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company name :
MyBioSource
product type :
protein
product name :
Recombinant Human Bone marrow proteoglycan
catalog :
MBS953649
quantity :
0.05 mg (Yeast)
price :
185 USD
more info or order :
product information
catalog number :
MBS953649
products type :
Recombinant Protein
products full name :
Recombinant Human Bone marrow proteoglycan
products short name :
Bone marrow proteoglycan
products name syn :
Proteoglycan 2
other names :
bone marrow proteoglycan isoform 2 preproprotein; Bone marrow proteoglycan; bone marrow proteoglycan; proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein); Proteoglycan 2
products gene name :
PRG2
other gene names :
PRG2; PRG2; MBP; BMPG; MBP1; MBP; BMPG; EMBP; MBP
uniprot entry name :
PRG2_HUMAN
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
106-222
sequence length :
211
sequence :
TCRYLLVRSLQTFSQAWFTCRRCYRGNLVSIHNFNINYR
IQCSVSALNQGQVWIGGRITGSGRCRRFQWVDGSRWNFA
YWAAHQPWSRGGHCVALCTRGGHWRRAHCLRRLPFICSY
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Signal Transduction
products description :
Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA.
products references :
Acidic precursor revealed in human eosinophil granule major basic protein cDNA.Barker R.L., Gleich G.J., Pease L.R.J. Exp. Med. 168:1493-1498(1988) Barker R.L.Cloning and sequence analysis of the human gene encoding eosinophil major basic protein.Barker R.L., Loegering D.A., Arakawa K.C., Pease L.R., Gleich G.J.Gene 86:285-289(1990) Isolation of a complementary DNA clone encoding a precursor to human eosinophil major basic protein.McGrogan M., Simonsen C., Scott R., Giffith J., Ellis N., Kennedy J., Campanelli D., Nathan C., Gabay J.J. Exp. Med. 168:2295-2308(1988) Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma sequence homology with animal lectins.Yoshimatsu K., Ohya Y., Shikata Y., Seto T., Hasegawa Y., Tanaka I., Kawamura T., Kitoh K., Toyoshima S., Osawa T.Mol. Immunol. 29:537-546(1992) Human eosinophil major basic protein, a mediator of allergic inflammation, is expressed by alternative splicing from two promoters.Li M.S., Sun L., Satoh T., Fisher L.M., Spry C.J.Biochem. J. 305:921-927(1995) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Pro-major basic protein has three types of sugar chains at the pro-portion.Shikata Y., Hayashi Y., Yoshimatsu K., Ohya Y., Seto T., Fukushima K., Yoshida Y.Biochim. Biophys. Acta 1163:243-249(1993) Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein.Oxvig C., Sand O., Kristensen T., Gleich G.J., Sottrup-Jensen L.J. Biol. Chem. 268:12243-12246(1993) Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma.Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.J. Biol. Chem. 270:13645-13651(1995) Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein.Wasmoen T.L., Bell M.P., Loegering D.A., Gleich G.J., Prendergast F.G., McKean D.J.J. Biol. Chem. 263:12559-12563(1988) Antibiotic proteins of human polymorphonuclear leukocytes.Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F.Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989) Eosinophil granule cationic proteins major basic protein is distinct from the smaller subunit of eosinophil peroxidase.Weller P.F., Ackerman S.J., Smith J.A.J. Leukoc. Biol. 43:1-4(1988) Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA.Kristensen T., Oxvig C., Sand O., Moller N.P.H., Sottrup-Jensen L.Biochemistry 33:1592-1598(1994) Evidence of eosinophil granule major basic protein in human placenta.Wasmoen T.L., McKean D.J., Benirschke K., Coulam C.B., Gleich G.J.J. Exp. Med. 170:2051-2063(1989) Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.Oxvig C., Haaning J., Hojrup P., Sottrup-Jensen L.Biochem. Mol. Biol. Int. 33:329-336(1994) Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein.Oxvig C., Gleich G.J., Sottrup-Jensen L.FEBS Lett. 341:213-217(1994) Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta.Bonno M., Oxvig C., Kephart G.M., Wagner J.M., Kristensen T., Sottrup-Jensen L., Gleich G.J.Lab. Invest. 71:560-566(1994) Messenger ribonucleic acid levels of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein expression in human reproductive and nonreproductive tissues.Overgaard M.T., Oxvig C., Christiansen M., Lawrence J.B., Conover C.A., Gleich G.J., Sottrup-Jensen L., Haaning J.Biol. Reprod. 61:1083-1089(1999) Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor.Overgaard M.T., Haaning J., Boldt H.B., Olsen I.M., Laursen L.S., Christiansen M., Gleich G.J., Sottrup-Jensen L., Conover C.A., Oxvig C.J. Biol. Chem. 275:31128-31133(2000) Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment sites.Overgaard M.T., Sorensen E.S., Stachowiak D., Boldt H.B., Kristensen L., Sottrup-Jensen L., Oxvig C.J. Biol. Chem. 278:2106-2117(2003) Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase.Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M., Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M., Doering G.J. Biol. Chem. 283:28629-28640(2008) Crystal structure of the eosinophil major basic protein at 1.8-A. An atypical lectin with a paradigm shift in specificity.Swaminathan G.J., Weaver A.J., Loegering D.A., Checkel J.L., Leonidas D.D., Gleich G.J., Acharya K.R.J. Biol. Chem. 276:26197-26203(2001) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006)
ncbi gi num :
342837699
ncbi acc num :
NP_001230174.1
ncbi gb acc num :
NM_001243245.2
uniprot acc num :
P13727
ncbi mol weight :
15.77kD
ncbi pathways :
Asthma Pathway (83120); Asthma Pathway (532)
ncbi summary :
The protein encoded by this gene is the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in placenta and pregnancy serum, where it exists as a complex with several other proteins including pregnancy-associated plasma protein A (PAPPA), angiotensinogen (AGT), and C3dg. This protein may be involved in antiparasitic defense mechanisms as a cytotoxin and helminthotoxin, and in immune hypersensitivity reactions. The encoded protein contains a peptide that displays potent antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. It is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2014]
size1 :
0.05 mg (Yeast)
price1 :
185 USD
size2 :
0.2 mg (Yeast)
price2 :
420
size3 :
0.5 mg (Yeast)
price3 :
680
size4 :
1 mg (Yeast)
price4 :
1070
more info or order :
company information
MyBioSource
P.O. Box 153308
San Diego, CA 92195-3308
sales@mybiosource.com
https://www.mybiosource.com
1-888-627-0165
headquarters: USA
MyBioSource, LLC was orginally founded in Vancouver by three enthusiastic scientists who are passionate about providing the world with the best reagents available. Together, they form a company with a big vision known as MyBioSource. MyBioSource is now located in San Diego, California, USA.

"MyBioSource's number 1 vision is to be the world's number 1 quality reagents provider."

Our goal is to provide researchers, scientists and customers alike with a one-stop-shop for all of their reagents needs, whether it is monoclonal antibody, polyclonal antibody, recombinant protein, peptide, etc...

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