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898 results found for “Density Lipoprotein”
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Name :
Borrelia DbpBDescription:
Borrelia Burgdorferi Decorin Binding Protein B Recombinant
Product # :
BOR-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Borrelia Burgdorferi Decorin Binding Protein B produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19,353 Dalton. Borrelia DbpB is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia DbpB (1.11mg/1ml) is supplied in 16mM HEPES buffer pH-8.0, 300mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Applications
Western blot with Lyme positive plasma.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
Quantity :
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Shipped with Ice Packs
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AFP ProteinDescription:
Alpha Fetoprotein Human Recombinant
Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.
Product # :
PRO-2229Price :
Quantity :
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Shipped with Ice Packs
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Description
AFP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 600 amino acids (19-609a.a.) and having a molecular mass of 67.5kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). AFP is expressed with a ADP at N-terminus and 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AFP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
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Synonyms
Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPRTLHRNEYGI ASILDSYQCT AEISLADLAT IFFAQFVQEA TYKEVSKMVK DALTAIEKPT GDEQSSGCLE NQLPAFLEEL CHEKEILEKY GHSDCCSQSE EGRHNCFLAH KKPTPASIPL FQVPEPVTSC EAYEEDRETF MNKFIYEIAR RHPFLYAPTI LLWAARYDKI IPSCCKAENA VECFQTKAAT VTKELRESSL LNQHACAVMK NFGTRTFQAI TVTKLSQKFT KVNFTEIQKL VLDVAHVHEH CCRGDVLDCL QDGEKIMSYI CSQQDTLSNK ITECCKLTTL ERGQCIIHAE NDEKPEGLSP NLNRFLGDRD FNQFSSGEKN IFLASFVHEY SRRHPQLAVS VILRVAKGYQ ELLEKCFQTE NPLECQDKGE EELQKYIQES QALAKRSCGL FQKLGEYYLQ NAFLVAYTKK APQLTSSELM AITRKMAATA ATCCQLSEDK LLACGEGAAD IIIGHLCIRH EMTPVNPGVG QCCTSSYANR RPCFSSLVVD ETYVPPAFSD DKFIFHKDLC QAQGVALQTM KQEFLINLVK QKPQITEEQL EAVIADFSGL LEKCCQGQEQ EVCFAEEGQK LISKTRAALG VHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PDCD6IP HumanDescription:
Programmed Cell Death 6 Interacting Protein Human Recombinant
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
Product # :
PRO-792Price :
Quantity :
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Shipped with Ice Packs
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Description
PDCD6IP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 45.8 kDa. The PDCD6IP is fused to a 20 amino acid His-tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PDCD6IP is a Class E VPS protein which participates in concentration and sorting of cargo proteins of the multivesicular body or incorporation into intralumenal vesicles that are generated by invagination and scission from the limiting membrane of the endosome. PDCD6IP binds to the phospholipid lysobisphosphatidic acid which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. PDCD6IP is an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. PDCD6IP is mandatory for completion of cytokinesis. PDCD6IP takes part in HIV-1 virus budding. PDCD6IP replaces TSG101 in its function of supporting HIV-1 release. PDCD6IP takes part in the regulation of both apoptosis and cell proliferation. PDCD6IP is a cytoplasmic protein that cooperates with apoptosis-associated proteins (ALG-2 and PDCD6) and with the endocytosis-regulator CIN85. Overexpression of PDCD6IP and endophilin
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Synonyms
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATFISVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RAAVGRPLDK HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK SCVLFNCAAL ASQIAAEQNL DNDEGLKIAA KHYQFASGAF LHIKETVLSA LSREPTVDIS PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE VFPVLAAKHC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKTVASR YDEYVNVKDF SDKINRALAA AKKDNDFIYH DRVPDLKDLD PIGKATLVKS TPVNVPISQK FTDLFEKMVP VSVQQSLAAY NQRKADLVNR SIAQMREATT LA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DAP HumanDescription:
Death-Associated Protein Human Recombinant
Death-associated protein 1, DAP-1, DAP, DAP1, Death-Associated Protein.
Product # :
PRO-2055Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DAP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102 a.a.) and having a molecular mass of 13.6kDa.DAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DAP protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Death-Associated Protein (DAP) is a proline-rich protein. DAP, which is a negative regulator of autophagy, takes part in the mediation of IFN-gamma-induced cell death.
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Synonyms
Death-associated protein 1, DAP-1, DAP, DAP1, Death-Associated Protein.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSPPEG KLETKAGHPP AVKAGGMRIV QKHPHTGDTK EEKDKDDQEW ESPSPPKPTV FISGVIARGD KDFPPAAAQV AHQKPHASMD KHPSPRTQHI QQPRK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PRND HumanDescription:
Prion Protein 2 Human Recombinant
Prion protein 2, DOPPEL, DPL, PrPL.
Product # :
PRO-018Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PRND Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (27-152a.a) and having a molecular mass of 16.9kDa. PRND is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PRND protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PRND is a membrane glycosylphosphatidylinositol-anchored glycoprotein which exists mainly in testis. PRND is expressed during embryogenesis, although in the central nervous system it is expressed minimally .Mutations in PRND may cause neurological disorders. PRND located on chromosome 20, about 20 kbp downstream of the gene encoding cellular prion protein, to which it is biochemically and structurally analogous.
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Synonyms
Prion protein 2, DOPPEL, DPL, PrPL.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRGIKHRI KWNRKALPST AQITEAQVAE NRPGAFIKQG RKLDIDFGAE GNRYYEANYW QFPDGIHYNG CSEANVTKEA FVTGCINATQ AANQGEFQKP DNKLHQQVLW RLVQELCSLK HCEFWLERG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DECR1 HumanDescription:
2,4-Dienoyl CoA Reductase 1 Human Recombinant
2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.
Product # :
ENZ-102Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DECR1 Human Recombinant fused to 21 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 322 amino acids (35-335 a.a.) and having a molecular mass of 34.4kDa. The DECR1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DECR1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DECR1 is a mitochondrial protein which exists as a homotetramer and is a member of a family of short-chain dehydrogenases/reductases. DECR1 acts as an auxiliary enzyme of beta-oxidation andt partakes in the metabolism of unsaturated fatty enoyl-CoA esters. in particular, DECR1 uses NADP+ to catalyze the reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA that can subsequently be used as an intermediate in the Krebs cycle. Furthermore, DECR1 is believed to work as a tumor suppressor, possibly downregulating the expression of Neu and slowing the rate of tumorigenesis.
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Synonyms
2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNTEALQSKF FSPLQKAMLP PNSFQGKVAF ITGGGTGLGK GMTTLLSSLG AQCVIASRKM DVLKATAEQI SSQTGNKVHA IQCDVRDPDM VQNTVSELIK VAGHPNIVIN NAAGNFISPT ERLSPNAWKT ITDIVLNGTA FVTLEIGKQL IKAQKGAAFL SITTIYAETG SGFVVPSASA KAGVEAMSKS LAAEWGKYGM RFNVIQPGPI KTKGAFSRLD PTGTFEKEMI GRIPCGRLGT VEELANLAAF LCSDYASWIN GAVIKFDGGE EVLISGEFND LRKVTKEQWD TIEELIRKTK GS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Borrelia Afzelii DbpADescription:
Borrelia Afzelii Decorin Binding Protein A Recombinant
Product # :
BOR-010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Borrelia Afzelii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19 kDa. Borrelia Afzelii DbpA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Afzelii DbpA is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).
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Applications
Western blot with Lyme positive plasma.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GLTP HumanDescription:
Glycolipid Transfer Protein Human Recombinant
Glycolipid transfer protein, GLTP.
Product # :
PRO-1313Price :
Quantity :
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Shipped with Ice Packs
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Description
GLTP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209 a.a.) and having a molecular mass of 26.2kDa.GLTP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLTP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycolipid transfer protein (GLTP) accelerates the intermembrane transfer of different glycolipids. GLTP catalyzes the transfer of various glycosphingolipids between membranes however does not catalyze the transfer of phospholipids. GLTP is involved in the intracellular translocation of glucosylceramides. The GLTP protein is similar to bovine and porcine proteins which accelerate transfer of certain glycosphingolipids and glyceroglycolipids between membranes. GLTP is assumed to be a cytoplasmic protein. GLTP is detected in fibroblasts and in various cancer cell lines.
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Synonyms
Glycolipid transfer protein, GLTP.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALLAEH LLKPLPADKQ IETGPFLEAV SHLPPFFDCL GSPVFTPIKA DISGNITKIK AVYDTNPAKF RTLQNILEVE KEMYGAEWPK VGATLALMWL KRGLRFIQVF LQSICDGERD ENHPNLIRVN ATKAYEMALK KYHGWIVQKI FQAALYAAPY KSDFLKALSK GQNVTEEECL EKIRLFLVNY TATIDVIYEM YTQMNAELNY KV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Clusterin MouseDescription:
Apolipoprotein-J Mouse Recombinant
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Product # :
CYT-1172Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.
Source
HEK293
Formulation
Clusterin filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 50.2kDa.
What is the source or expression system of CLUSTERIN Protein?
HEK293
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DKK1 MouseDescription:
Dickkopf-Related Protein 1 Mouse Recombinant
Dkk-1, mDkk-1, Dkk1, Dickkopf-related protein 1, Dickkopf-1.
Product # :
PRO-2756Price :
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Shipped with Ice Packs
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Description
DKK1 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-272a.a) containing 247 amino acids and having a molecular mass of 26.9kDa.DKK1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The DKK1 solution (0.25mg/ml) contains 50mM MES buffer (pH 6.5) and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Dickkopf-related protein 1 (DKK1) antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by creating a ternary complex with the transmembrane protein KREMEN which promotes internalization of LRP5/6. DKKs have a significant role in vertebrate development, where they locally inhibit Wnt controlled processes for instance antero-posterior axial patterning, limb development, somitogenesis and eye formation. Furthermore, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease in Adults.
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Synonyms
Dkk-1, mDkk-1, Dkk1, Dickkopf-related protein 1, Dickkopf-1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
TLNSVLINSN AIKNLPPPLG GAGGQPGSAV SVAPGVLYEG GNKYQTLDNY QPYPCAEDEE CGSDEYCSSP SRGAAGVGGV QICLACRKRR KRCMRHAMCC PGNYCKNGIC MPSDHSHFPR GEIEESIIEN LGNDHNAAAG DGYPRRTTLT SKIYHTKGQE GSVCLRSSDC AAGLCCARHF WSKICKPVLK EGQVCTKHKR KGSHGLEIFQ RCYCGEGLAC RIQKDHHQAS NSSRLHTCQR
HHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Protein-A/G/L-CysDescription:
Protein A/G/L-Cys Recombinant
Product # :
PRO-1934Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein- A/G/L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ATF HumanDescription:
Apo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Apo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.
Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Protein-L CysDescription:
Protein L Cys Recombinant
Product # :
PRO-1931Price :
Quantity :
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Shipped at Room temp
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- sds-page, HPLC
Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.sds-page, HPLC
More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ADFP HumanDescription:
Adipose Differentiation-Related Protein Human Recombinant
Adipophilin, Adipose differentiation-related protein, ADRP, ADFP, MGC10598.
Product # :
PRO-405Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ADFP Human Recombinant produced in E.Coli is a signle, non-glycosylated, Polypeptide chain containing 444 amino acids and having a molecular mass of 49 kDa. The protein contains an extra 8 amino acid His tag at N-terminus. The ADFP amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q99541 amino acids 4–437.The ADFP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Human ADFP was lyophilized from 0.5mg/ml solution containing 20mM Tris pH-7.5, and 20mM NaCl.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
ADFP is related with the globule surface membrane material. ADFP is a major constituent of the globule surface. Rise in mRNA levels is one of the initial indications of adipocyte differentiation. Mycobacterium leprae regulates ADFP expression to facilitate the accumulation of lipids within infected macrophages for intracellular survival. ADFP is expressed in lipid droplets of vitamin A-storing hepatic stellate cells and additionally in lipid droplets of steatotic hepatocytes. ADFP expression has a role in clear cell renal carcinoma differentiation. ADFP is a component of the lipid droplets in THP-1 cells.
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Synonyms
Adipophilin, Adipose differentiation-related protein, ADRP, ADFP, MGC10598.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS VAVDPQPSVV TRVVNLPLVS STYDLMSSAY LSTKDQYPYL KSVCEMAENG VKTITSVAMT SALPIIQKLE PQIAVANTYA CKGLDRIEER LPILNQPSTQ IVANAKGAVT GAKDAVTTTV TGAKDSVAST ITGVMDKTKG AVTGSVEKTK SVVSGSINTV LGSRMMQLVS SGVENALTKS ELLVEQYLPL TEEELEKEAK KVEGFDLVQK PSYYVRLGSL STKLHSRAYQ QALSRVKEAK QKSQQTISQL HSTVHLIEFA RKNVYSANQK IQDAQDKLYL SWVEWKRSIG YDDTDESHCA EHIESRTLAI ARNLTQQLQT TCHTLLSNIQ GVPQNIQDQA KHMGVMAGDI YSVFRNAASF KEVSDSLLTS SKGQLQKMKE SLDDVMDYLV NNTPLNWLVG PFYPQLTESQ NAQDQGAEMD KSSQETQRSEHKTH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DBI HumanDescription:
DBI Human Recombinant
ACBP, ACBD1, CCK-RP, EP, DBI, EP, MGC70414, Acyl-CoA-binding protein, GABA receptor modulator.
Product # :
PRO-832Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DBI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 107 amino acids (1-87a.a.) and having a molecular mass of 12.2kDa. DBI protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
DBI Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DBI, also known as Acyl-CoA-binding protein isoform 2, is a binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.
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Synonyms
ACBP, ACBD1, CCK-RP, EP, DBI, EP, MGC70414, Acyl-CoA-binding protein, GABA receptor modulator.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF TGKAKWDAWN ELKGTSKEDA MKAYINKVEE LKKKYGI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DCXR HumanDescription:
Dicarbonyl/L-Xylulose Reductase Human Recombinant
DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.
Product # :
ENZ-540Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCXR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 28 kDa. The DCXR is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCXR Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 50mM NaCl & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DCXR catalyzes the NADPH-dependent reduction of numerous pentoses, tetroses, trioses, alpha-dicarbonyl molecules and L-xylulose. DCXR takes part in the uronate cycle of glucose metabolism. DCXR participates in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thus preventing osmolytic stress from occurring in the renal tubules.
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Synonyms
DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG FWAC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DNTTIP1 HumanDescription:
Deoxynucleotidyltransferase Terminal Interacting Protein 1 Human Recombinant
Deoxynucleotidyltransferase Terminal Interacting Protein 1, Novel Protein Similar To Synaptotagmin 1, Terminal Deoxynucleotidyltransferase-Interacting Factor 1, Chromosome 20 Open Reading Frame 167, Tdif1, C20orf167, TdT-Interacting Factor 1, TdT Binding Protein, dJ447F3.4, TDIF1.
Product # :
PRO-1706Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DNTTIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329) and having a molecular mass of 39.0kDa.DNTTIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DNTTIP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
DNTTIP1 binds DNA and increases the activity of terminal deoxynucleotidyltransferase (TDT or DNTT), a DNA polymerase which catalyzes the polymerization of DNA in the absence of a DNA template.
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Synonyms
Deoxynucleotidyltransferase Terminal Interacting Protein 1, Novel Protein Similar To Synaptotagmin 1, Terminal Deoxynucleotidyltransferase-Interacting Factor 1, Chromosome 20 Open Reading Frame 167, Tdif1, C20orf167, TdT-Interacting Factor 1, TdT Binding Protein, dJ447F3.4, TDIF1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGATGDA EQPRGPSGAE RGGLELGDAG AAGQLVLTNP WNIMIKHRQV QRRGRRSQMT TSFTDPAISM DLLRAVLQPS INEEIQTVFN KYMKFFQKAA LNVRDNVGEE VDAEQLIQEA CRSCLEQAKL LFSDGEKVIP RLTHELPGIK RGRQAEEECA HRGSPLPKKR KGRPPGHILS SDRAAAGMVW KPKSCEPIRR EGPKWDPARL NESTTFVLGS RANKALGMGG TRGRIYIKHP HLFKYAADPQ DKHWLAEQHH MRATGGKMAY LLIEEDIRDL AASDDYRGCL DLKLEELKSF VLPSWMVEKM RKYMETLRTE NEHRAVEAPP QT
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DPY30 HumanDescription:
DPY30 Human Recombinant
Dpy-30 Homolog (C. Elegans), Dpy-30-Like Protein, Dpy-30L, Protein Dpy-30 Homolog, HDPY-30, Cps25, Saf19, Protein dpy-30 homolog.
Product # :
PRO-2069Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DPY30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 122 amino acids (1-99 a.a) and having a molecular mass of 13.6 kDa. DPY30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DPY30 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DPY30 is implicated in the methylation of histone H3 at Lys-4, mainly trimethylation. Histone H3 Lys-4 methylation symbolize a specific tag for epigenetic transcriptional activation. DPY30 takes part in histone H3 acetylation. In a teratocarcinoma cell, DPY30 plays a criticalrole in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 Lys-4 methylation at key developmental loci. DPY30 also plays an indirect or direct part in endosomal transport.
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Synonyms
Dpy-30 Homolog (C. Elegans), Dpy-30-Like Protein, Dpy-30L, Protein Dpy-30 Homolog, HDPY-30, Cps25, Saf19, Protein dpy-30 homolog.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEPEQML EGQTQVAENP HSEYGLTDNV ERIVENEKIN AEKSSKQKVD LQSLPTRAYL DQTVVPILLQ GLAVLAKERP PNPIEFLASY LLKNKAQFED RN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DTNBP1 HumanDescription:
Dystrobrevin-Binding Protein 1 Isoform C Human Recombinant
Dysbindin, SDY, DBND, HPS7, My031, FLJ30031, MGC20210, DKFZp564K192, Dystrobrevin-binding protein 1, Hermansky-Pudlak syndrome 7 protein homolog, Hps7-like protein, DTNBP1.
Product # :
PRO-675Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DTNBP1 Human Recombinant fused to 37 a.a. N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-270a.a.) and having a molecular mass of 34.6 kDa.
Source
Escherichia Coli.
Formulation
The DTNBP1 solution contains 20mM Tris pH-8, 0.5mM DTT, 0.1M NaCl, and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DTNBP1 is involved in organelle biogenesis connected with melanosomes, platelet dense granules, and lysosomes. An analogous protein in murine is a part of a protein complex called BLOC-1, and connects to alpha- and beta-dystrobrevins, which are factors of the dystrophin-associated protein complex (DPC). Mutations in DTNBP1 gene are associated with Hermansky-Pudlak syndrome type 7. DTNBP1 gene may also be associated with schizophrenia.
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Synonyms
Dysbindin, SDY, DBND, HPS7, My031, FLJ30031, MGC20210, DKFZp564K192, Dystrobrevin-binding protein 1, Hermansky-Pudlak syndrome 7 protein homolog, Hps7-like protein, DTNBP1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMLS AHWEKKKTSL VELQEQLQQL PALIADLESM TANLTHLEAS FEEVENNLLHLEDLCGQCEL ERCKHMQSQQ LENYKKNKRK ELETFKAELD AEHAQKVLEM EHTQQMKLKE RQKFFEEAFQ QDMEQYLSTG YLQIAERREP IGSMSSMEVN VDMLEQMDLM DISDQEALDV FLNSGGEENT VLSPALGPES STCQNEITLQ VPNPSELRAK PPSSSSTCTD SATRDISEGG ESPVVQSDEE EVQVDTALAT SHTDREATPD GGEDSDS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DCUN1D4 HumanDescription:
DCN1 Defective in Cullin Neddylation 1 Domain Containing 4 Human Recombinant
DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.
Product # :
PRO-1715Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCUN1D4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 36.5kDa.DCUN1D4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DCUN1D4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
DCUN1D4 holds 1 DCUN1 domain.
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Synonyms
DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMHSDAAA VNFQLNSHLS TLANIHKIYH TLNKLNLTED IGQDDHQTGS LRSCSSSDCF NKVMPPRKKR RPASGDDLSA KKSRHDSMYR KYDSTRIKTE EEAFSSKRCL EWFYEYAGTD DVVGPEGMEK FCEDIGVEPE NVVMLVLAWK LDAQNMGYFT LQEWLKGMTS LQCDTTEKLR NTLDYLRSFL NDSTNFKLIY RYAFDFAREK DQRSLDINTA KCMLGLLLGK IWPLFPVFHQ FLEQSKYKVI NKDQWCNVLE FSRTINLDLS NYDEDGAWPV LLDEFVEWYK DKQMS
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DLX3 HumanDescription:
Distal-Less Homeobox 3 Human Recombinant
Homeobox protein DLX-3, DLX3, Distal-Less Homeobox 3, AI4, TDO.
Product # :
PRO-1816Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DLX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (1-186 a.a) and having a molecular mass of 23.4kDa.DLX3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DLX3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
DLX3 belongs to the Distal-less (Dlx) family of genes which includes at least 6 different members. DLX3 plays a regulatory role in the development of the ventral forebrain and also in craniofacial patterning and morphogenesis. Mutation in DLX3 is correlated with Trichodentoosseous syndrome which is an autosomal dominant condition. DLX3 is located in a tail-to-tail configuration with another member of the gene family on the long arm of chromosome 17.
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Synonyms
Homeobox protein DLX-3, DLX3, Distal-Less Homeobox 3, AI4, TDO.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSGSFDR KLSSILTDIS SSLSCHAGSK DSPTLPESSV TDLGYYSAPQ HDYYSGQPYG QTVNPYTYHH QFNLNGLAGT GAYSPKSEYT YGASYRQYGA YREQPLPAQD PVSVKEEPEA EVRMVNGKPK KVRKPRTIYS SYQLAALQRR FQKAQYLALP ERAELAAQLG LTQTQVKIWF QNRRSKFKK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Adiponectin (108-244) HumanDescription:
Adiponectin (108-244 a.a.) Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-073Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
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Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ANGPTL4 HumanDescription:
Angiopoietin-like Protein 4 Human Recombinant
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Product # :
CYT-249Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The ANGPTL4 Human Recombinant is manufactured with N-terminal fusion of His Tag. The Angiopoietin-like Protein 4 His -Tagged Fusion Protein is 25 kDa protein containing 204 amino acid residues of the Angiopoietin-like Protein 4 and 16 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
FIAF (fasting-induced adipose factor) a.k.a ANGPTL4 or PGAR or HFARP is an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. ANGPTL4 is found in human and mouse blood plasma both as a native protein and in a truncated form. In human white adipose tissue and SGBS adipocytes, only the native form of ANGPTL4 could be detected, whereas in mice the differentiation of mouse 3T3-L1 adipocytes is associated with the production of truncated ANGPTL4. However, the truncated ANGPTL4 is produced by human liver. In human blood plasma FIAF is mainly presented in a truncated form (FIAF-S2), whose levels treatment increases (as shown by experimental data). There is an inter individual variation in ANGPTL4 levels of both the truncated and the native form, however those levels were not influenced by prolonged semistarvation and are not associated with body mass index.
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Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Angiopoietin-like Protein 4 Human recombinant at -20°C. Aliquot the ANGPTL4 after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted ANGPTL4 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
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Amino Acid Sequence
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
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Background
Angiopoietin-like Protein 4 Human Recombinant: A Promising Therapeutic Approach for Metabolic Disorders
Abstract:
Angiopoietin-like protein 4 (ANGPTL4) is a multifunctional protein involved in the regulation of lipid metabolism and energy homeostasis. It has emerged as a potential therapeutic target for metabolic disorders, including obesity, dyslipidemia, and insulin resistance. The availability of human recombinant ANGPTL4 protein has provided researchers with a valuable tool to investigate its biological functions and explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL4 in metabolic regulation and discusses the potential of ANGPTL4 human recombinant protein as a therapeutic intervention.Introduction:
Metabolic disorders are a global health challenge with significant implications for cardiovascular health. ANGPTL4, a member of the angiopoietin-like protein family, has gained attention for its role in lipid metabolism and energy balance. ANGPTL4 influences the uptake, storage, and utilization of lipids, as well as glucose metabolism, making it an attractive target for therapeutic interventions.Mechanisms of ANGPTL4 Action:
ANGPTL4 exerts its effects through multiple mechanisms. It inhibits lipoprotein lipase (LPL) activity, reducing the hydrolysis of triglycerides and leading to elevated plasma triglyceride levels. ANGPTL4 also promotes adipose tissue lipolysis, facilitating the release of fatty acids for energy utilization. Moreover, ANGPTL4 affects glucose metabolism by modulating insulin signaling and glucose uptake in various tissues.Role of ANGPTL4 in Metabolic Regulation:
ANGPTL4 plays a critical role in lipid and glucose metabolism. It regulates plasma lipid levels by modulating LPL activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL4 also influences energy homeostasis by promoting lipid mobilization from adipocytes and regulating fatty acid oxidation. Additionally, ANGPTL4 impacts glucose metabolism by modulating insulin sensitivity and glucose uptake in skeletal muscle and adipose tissue.Therapeutic Potential of ANGPTL4 Human Recombinant Protein:
The availability of ANGPTL4 human recombinant protein opens new avenues for therapeutic interventions targeting metabolic disorders. Administration of ANGPTL4 recombinant protein or modulation of ANGPTL4 activity offers potential strategies to improve lipid profiles, reduce adiposity, and enhance insulin sensitivity. Preclinical studies have shown promising results, demonstrating the potential of ANGPTL4 as a therapeutic target for metabolic disorders.Conclusion:
ANGPTL4 represents a promising target for therapeutic interventions in metabolic disorders. Its involvement in the regulation of lipid and glucose metabolism makes it an attractive candidate for the development of novel treatment approaches. The availability of ANGPTL4 human recombinant protein enables further exploration of its therapeutic potential and may contribute to the development of effective interventions for metabolic disorders.What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 25kDa.
What is the source or expression system of ANGPTL4 Protein?
Escherichia Coli.
What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL4 Protein?
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.