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ROAHAHA

Roche

Anti-HA High Affinity

from rat IgG1

Synonym(s):

antibody

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About This Item

UNSPSC Code:
12352203

biological source

rat

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

3F10, monoclonal

form

lyophilized

packaging

pkg of 50 μg (11867423001)
pkg of 500 μg (11867431001)

manufacturer/tradename

Roche

isotype

IgG1

epitope sequence

YPYDVPDYA

storage temp.

2-8°C

Related Categories

General description

Anti-HA High Affinity is a monoclonal antibody to the HA-peptide (clone 3F10). Anti-HA High Affinity recognizes the HA peptide sequence (YPYDVPDYA), derived from the influenza hemagglutinin protein. The antibody recognizes its antigenic determinant even when the HA peptide epitope is introduced into unrelated recombinant proteins by a technique known as "epitope tagging".

Specificity

Anti-HA, High Affinity recognizes the 9-amino acid sequence YPYDVPDYA, derived from the human influenza hemagglutinin (HA) protein. This epitope is also recognized in fusion proteins regardless of its position (N-terminal, C-terminal or internal).

Immunogen

Amino acids 98-106 from the human influenza virus hemagglutinin protein

Application

Use Anti-HA High Affinity for the detection of native influenza hemagglutinin protein and recombinant proteins that contain the HA epitope using:
  • Dot blots
  • ELISA
  • Immunocytochemistry
  • Immunoprecipitation
  • Western blots
Since Anti-HA High Affinity is a rat monoclonal, it is possible to use it in conjunction with murine monoclonals for double labeling.

Quality

Function tested in western blot.

Preparation Note

Working concentration: Working concentration of conjugate depends on application and substrate.

The following concentrations should be taken as a guideline:
  • ELISA: for detection 100 ng/ml; for coating 1 to 5 μg/ml
  • Immunoprecipitation: 0.5 to 5 μg/ml
  • Western blot: 50 to 200 ng/ml

Reconstitution

Add 0.5 ml (11 867 423 001; 50 μg) or 2.5 ml (11 867 431 001; 500 μg) double-distilled water to a final concentration of 100 μg/ml or 200 μg/ml respectively.
Rehydrate for 10 min prior to use.

Other Notes

For life science research only. Not for use in diagnostic procedures.

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Hazard Classifications

Aquatic Chronic 3 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

does not flash

flash_point_c

does not flash


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Toshiki Kinuhata et al.
Journal of developmental biology, 10(4) (2022-11-23)
The first event of differentiation and morphogenesis in the optic vesicle (OV) is specification of the neural retina (NR) and retinal pigment epithelium (RPE), separating the inner and outer layers of the optic cup, respectively. Here, we focus on a
Elisabeth Stes et al.
Journal of proteome research, 13(6), 3107-3113 (2014-05-13)
Here, we apply the COmbined FRActional DIagonal Chromatography (COFRADIC) technology to enrich for ubiquitinated peptides and to identify sites of ubiquitination by mass spectrometry. Our technology bypasses the need to overexpress tagged variants of ubiquitin and the use of sequence-biased
Kristina Halbleib et al.
Molecular cell, 67(4), 673-684 (2017-07-12)
The unfolded protein response (UPR) is a conserved homeostatic program that is activated by misfolded proteins in the lumen of the endoplasmic reticulum (ER). Recently, it became evident that aberrant lipid compositions of the ER membrane, referred to as lipid bilayer stress
Alexandra Atienza-Manuel et al.
Development (Cambridge, England) (2021-11-06)
The vertebrate endocytic receptor CUBAM, consisting of three cubilin monomers complexed with a single amnionless molecule, plays a major role in protein reabsorption in the renal proximal tubule. Here, we show that Drosophila CUBAM is a tripartite complex composed of
Gizem Sancer et al.
Current biology : CB, 29(17), 2812-2825 (2019-08-14)
In the fly optic lobe, ∼800 highly stereotypical columnar microcircuits are arranged retinotopically to process visual information. Differences in cellular composition and synaptic connectivity within functionally specialized columns remain largely unknown. Here, we describe the cellular and synaptic architecture in

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