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Glycophorin-A (GYPA) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS960329

Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for… More details

$335 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Certificate of Analysis (COA) View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Glycophorin-A (GYPA), Recombinant Protein
Full Product Name
Recombinant Human Glycophorin-A
Product Gene Name
Product Synonym Gene Name
GPA
Product Synonym Names
MN sialoglycoprotein; PAS-2Sialoglycoprotein alpha; CD235a
Sequence
LSTTEVAMHT STSSSVTKSY ISSQTNDTHK RDTYAATPRA HEVSEISVRT VYPPEEETGE RVQLAHHFSE PE
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
34.9 kDa
Sequence Positions
20-91aa; Extracellular Domain
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
111300
3D Structure
ModBase 3D Structure for P02724
Production Note
Special Offer: The E Coli, Yeast host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Coli, Yeasthost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli, Yeast host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli, Yeast host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to support@mybiosource.com for more details.

Product Categories/Family for GYPA recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for GYPA recombinant protein

Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach nucleotide sequence and mRNA structure.Siebert P.D., Fukuda M.Proc. Natl. Acad. Sci. U.S.A. 83:1665-1669(1986) Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta.Tate C.G., Tanner M.J.A.Biochem. J. 254:743-750(1988) Structural organization of glycophorin A and B genes glycophorin B gene evolved by homologous recombination at Alu repeat sequences.Kudo S., Fukuda M.Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989) The mechanism of production of multiple mRNAs for human glycophorin A.Jawad K., Burness T.H.Nucleic Acids Res. 18:5829-5836(1990) Characterization of glycophorin A transcripts control by the common erythroid-specific promoter and alternative usage of different polyadenylation signals.Kudo S., Onda M., Fukuda M.J. Biochem. 116:183-192(1994) Extensive alternative splicing of glycophorins in Southeast Asian populations.Hsu K., Huang S.-Y., Chi N., Lin M. 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) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Molecular biological study of the structure and expression of human glycophorin A.Siebert P.D., Fukuda M.Rev. Fr. Transfus. Immunohematol. 29:251-266(1986) Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.Tomita M., Marchesi V.T.Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975) Furthmayr H., Galardy R., Tomita M., Marchesi V.T.Submitted (JUN-1977) to the PIR data bankCharacterization of cDNA clones for human glycophorin A. Use for gene localization and for analysis of normal of glycophorin-A-deficient (Finnish type) genomic DNA.Rahuel C., London J., D'Auriol L., Mattei M.-G., Tournamille C., Skrzynia C., Lebouc Y., Galibert F., Cartron J.-P.Eur. J. Biochem. 172:147-153(1988) Mg and Mc mutations within the amino-terminal region of glycophorin A.Furthmayr H., Metaxas M.N., Metaxas-Buhler M.Proc. Natl. Acad. Sci. U.S.A. 78:631-635(1981) Amino acid and carbohydrate structural variants of glycoprotein products (M-N glycoproteins) of the M-N allelic locus.Blumenfeld O.O., Adamany A.M., Puglia K.V.Proc. Natl. Acad. Sci. U.S.A. 78:747-751(1981) Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides.Thomas D.B., Winzler R.J.J. Biol. Chem. 244:5943-5946(1969) Erythrocytes deficiency in glycophorin resist invasion by the malarial parasite Plasmodium falciparum.Pasvol G., Wainscoat J.S., Weatherall D.J.Nature 297:64-66(1982) Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.Fukuda M., Lauffenburger M., Sasaki H., Rogers M.E., Dell A.J. Biol. Chem. 262:11952-11957(1987) The glycophorin A transmembrane domain dimer sequence-specific propensity for a right-handed supercoil of helices.Treutlein H.R., Lemmon M.A., Engelman D.M., Brunger A.T.Biochemistry 31:12726-12732(1992) Glycosylation sites identified by solid-phase Edman degradation O-linked glycosylation motifs on human glycophorin A.Pisano A., Redmond J.W., Williams K.L., Gooley A.A.Glycobiology 3:429-435(1993) Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum.Sim B.K., Chitnis C.E., Wasniowska K., Hadley T.J., Miller L.H.Science 264:1941-1944(1994) Identification of blood group A and B antigens in human glycophorin.Podbielska M., Krotkiewski H.Arch. Immunol. Ther. Exp. 48:211-221(2000) Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface.Young M.T., Beckmann R., Toye A.M., Tanner M.J.Biochem. J. 350:53-60(2000) Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis in vivo studies in human glycophorin A transgenic mice.Auffray I., Marfatia S., de Jong K., Lee G., Huang C.H., Paszty C., Tanner M.J., Mohandas N., Chasis J.A.Blood 97:2872-2878(2001) In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane.Gerber D., Shai Y.J. Biol. Chem. 276:31229-31232(2001) Distinct regions of human glycophorin A enhance human red cell anion exchanger (band 3; AE1) transport function and surface trafficking.Young M.T., Tanner M.J.J. Biol. Chem. 278:32954-32961(2003) The blood group system.Reid M.E., Christine Lomas-Francis C.(In) Reid M.E., Christine Lomas-Francis C. (eds.) ;The blood group antigen factsbook, pp.29-104, Academic Press, Oxford (2004) ABH blood group antigens in O-glycans of human glycophorin A.Podbielska M., Fredriksson S.A., Nilsson B., Lisowska E., Krotkiewski H.Arch. Biochem. Biophys. 429:145-153(2004) Altered structure and anion transport properties of band 3 (AE1, SLC4A1) in human red cells lacking glycophorin A.Bruce L.J., Pan R.J., Cope D.L., Uchikawa M., Gunn R.B., Cherry R.J., Tanner M.J.J. Biol. Chem. 279:2414-2420(2004) Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane.Sanchez G., Aragones L., Costafreda M.I., Ribes E., Bosch A., Pinto R.M.J. Virol. 78:9807-9813(2004) Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane.Yajima A., Urano-Tashiro Y., Shimazu K., Takashima E., Takahashi Y., Konishi K.Microbiol. Immunol. 52:69-77(2008) Interaction of anion exchanger 1 and glycophorin A in human erythroleukaemic K562 cells.Pang A.J., Reithmeier R.A.Biochem. J. 421:345-356(2009) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.Dill K., Hu S.H., Berman E., Pavia A.A., Lacombe J.M.J. Protein Chem. 9:129-136(1990) A transmembrane helix dimer structure and implications.Mackenzie K.R., Prestegard J.H., Engelman D.M.Science 276:131-133(1997) Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching.Adams P.D., Engelman D.M., Bruenger A.T.3.3.CO;2-O>Proteins 26:257-261(1996) Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype.Huang C.-H., Spruell P., Moulds J.J., Blumenfeld O.O.Blood 80:257-263(1992) Molecular analysis of human glycophorin MiIX gene shows a silent segment transfer and untemplated mutation resulting from gene conversion via sequence repeats.Huang C.H., Skov F., Daniels G., Tippett P., Blumenfeld O.O.Blood 80:2379-2387(1992) Alteration of splice site selection by an exon mutation in the human glycophorin A gene.Huang C.H., Reid M., Daniels G., Blumenfeld O.O.J. Biol. Chem. 268:25902-25908(1993) Glycophorin A mutation Ala65 --> Pro gives rise to a novel pair of MNS alleles ENEP (MNS39) and HAG (MNS41) and altered Wrb expression direct evidence for GPA/band 3 interaction necessary for normal Wrb expression.Poole J., Banks J., Bruce L.J., Ring S.M., Levene C., Stern H., Overbeeke M.A., Tanner M.J.Transfus. Med. 9:167-174(1999) The low-frequency MNS blood group antigens Ny(a) (MNS18) and Os(a) (MNS38) are associated with GPA amino acid substitutions.Daniels G.L., Bruce L.J., Mawby W.J., Green C.A., Petty A., Okubo Y., Kornstad L., Tanner M.J.Transfusion 40:555-559(2000) The MNS blood group antigens, Vr (MNS12) and Mt(a) (MNS14) , each arise from an amino acid substitution on glycophorin A.Storry J.R., Coghlan G., Poole J., Figueroa D., Reid M.E.Vox Sang. 78:52-56(2000) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of GYPA recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for GYPA purchase

MBS960329 is a recombinant protein targeting GYPA. Also known as Recombinant Human Glycophorin-A. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for GYPA. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
glycophorin-A isoform 3
NCBI Official Synonym Full Names
glycophorin A (MNS blood group)
NCBI Official Symbol
GYPA
NCBI Official Synonym Symbols
MN; GPA; MNS; GPSAT; PAS-2; CD235a; GPErik; HGpMiV; HGpMiXI; HGpSta(C)
UniProt Protein Name
Glycophorin-A
UniProt Synonym Protein Names
MN sialoglycoprotein; PAS-2; Sialoglycoprotein alpha; CD_antigen: CD235a
Protein Family
UniProt Gene Name
GYPA
UniProt Synonym Gene Names
GPA
UniProt Entry Name
GLPA_HUMAN
NCBI Protein Information
glycophorin-A

NCBI Summary for GYPA

Glycophorins A (GYPA) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. In addition to the M or N and S or s antigens that commonly occur in all populations, about 40 related variant phenotypes have been identified. These variants include all the variants of the Miltenberger complex and several isoforms of Sta, as well as Dantu, Sat, He, Mg, and deletion variants Ena, S-s-U- and Mk. Most of the variants are the result of gene recombinations between GYPA and GYPB. [provided by RefSeq, Jul 2008]
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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