changes our view of viral restriction
Laguette N and Benkirane M.
Trends in Immunology, 33(1), 26-33 (2012)
Combination of exome sequencing and immune testing confirms Aicardi-Goutieres syndrome type 5 in a challenging pediatric neurology case
Haskell G T, et al.
Cold Spring Harbor molecular case studies, 4(5), a002758-a002758 (2018)
SAMHD1 is the dendritic-and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx
Laguette N, et al.
Nature, 474(7353), 654-657 (2011)
M Chodorge et al.
Cell death and differentiation, 19(7), 1187-1195 (2012-01-21)
Receptor agonism remains poorly understood at the molecular and mechanistic level. In this study, we identified a fully human anti-Fas antibody that could efficiently trigger apoptosis and therefore function as a potent agonist. Protein engineering and crystallography were used to

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