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SAB5600193

Sigma-Aldrich

Anti-HA-Tag-Biotin antibody, Rabbit monoclonal

recombinant, expressed in HEK 293 cells, clone RM305, purified immunoglobulin

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

recombinant

expressed in HEK 293 cells

conjugate

biotin conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

RM305, monoclonal
recombinant monoclonal

form

buffered aqueous glycerol solution

concentration

1 mg/mL

technique(s)

flow cytometry: 0.1-1.0 μg/mL
immunofluorescence: 0.1-1.0 μg/mL
immunohistochemistry: 0.01-0.5 μg/mL
western blot: 0.1-1.0 μg/mL

isotype

IgG

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Specificity

This antibody reacts to recombinant proteins containing a HA-Tag fused to either the amino or carboxy terminus. No cross reactivity with other endogenous protein.

Immunogen

A peptide corresponding to HA-tag (Human influenza hemagglutinin amino acids 98-106)

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 50% glycerol, 1% BSA and 0.09% sodium azide.

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

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Igor Patrick Vasconcelos Vieira et al.
AMB Express, 13(1), 131-131 (2023-11-22)
The methylotrophic yeast Komagataella phaffii is one of the most important microbial platforms to produce recombinant proteins. Despite its importance in the context of industrial biotechnology, the use of synthetic biology approaches in K. phaffii is hampered by the fact

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