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$1,160.00
$1,160.00
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.54
Conjugate:
agarose conjugate
Clone:
3F10, monoclonal
Application:
—
Citations:
75
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biological source
rat
conjugate
agarose conjugate
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
3F10, monoclonal
form
slurry
packaging
pkg of 1 mL (settled resin volume)
manufacturer/tradename
Roche
isotype
IgG1
epitope sequence
YPYDVPDYA
capacity
2-8 nmol/mL binding capacity
storage temp.
2-8°C
Related Categories
1 of 4
This Item | |||
|---|---|---|---|
| biological source rat | biological source rabbit | biological source mouse | biological source mouse |
| clone 3F10, monoclonal | clone polyclonal | clone HA-7, monoclonal | clone HA-7, monoclonal |
| conjugate agarose conjugate | conjugate unconjugated | conjugate TRITC conjugate | conjugate unconjugated |
| antibody form purified immunoglobulin | antibody form affinity isolated antibody | antibody form purified from hybridoma cell culture | antibody form purified immunoglobulin |
| form slurry | form buffered aqueous solution | form buffered aqueous solution | form - |
| storage temp. 2-8°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
General description
Anti-HA High Affinity antibody (clone 3F10) recognizes the 9-amino acid sequence YPYDVPDYA, derived from the human influenza hemagglutinin (HA) protein. This epitope is also recognized in fusion proteins that are derived from mammalian, bacterial, and yeast expression vectors, regardless of its position (N-terminal, C-terminal or internal)
Immunogen
Amino acids 98-106 from the human influenza virus hemagglutinin protein
Application
Following immunoprecipitation or purification, the tagged protein of interest may be analyzed by:
- Western blotting using the Anti-HA antibody
- Silver staining (or similar protein stain)
- In coimmunoprecipitation.[1]
Biochem/physiol Actions
Anti-HA High Affinity antibody (clone 3F10) recognizes the 9-amino acid sequence YPYDVPDYA, derived from the human influenza hemagglutinin (HA) protein. This epitope is also recognized in fusion proteins that are derived from mammalian, bacterial, and yeast expression vectors, regardless of its position (N-terminal, C-terminal or internal).
Features and Benefits
- Achieve enhanced specificity and reduced cross-reactivity of Anti-HA High Affinity.
- Use nondenaturing conditions for elution of your HA-tagged protein of choice.
- Purify even rarely expressed HA-tagged proteins.
- Highly specific to YPYDVPDYA.
- Suitable for purification of proteins containing HA-epitop as N-terminal, C-terminal or internal fusion.
- Applicable with crued cell extracts from mammalian, bacterial and yeast expression systems.
Physical form
1 ml settled resin of Anti-HA Affinity Matrix in PBS containing 0.09% sodium azide (w/v); 2 ml suspension equals to 1 ml bed volume. One plastic column with top and bottom caps is included.
Analysis Note
Each lot of Anti-HA Affinity Matrix is tested for its ability to purify a HA-tagged protein expressed in stably transfected cells from a crude mammalian extract. The immunoprecipitate is analyzed by western blot using Anti-HA, High Affinity antibody.
Yield of 9 nmol purified protein/ml affinity matrix was determined using a whole-cell bacterial extract containing expressed HA-tagged bacterial alkaline phosphatase.
Other Notes
For life science research only. Not for use in diagnostic procedures.
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Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
does not flash
flash_point_c
does not flash
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Geetha Hewawasam et al.
Molecular cell, 40(3), 444-454 (2010-11-13)
Cse4 is a variant of histone H3 that is incorporated into a single nucleosome at each centromere in budding yeast. We have discovered an E3 ubiquitin ligase, called Psh1, which controls the cellular level of Cse4 via ubiquitylation and proteolysis.
Abdirahman Abdi et al.
Cellular and molecular life sciences : CMLS, 67(19), 3355-3369 (2010-06-29)
Over the last decade, several protein kinases inhibitors have reached the market for cancer chemotherapy. The kinomes of pathogens represent potentially attractive targets in infectious diseases. The functions of the majority of protein kinases of Plasmodium falciparum, the parasitic protist
Stephen C Kales et al.
PloS one, 9(1), e87116-e87116 (2014-01-28)
The Cbl proteins (Cbl, Cbl-b, and Cbl-c) are a highly conserved family of RING finger ubiquitin ligases (E3s) that function as negative regulators of tyrosine kinases in a wide variety of signal transduction pathways. In this study, we identify a
Jinyan Cheng et al.
Journal of virology, 94(7) (2020-01-17)
Stress granules (SGs) are formed in the cytoplasm under environmental stress, including viral infection. Human enterovirus D68 (EV-D68) is a highly pathogenic virus which can cause serious respiratory and neurological diseases. At present, there is no effective drug or vaccine
Wim Schepers et al.
The Journal of biological chemistry, 287(53), 44130-44142 (2012-11-17)
The readdition of an essential nutrient to starved, fermenting cells of the yeast Saccharomyces cerevisiae triggers rapid activation of the protein kinase A (PKA) pathway. Trehalase is activated 5-10-fold within minutes and has been used as a convenient reporter for
Protocols
Anti-HA Affinity Matrix Protocol & Troubleshooting
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