Anti-AlaRS antibody (ab139993)
Key features and details
- Rabbit polyclonal to AlaRS
- Suitable for: ICC/IF, WB
- Reacts with: Mouse, Human
- Isotype: IgG
Overview
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Product name
Anti-AlaRS antibody
See all AlaRS primary antibodies -
Description
Rabbit polyclonal to AlaRS -
Host species
Rabbit -
Tested Applications & Species
See all applications and species dataApplication Species ICC/IF HumanWB Human
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Immunogen
Recombinant fragment corresponding to amino acids 695-968 (UniProt ID: Q8CFX8) of Hamster AlaRS with proprietary tag.
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Positive control
- HeLa and NIH3T3 whole cell lysates
Properties
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Form
Liquid -
Storage instructions
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles. -
Storage buffer
pH: 6
Preservative: 0.05% Sodium azide -
Concentration information loading... -
Purity
Whole antiserum -
Clonality
Polyclonal -
Isotype
IgG -
Research areas
Associated products
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Compatible Secondaries
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Isotype control
Applications
The Abpromise guarantee
Our Abpromise guarantee covers the use of ab139993 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Tested applications are guaranteed to work and covered by our Abpromise guarantee.
Predicted to work for this combination of applications and species but not guaranteed.
Does not work for this combination of applications and species.
| Application | Species |
|---|---|
| ICC/IF |
Human
|
| WB |
Human
|
| All applications |
Rat
Guinea pig
Cow
|
| Application | Abreviews | Notes |
|---|---|---|
| ICC/IF |
1/100.
|
|
| WB |
1/100 - 1/1000. Predicted molecular weight: 107 kDa.
|
| Notes |
|---|
|
ICC/IF
1/100. |
|
WB
1/100 - 1/1000. Predicted molecular weight: 107 kDa. |
Target
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Function
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. -
Involvement in disease
Charcot-Marie-Tooth disease 2N -
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. -
Domain
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
The C-terminal C-Ala domain (residues 756 to 968), along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The human domain can be used in vitro to replace the corresponding domain in E.coli. -
Post-translational
modificationsISGylated. -
Cellular localization
Cytoplasm. - Information by UniProt
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Database links
- Entrez Gene: 510933 Cow
- Entrez Gene: 16 Human
- Entrez Gene: 234734 Mouse
- Entrez Gene: 292023 Rat
- Omim: 601065 Human
- SwissProt: P49588 Human
- SwissProt: Q8BGQ7 Mouse
- SwissProt: P50475 Rat
see all -
Alternative names
- AARS antibody
- AI316495 antibody
- Alanine tRNA ligase 1, cytoplasmic antibody
see all
Images
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Immunocytochemistry/ Immunofluorescence - Anti-AlaRS antibody (ab139993)
Immunocytochemistry/ Immunofluorescence analysis of HeLa cells labeling AlaRS with ab139993 at 1/100 dilution. The cells were fixed with 4% paraformaldehyde and permeabilized with 0.25% TritonX100. Alexa Fluor 488 conjugated goat anti-rabbit IgG antibody was used as the secondary antibody at 1/1,000 dilution. Nuclear DNA was stained with DAPI (left) and the merged image was shown in the center.
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Western blot - Anti-AlaRS antibody (ab139993)All lanes : Anti-AlaRS antibody (ab139993) at 1/100 dilution
Lane 1 : HeLa whole cell lysate
Lane 2 : NIH3T3 whole cell lysate
Lysates/proteins at 10 µg per lane.
Predicted band size: 107 kDa
Datasheets and documents
References (0)
ab139993 has not yet been referenced specifically in any publications.
