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Merck
CN

SAB4200614

Monoclonal Anti-SAMHD1 antibody produced in mouse

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

别名:

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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关于此项目

NACRES:
NA.41
UNSPSC Code:
12352203
Clone:
SM1.1, monoclonal
Species reactivity:
monkey, human
Application:
ICC, IF
Citations:
5
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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.

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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存储类别

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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)
How SAMHD1 changes our view of viral restriction
Laguette N and Benkirane M.
Trends in Immunology, 33(1), 26-33 (2012)
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)
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)
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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