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冷藏/冷冻
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Human Clusterin
大量
上海经科化学科技有限公司
无
2μg/10μg/1mg
Catalogue Number | CYT-549 |
Synonyms | CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J. |
Introduction | Clusterin also named 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 five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 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. A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates. Clusterin is up- or 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. |
Description | Apolipoprotein-J canine Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 433 amino acids and having a molecular mass of 50.6 kDa. The protein is fused to His tag at N-Terminus. The Apolipoprotein-J canine is purified by proprietary chromatographic techniques. The amino acids sequence is identical to UniProtKB/Swiss-Prot entry P25473 amino acids 23–445. |
Source | Escherichia Coli. |
Physical Appearance | Sterile Filtered White lyophilized (freeze-dried) powder. |
Formulation | Canine Clusterin was lyophilized from PBS, pH 7.5. |
Solubility | Add deionized H2O to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. |
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. |
Amino Acid Sequence | MKHHHHHHAS DQAVSDTELQ EMSTEGSKYI NKEIKNALKG VKQIKTLIEQ TNEERKSLLS NLEEAKKKKE DALNDTKDSE TKLKASQGVC NDTMMALWEE CKPCLKQTCM KFYARVCRSG SGLVGHQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHA LDVMQDSFNR ASSIMDELFQ DRFFTREPQD TYHYSPFSLF QRRPFFNPKF RIARNIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE. |
Purity | Greater than 95% as determined by SDS PAGE. |
Catalogue Number | CYT-618 |
Synonyms | CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Glycoprotein 80, Gp80, CLU. |
Introduction | Clusterin mRNA and Clusterin protein are shown to increase with androgen treatment. Binding of clusterin to the LDL-Receptor plays a role in the pathogenesis of membranous glomerulonephritis. Clusterin is down regulated in CaP in association with matched benign controls. Clusterin is involved in cellular senescence and tumorigenesis. Clusterin is involved in photo-oxidative cell death pathway. Clusterin is a functional tumor marker for the diagnosis of pediatric large cell lymphoma. Clusterin is activated in low pH. Clusterin is involved in the inhibition of NF-kappaB signaling through stabilization of IkappaBs thus results in suppression of tumor cell motility. N-terminal deletion of clusterin is vital for its alterations of biogenesis in esophageal squamous cell carcinoma. |
Description | Clusterin Canine Recombinant produced in HEK293 cells is a glycosylated, Polypeptide chain containing 436 amino acids and having a molecular mass of 50.72 kDa. The protein is fused with 13 amino acid Flag tag at N-Terminus. The Apolipoprotein-J Canine is purified by proprietary chromatographic techniques. |
Source | Human Embryonic Kidney 293 Cells. |
Physical Appearance | Filtered White lyophilized (freeze-dried) powder. |
Formulation | Canine Clusterin was filtered (0.4µm) and lyophilized from 0.5mg/ml solution containing 20mM Tris buffer and 20mM NaCl, pH 7.5. |
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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture. |
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. |
Purity | Greater than 95% as determined by SDS PAGE. |
Amino Acid Sequence | PGDYKDDDDK PAGDQAVSDT ELQEMSTEGS KYINKEIKNA LKGVKQIKTL IEQTNEERKS LLSNLEEAKK KKEDALNDTK DSETKLKASQ GVCNDTMMAL WEECKPCLKQ TCMKFYARVC RSGSGLVGHQ LEEFLNQSSP FYFWMNGDRI DSLLENDRQQ THALDVMQDS FNRASSIMDE LFQDRFFTRE PQDTYHYSPF SLFQRRPFFN PKFRIARNII PFPRFQPLNF HDMFQPFFDM IHQAQQAMDV NLHRIPYHFP IEFPEEDNRT VCKEIRHNST GCLKMKDQCE KCQEILSVDC SSNNPAQVQL RQELSNSLQI AEKFTKLYDE LLQSYQEKMF NTSSLLKQLN EQFSWVSQLA NLTQSEDPFY LQVTTVGSQT SDSNVPVGFT KVVVKLFDSD PITVMIPEAV SRNNPKFMET VAEKALQEYRQKHREE. |
Catalogue Number | CYT-548 |
Synonyms | CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J. |
Introduction | Clusterin also named 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 five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 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. A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates. Clusterin is up- or 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. |
Source | Plasma. |
Physical Appearance | Filtered White lyophilized (freeze-dried) powder. |
Formulation | Human native Clusterin was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.1M phosphate buffer, 0.15M NaCl pH 7.5. |
Solubility | It is recommended to add deionized H2O to prepare a working stock solution of 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. |
Stability | Store lyophilized Clusterin 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. |
Purity | Greater than 95% as determined by SDS PAGE. |
Catalogue Number | CYT-278 |
Synonyms | CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J. |
Introduction | Clusterin also named 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 five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 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. A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates. Clusterin is up- or 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. |
Description | Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa. Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques. |
Source | 293 cell line (Human embryonic kidney). |
Physical Appearance | Filtered, White, Lyophilized powder. |
Formulation | Filtered (0.4 micron) and lyophilized PBS, pH 7.5. |
Solubility | Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture. |
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. |
Amino acid sequence | DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK. |
Purity | Greater than 95% as determined by SDS PAGE. |
Catalogue Number | CYT-814 |
Synonyms | CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU. |
Introduction | Clusterin also named 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 five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 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. A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates. Clusterin is up- or 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. |
Description | Clusterin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 463 amino acids (23-449 a.a.) and having a molecular mass of 54.1kDa. Clusterin is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. |
Source | Escherichia Coli. |
Physical Appearance | Sterile filtered colorless solution. |
Formulation | Clusterin protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT. |
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. |
Purity | Greater than 85% as determined by SDS-PAGE. |
Amino Acid Sequence | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE. |
Catalogue Number | CYT-437 |
Synonyms | CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2. |
Introduction | Clusterin also named 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 five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 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. A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates. Clusterin is up- or 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. |
Description | The Clusterin Rat was constructed as a recombinant protein with N-terminal fusion of T7-Tag (16AA) and C-terminal fusion of His-Tag (9AA). The Clusterin Rat His-Tagged Fusion Protein, produced in E.coli, is 26.5 kDa protein containing 215 amino acid residues of the APO-J Rat and 25 additional amino acid residues – His-Tag, T7-Tag (underlined). |
Amino Acid Sequence | MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH. |
Source | Escherichia Coli. |
Physical Appearance | White lyophilized (freeze-dried) powder. |
Formulation | Lyophilized from 0.5 mg/ml in 0.01M Tris pH 7.2. |
Solubility | Add 0.2 ml of deionized H2O and let the lyophilized pellet dissolve completely. |
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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