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SAB4300603

Sigma-Aldrich

Anti-HA-Tag antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-Hemagglutinin-Tag antibody produced in rabbit

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

concentration

1 mg/mL

technique(s)

western blot: 1:500-1:1000

isotype

IgG

immunogen sequence

(Y-P-Y-D-V-P-D-Y-A)

application(s)

research pathology

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

The HA tag (Y-P-Y-D-V-P-D-Y-A) is derived from an epitope (amino acids 98-106) of the influenza hemagglutinin (HA) protein. HA tag is used as a general epitope tag in expression vectors for many recombinant proteins. The presence of HA tag facilitates the detection, isolation and purification of recombinant fusion proteins.
This antibody is specific for the HA tag containing fusion proteins and does not detect other proteins.

Immunogen

Peptide sequence (Y-P-Y-D-V-P-D-Y-A)HA-Tag.

Application

Anti-HA-Tag antibody produced in rabbit has been used in western blotting.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Chromatin immunoprecipitation (1 paper)
Rabbit polyclonal anti-HA-Tag antibody may be used as an epitope specific reagent for the detection and/or purification of multiple engineered proteins. The specific advantage is that the use of HA-tag sequence in engineered proteins eliminates the requirement to have a protein specific antibody for detection and purification of specific proteins.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Wei Zhao et al.
Journal of immunology (Baltimore, Md. : 1950), 205(8), 2255-2264 (2020-09-16)
The cytosolic pattern recognition receptor NLRP3 senses host-derived danger signals and certain microbe-derived products in both humans and rodents. NLRP3 activation assembles an inflammasome complex that contains the adapter proteins ASC and caspase-1, whose activation triggers the maturation and release
Yu Liu et al.
Nature genetics, 49(8), 1211-1218 (2017-07-04)
Genetic alterations that activate NOTCH1 signaling and T cell transcription factors, coupled with inactivation of the INK4/ARF tumor suppressors, are hallmarks of T-lineage acute lymphoblastic leukemia (T-ALL), but detailed genome-wide sequencing of large T-ALL cohorts has not been carried out.
G Lu et al.
Gene therapy, 23(4), 323-329 (2016-01-12)
Glucokinase (GCK) is an important enzyme critical for glucose metabolism, and has been targeted as such in the pursuit of a cure for diabetes mellitus. We show that streptozotocin (STZ)-induced diabetic murine model exhibits low GCK expression with high blood
Elena Loreti et al.
Plant physiology, 176(2), 1286-1298 (2017-11-01)
Plants respond to hypoxia, often caused by submergence, by expressing a specific set of genes that contribute to acclimation to this unfavorable environmental condition. Genes induced by low oxygen include those encoding enzymes for carbohydrate metabolism and fermentation, pathways that
GATA3 transcription factor abrogates Smad4-mediated fascin overexpression, invadopodium formation and breast cancer cell invasion.
Sun J, et al.
Test, jbc-M113 (2013)

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