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A3937

Sigma-Aldrich

Anti-Rabbit IgG (whole molecule), F(ab′)2 fragment−Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous glycerol solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

Quality Level

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

rabbit

technique(s)

direct ELISA: 1:30,000
dot blot: 1:30,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50
western blot: 1:30,000

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

IgGs are glycoprotein antibodies that modulate several immune responses. Rabbit IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rabbit IgGs conjugated to a detectable substrate are useful tools for the analysis of target proteins. Anti-Rabbit IgG (whole molecule), (F(ab′)2) fragment-Alkaline Phosphatase antibody binds all rabbit immunoglobulins.

Immunogen

Purified rabbit IgG

Application

Anti-Rabbit IgG (whole molecule), (F(ab′)2) fragment-Alkaline Phosphatase antibody is suitable for use in immunoblotting (5μl) and direct ELISA (1:30,000). The product may also be used for immunohistochemistry (1:50 using formalin-fixed, paraffin-embedded sections).
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)
Western Blotting (1 paper)
Western blot analysis of prostate epithelial cell lysates was performed using alkaline phosphatase conjugated goat anti-rabbit F2 Fragment specific antibody as the secondary at a dilution of 1:7500 for 2 hours at room temperature.

Physical form

Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl2, 10 mM glycine, 1% bovine serum albumin, 50% glycerol and 15 mM 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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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Stromal and Epithelial Expression of Tumor Markers Hyaluronic Acid and HYAL1 Hyaluronidase in Prostate Cancer
Lokeshwar, V.
Journal of Biochemistry, 276, 11922-11932 (2001)
J T San Agustin et al.
The Journal of biological chemistry, 273(38), 24874-24883 (1998-09-12)
The basis for the unusual properties of the catalytic subunit (C) of ram sperm cAMP-dependent protein kinase was investigated. Ram sperm C was purified and found by mass spectrometry (MS) to be approximately 890 Da smaller than Calpha, the predominant
Keiko Igaki et al.
International immunopharmacology, 60, 160-169 (2018-05-08)
C-C chemokine receptor 9 (CCR9) is the homing receptor for C-C motif chemokine ligand 25 (CCL25), and contributes to the maintenance of mucosal immunity and pathogenesis of inflammatory bowel disease (IBD) through the recruitment of T cells into the gut
Naoya Takanashi et al.
BMC microbiology, 13, 54-54 (2013-03-19)
Previously, a bovine intestinal epithelial cell line (BIE cells) was successfully established. This work hypothesized that BIE cells are useful in vitro model system for the study of interactions of microbial- or pathogen-associated molecular patterns (MAMPs or PAMPs) with bovine
Ratthaphol Charlermroj et al.
PloS one, 8(4), e62344-e62344 (2013-05-03)
Plant pathogens are a serious problem for seed export, plant disease control and plant quarantine. Rapid and accurate screening tests are urgently required to protect and prevent plant diseases spreading worldwide. A novel multiplex detection method was developed based on

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