CoraLite® Plus 488-conjugated AlaRS Monoclonal antibody

AlaRS Monoclonal Antibody for IF

Host / Isotype

Mouse / IgG1

Reactivity

Human, Mouse, Rat

Applications

IF

Conjugate

CoraLite® Plus 488 Fluorescent Dye

CloneNo.

1C8H3

Cat no : CL488-67909

Synonyms

AARS, Alanine tRNA ligase, alanyl tRNA synthetase, AlaRS

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Validation Data Gallery

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  IF Staining of A431 using CL488-67909

  Immunofluorescent analysis of (-20°C Methanol) fixed A431 cells using CoraLite® Plus 488 AlaRS antibody (CL488-67909, Clone: 1C8H3 ) at dilution of 1:200.

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Tested Applications

• Positive IF detected in: A431 cells

Recommended dilution

• Immunofluorescence (IF): IF : 1:50-1:500

It is recommended that this reagent should be titrated in each testing system to obtain optimal results.

Sample-dependent, Check data in validation data gallery.

Product Information

CL488-67909 targets AlaRS in IF applications and shows reactivity with Human, Mouse, Rat samples.

• Tested Reactivity: Human, Mouse, Rat
• Host / Isotype: Mouse / IgG1
• Class: Monoclonal
• Type: Antibody
• Immunogen: AlaRS fusion protein Ag11151
• Full Name: alanyl-tRNA synthetase
• Calculated Molecular Weight: 968 aa, 107 kDa
• Observed Molecular Weight: 107 kDa
• GenBank Accession Number: BC011451
• Gene Symbol: AARS
• Gene ID (NCBI): 16
• RRID: AB_2919560
• Conjugate: CoraLite® Plus 488 Fluorescent Dye
• Excitation/Emission Maxima Wavelengths: 493 nm / 522 nm
• Form: Liquid
• Purification Method: Protein G purification
• Storage Buffer: PBS with 50% Glycerol, 0.05% Proclin300, 0.5% BSA, pH 7.3.
• Storage Conditions: Store at -20°C. Avoid exposure to light. Aliquoting is unnecessary for -20^oC storage. 20ul sizes contain 0.1% BSA.

Background Information

AARS(alanyl-tRNA synthetase) is also named as AlaRS(alanine tRNA ligase 1, cytoplasmic), renal carcinoma antigen NY-REN-42 and belongs to the class-II aminoacyl-tRNA synthetase family. It can interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. AARS 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(PMID:19661429).