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ANTIBODIES  

(anti-Human and others as indicated)

RDI Division of Fitzgerald Industries Intl  offers a wide line of  antibodies. Since no one antibody works best for all applications (neutralization, blotting, histochemistry, ELISA, etc), we offer many different types of antibodies to help solve this problem. Please inquire for other applications or types of antibodies not listed below.


see below monoclonals to Bacillus anthracis lethal factor and protective antigen of bacillus anthracis (ANTHRAX)

and polyclonal  and  NEW monoclonal to Anthrax spore and new anthrax receptor antibodies

see also recombinant anthrax protective antigen (Pa83 and PA63) and lethal factor

-for more information on anthrax see   http://www.bt.cdc.gov

-for diagnosis protocol in .pdf format   http://www.bt.cdc.gov/agent/anthrax/anthracis20010417.pdf


Monoclonal mouse anti-protective antigen Bacillus anthracis

CAT#: RDI-TRK3BA16-C3 (clone C3)

            RDI-TRK3BA16-101 (clone BAP0101)

            RDI-TRK3BA16-102 (clone BAP0102)

            RDI-TRK3BA16-103 (clone BAP0103)

           RDI-TRK3BA16-104 (clone BAP0104)

           RDI-TRK3BA16-105 (clone BAP0105)

           RDI-TRK3BA16-106 (clone BAP0106)

PRICE: $440.00/mg     $406.00/mg 2-9mg  BULK  on quote

Clone: C3, BAP0101, BAP0102, BAP0103, BAP0104, BAP0105, BAP0106

These clones have been derived from hybridization of SP2/0 myeloma cells with spleen cells of a Balb/c mice immunized with highly purified protective antigen of Bacillus anthracis

Specificity: protective antigen Bacillus antracis Antibodies do not cross react with lethal factor antigen of b.antracis, Y. Pestis, F. Tularensis, Toxoplasma gondii.

Mouse isotype: mIgG1 for clone C3, BAP0105, BAP0106

                        mIgG2B for clones BAP0101, BAP0102, BAP0103, BAP0104

Application: Elisa of protective antigen of B. antracis For Elisa:

     coat: clone C3, detect with BAP0102 or BAP0103

     coat:clone BAP0103, detect with clone BAP0102.

     best pair to date: coat BAP0105, detect with Biotin or HRP labeled BAP0106

-custom order:

HRP labeled clone BAP0106  cat#RDI-TRK3BA16-106HRP  $750.00/1mg   $625.00/mg 2 or more (6 week special order)

Purification: Purified by chromatography on protein A (clone C3) or Protein G (others) Sepharose. Purity is tested by electrophoresis.

Presentation: Each vial contains 1mg of antibodies in ml (mg/ml) PBS pH 7.4 containing 0.1% of sodium azide as preservative. Store at 4 DEG C.

Material safety note:   This product is sold as an antibody preparation for research purpose only. Standard Laboratory Practices should be followed when handling this material. Contains sodium azide (0.1%) as preservative. Although the amount of sodium azide is very small appropriate care must be taken when handling this product.For in Vitro Research Use Only

NOTE: Recommend centrifuging the unopened vial at 500-1000 RPM for 2 minutes to concentrate antibody in bottom of vial. If desired, you can add ml PBS containing 0.1% NaN3 to bringvolume to 1mg in 1ml


Monoclonal mouse anti-Bacillus anthracis lehtal factor

CAT#: RDI-TRK3BA17-105 (clone BAL0105)

            RDI-TRK3BA17-106 (clone BAL0106)

PRICE: $438.00/mg  $406.00/mg 2-9mg  

Clone: BAL0105, BAL0106

These clones have been derived from hybridization of SP2/0 myeloma cells with spleen cells of a Balb/c mice immunized with highly purified lethal factor antigen of Bacillus anthracis

Specificity: lethal factor Bacillus antracis

Mouse isotype: mIgG1 (both)

Application: Elisa of lethal factor of B. antracis For Elisa: best pair coat clone BAL0106, detect with clone BAL0105.

Purification: Purified by chromatography on protein G Sepharose. Purity is tested by electrophoresis.

Presentation: Each vial contains 1mg of antibodies in ml (mg/ml) PBS pH 7.4 containing 0.1% of sodium azide as preservative. Store at 4 DEG C.

Material safetynote: This product is sold as an antibody preparation for research purpose only. Standard Laboratory Practices should be followed when handling this material. Contains sodium azide (0.1%) as preservative. Although the amount of sodium azide is very small appropriate care must be taken when handling this product.

For in Vitro Research Use Only

NOTE: Recommend centrifuging the unopened vial at 500-1000 RPM for 2 minutes to concentrate antibody in bottom of vial. If desired, you can add ml PBS containing 0.1% NaN3 to bringvolume to 1mg in 1ml


IgG fraction of rabbit serum to spore antigen of Bacillus anthracis

Catalog #RDI-TRK3BA18P  $438.00/1mg   $406.00/mg 5+   $375.00/mg 10+   Bulk quotes on request

Immunogen:       Spore extract (MW 90 kD)

Host Animal: Rabbit

Specificity : Spore antigen of Bacillus antracis. Cross-reaction with extracts from spore and vegetative cells of other Bacillus species is less than 5%.

Purification : Protein A sepharose.

Application : Detection of Bacilllus antracis spores

Presentation : Each vial contains antibodies in PBS, pH 7,2, containing 0,005% of merthiolate as preservative. Store at +4°C.

Material safety note: This product is sold as an antibody preparation for research purpose only. Standard Laboratory Practices should be followed when handling this material.

For In Vitro Research Use Only


Monoclonal mouse anti-Bacillus antracis SPORE Antigen   2 clones

Catalogue # RDI-TRK3BA19-SA26 (clone SA26)

                    RDI-TRK3BA19-SA27 (clone SA27)

          $500.00/mg    $469.00/mg 2-9mg    $438.00/mg 10+

Clone: SA26, SA27These clones have been derived from hybridization of Sp2/0 myeloma cells with spleen cells of Balb/c mice, immunised with B. anthracis spore extract

Mouse isotype : IgG2a for both clones

Purification: Purified by chromatography on protein G Sepharose. Purity is tested by SDS-PAGE.

Immunoreactivity: Mab SA26 and SA27 recognize 92-94K protein bands in Western blotting of B. Anthracis spore extract. No cross-reactivity found in ELISA with B. anthracis vegetative cells, B. globigii, B. subtilis and B. cereus spores. Mab SA26 is suitable for coating, Mab SA27 could be used as a conjugate in sandwich ELISA fot anthrax spore determination.

Presentation: Each vial contains antibodies in PBS, pH 7.2, containing 0.1% of sodium azide as preservative. Store at + 4 °C.

Material safety note: This product is sold as an antibody preparation for research purpose only. Standard Laboratory Practices should be followed when handling this material. Contains sodium azide (0.1%) as preservative. Although the amount of sodium azide is very small appropriate care must be taken when handling this product.

For Research Use Only

NOTE: Recommend centrifuging the unopened vial at 500-1000 RPM for 2 minutes to concentrate antibody in bottom of vial. If desired, you can add ml PBS containing 0.1% NaN3 to bring volume to 1mg in 1ml


Anthrax Protective Antigen, Recombinant,   Bacillus anthracis  (see also PA63 below)

cat# RDI-ANTHRXPA-AG   $500.00/100ug     $469.00/vial 5+

Presentation: 100 µg lyophilized solid. Lyophilized from 1 ml of solution containing 50 mM NaCl and 5 mM HEPES, pH 7.5.

MW: 83,000

Purity: Single major band by SDS-PAGE

Solubility: Reconstitute in 1 ml of sterile, distilled H2O .

Storage: Refrigerate (+4 DEG C) Following reconstitution aliquot and freeze (-20 o C). This product is stable for 2 years as supplied. Avoid freeze/thaw cycles of solutions. Stock solutions are stable for up to 6 months at -20 o C.

Description: One of three protein components of anthrax toxin produced by the pathogenic bacterium, Bacillus anthracis. Central moiety that mediates entry of lethal factor (LF) and edema factor (EF) into the target cell. Protective antiogen (also known as PA or PA63) binds to the cell surface via a type I membrane receptor with a von Willebrand factor A domain, known as anthrax toxin receptor. It is proteolytically activated in vivo by a furin-like protease to produce a 63 kDa protein (PA63). PA63 self-associates to form a heptameric, cation- selective, voltage-gated, membrane channel that subsequently binds to LF and/or EF. Cleavage of the 20 kDa fragment from PA83 is necessary for binding of protective antigen to LF and EF.

References:

Mogridge, J., et al. 2002. Biochemistry 41,1079.

Nassi, S., et al. 2002. Biochemistry 41, 1445.

Ahuja, N., et al. 2001. Biochem. Biophys. Res. Commun. 286, 6.

Bradley, K.A., et al. 2001. Nature 414, 225.

Brossier, F., and Mock, M. 2001. Toxicon 39, 1747.

For In Vitro Research Use Only


Anthrax Protective Antigen, PA63 Recombinant, Bacillus anthracis

cat# RDI-ANTHRXP63-AG   $625.00/100ug   $562.00/vial 5+

Presentation: 100 µg lyophilized solid. Lyophilized from 1 ml of solution containing 50 mM NaCl and 5 mM HEPES, pH 7.5.

MW: 63,000

Purity: Single major band by SDS-PAGE

Solubility: Reconstitute with 0.1-1.0ml of sterile, distilled H2O .

Storage: Refrigerate (+4 DEG C) Following reconstitution aliquot and freeze (-20 o C). This product is stable for 2 years as supplied. Avoid freeze/thaw cycles of solutions. Stock solutions are stable for up to 6 months at -20 o C.

Description: PA63 is the carboxyl-terminal 63-kDa fragment obtained by the proteolytic cleavage of the receptor-bound protective antigen (PA), one of the three proteins that comprise anthrax toxin. Unlike native PA, PA63 oligomerizes to form a ring-shaped heptamer which binds up to three copies of EF and/or LF competitively and with high affinity (Kd ~1 nM). Whereas native PA persists on the cell surface, the heptamer is endocytosed, presumably because oligomerization aggregates anthrax toxin receptor. The endocytosed toxic complexes are trafficked to endosomal compartments where the low pH causes the PA63 heptamer to insert into the membrane and form a water-filled channel.

One of three protein components of anthrax toxin produced by the pathogenic bacterium, Bacillus anthracis. Central moiety that mediates entry of lethal factor (LF) and edema factor (EF) into the target cell. Protective antigen (also known as PA or PA63) binds to the cell surface via a type I membrane receptor with a von Willebrand factor A domain, known as anthrax toxin receptor. It is proteolytically activated in vivo by a furin-like protease to produce a 63 kDa protein (PA63). PA63 self-associates to form a heptameric, cation- selective, voltage-gated, membrane channel that subsequently binds to LF and/or EF. Cleavage of the 20 kDa fragment from PA83 is necessary for binding of protective antigen to LF and EF.

References: Mogridge, J., et al. 2002. Proc. Natl. Acad. Sci. USA 99, 7045;

                   Singh, Y., et al. 1999. Infect. Immun. 67, 1853;

                   Leppla, S.H. 1988. Methods Enzymol. 165, 103.

see also PA83 and LF

For In Vitro Research Use Only


Anthrax Lethal Factor, Recombinant,   Bacillus anthracis

cat# RDI-ANTHRXLF-AG   $500.00/100ug   $469.00/vial 5+

Presentation: 100 µg lyophilized solid. Lyophilized from 1 ml of solution containing 50 mM NaCl and 5 mM HEPES, pH 7.5.

MW: 90,000

Purity: Single major band by SDS-PAGE

Solubility: Reconstitute in 1 ml of sterile, distilled H2O Storage: Refrigerate (+4 DEG C)

Storage: Following reconstitution aliquot and freeze (-20 o C). Avoid freeze/thaw cycles of solutions. This product is stable for 2 years as supplied. Stock solutions are stable for up to 6 months at -20 o C.

Description: One of three protein components of anthrax toxin produced by the pathogenic bacterium, Bacillus anthracis. Highly specific protease component that cleaves members of the mitogen-activated protein kinase kinase (MAPKK) family. LF is comprised of four domains: domain I that binds to protective antigen (necessary for entry into the cellular target) and domains II, III, and IV which form a long groove to hold and cleave the target proteins. Requires passage through an acidic vesicle prior to translocation to the cytoplasm of the cell. Cleavage of target proteins leads to the inhibition of multiple signaling pathways and cell death.

References:

Brossier, F., and Mock, M. 2001. Toxicon 39, 1747.

Friedlander, A.M. 2001. Nature 414, 160.

Gupta, P., et al. 2001. Biochem. Biophys. Res. Commun. 284, 568.

Pannifer, A.D., et al. 2001. Nature 414, 229.

Pugsley, A.P. 1996. Proc. Natl. Acad. Sci. USA 93, 8155.

Leppla, S.H. 1991. Methods Enzymol. 195, 153.

For Research Use Only


Anthrax Receptor Antibodies:

After inhalation by mammals, Bacillus anthracis spores germinate in alveolar macrophages then migrate to lymph nodes where they multiply. The vegetative bacteria excrete the tripartite exotoxin, which consists of three polypeptides: protective antigen (PA, 83 kDa), lethal factor (LF, 90 kDa) and oedma factor (OF, 89 kDa). The two components (OF and LF) of the toxin enzymatically modify substrates within the cytosol of the mammalian cells: The OF is an adenylate cyclase that impairs the host defenses through a variety of mechanisms inhibiting phagocytosis. The LF is a zinc dependent protease that cleaves several mitogen activated protein kinase kinases (MAPKK) and causes lysis of macrophages. To intoxicate mammalian cells, the third component of the toxin PA, binds to a ubiquitously expressed cellular receptor, Tumor Endothelium Marker-8 (TEM8). Upon binding to TEM8, PA is cleaved into 20 and 63kDa fragments (PA20 and PA63) by furin or furin-like proteases. PA20 dissociates into medium and allows the PA63 fragment to heptamerize and bind LF and OF of the toxin. The resulting complex of PA63 fragment with EF and/or OF binds to PA-receptor TEM8/ATR and internalized into endosomes followed by translocation of LF and OF into cytosol of the cells. PA receptor TEM8 (also known as Anthrax Toxin receptor, ATR1) (human 564aa, mouse 562aa) is a glycoprotein with a extracellular (1-321aa), cytosolic (343-564aa) and TM (322-342) domains. The cytosolic domain is not required for translocation of LF into cytosol. The ATR/TEM8 gene is mapped at chromosome 4. Three splice variants (ATR1, ATR2 and ATR3) of TEM8/ATR have been reported. ATR1 (564aa) is the largest isoform whereas ATR2 (368aa) and ATR3 (333aa) are proteins truncated after the TM domain. The seqs (1-364aa) of ATR2 and ATR1 are identical whereas ATR3 has a unique 15aa seq at its C-terminal. ATR/TEM8 protein is expressed in a variety of cell lines and in heart, lung, lymphocytes and in central nervous system. The Von Willebrand Factor Type A domain (VWA) (44-216aa) present in ATR -1, -2 and -3 by itself is able to interact inactivate anthrax toxin. ATR antibodies might help in developing new approaches for PA-receptor study and treatment of anthrax.


RDI Division of Fitzgerald Industries Intl

34 Junction Square Drive

Concord MA 01742-3049

USA

phone (978) 371-6446 or (800) 370-2222

fax     (978) 371-2266

EMAIL:antibodies@fitzgerald-fii.com

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