Recombinant Anti-AlaRS antibody [EPR11037(B)] - BSA and Azide free (ab249194)
Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- Rabbit monoclonal [EPR11037(B)] to AlaRS - BSA and Azide free
- Suitable for: Flow Cyt (Intra), IHC-P, WB
- Reacts with: Human
Related conjugates and formulations
Overview
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Product name
Anti-AlaRS antibody [EPR11037(B)] - BSA and Azide free
See all AlaRS primary antibodies -
Description
Rabbit monoclonal [EPR11037(B)] to AlaRS - BSA and Azide free -
Host species
Rabbit -
Tested applications
Suitable for: Flow Cyt (Intra), IHC-P, WBmore details
Unsuitable for: ICC/IF or IP -
Species reactivity
Reacts with: Human -
Immunogen
Synthetic peptide. This information is proprietary to Abcam and/or its suppliers.
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General notes
ab249194 is the carrier-free version of ab155275.
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. The carrier-free buffer and high concentration allow for increased conjugation efficiency.
This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our conjugation kits for antibody conjugates that are ready-to-use in as little as 20 minutes with <1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
This product is compatible with the Maxpar® Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar® is a trademark of Fluidigm Canada Inc.
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
Properties
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Form
Liquid -
Storage instructions
Shipped at 4°C. Store at +4°C. Do Not Freeze. -
Storage buffer
pH: 7.2
Constituent: PBS -
Carrier free
Yes -
Concentration information loading...
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Purity
Protein A purified -
Clonality
Monoclonal -
Clone number
EPR11037(B) -
Isotype
IgG -
Research areas
Associated products
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Alternative Versions
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Conjugation kits
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Isotype control
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Positive Controls
Applications
The Abpromise guarantee
Our Abpromise guarantee covers the use of ab249194 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application | Abreviews | Notes |
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Flow Cyt (Intra) |
Use at an assay dependent concentration.
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IHC-P |
Use at an assay dependent concentration. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.
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WB |
Use at an assay dependent concentration. Predicted molecular weight: 107 kDa.
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Notes |
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Flow Cyt (Intra)
Use at an assay dependent concentration. |
IHC-P
Use at an assay dependent concentration. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. |
WB
Use at an assay dependent concentration. 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: 16 Human
- Omim: 601065 Human
- SwissProt: P49588 Human
- Unigene: 315137 Human
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Alternative names
- AARS antibody
- AI316495 antibody
- Alanine tRNA ligase 1, cytoplasmic antibody
see all
Images
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All lanes : Anti-AlaRS antibody [EPR11037(B)] (ab155275) at 1/1000 dilution
Lane 1 : Human fetal liver lysate
Lane 2 : HeLa lysate
Lane 3 : K562 lysate
Lane 4 : HepG2 lysate
Lysates/proteins at 10 µg per lane.
Predicted band size: 107 kDaThis data was developed using ab155275, the same antibody clone in a different buffer formulation.
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This data was developed using ab155275, the same antibody clone in a different buffer formulation.Immunohistochemical analysis of paraffin embedded Human endometrial adenocarcinoma tissue labeling AlaRS with ab155275 at a 1/50 dilution. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.
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This data was developed using ab155275, the same antibody clone in a different buffer formulation.Immunohistochemical analysis of paraffin embedded Human kidney tissue labeling AlaRS with ab155275 at a 1/50 dilution. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
Certificate of Compliance
References (0)
ab249194 has not yet been referenced specifically in any publications.