Search results
1000 results found for “Phospholipid Scramblase”
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Name :
ACOT7 HumanDescription:
Acyl-CoA Thioesterase 7 Human Recombinant
Cytosolic acyl coenzyme A thioester hydrolase, Acyl-CoA thioesterase 7, Brain acyl-CoA hydrolase, BACH, CTE-IIa, CTE-II, Long chain acyl-CoA thioester hydrolase, ACOT7, ACT, ACH1, LACH, LACH1, hBACH, RP1-120G22.10.
Product # :
ENZ-214Price :
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Description
ACOT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-370) and having a molecular mass of 42.6kDa.ACOT7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACOT7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Acyl-CoA Thioesterase 7 (ACOT7) belongs to the acyl coenzyme family. ACOT7 hydrolyzes the CoA thioester of palmitoyl-CoA and other long-chain fatty acids. Decreased expression of the ACOT7 protein may be linked to mesial temporal lobe epilepsy.
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Synonyms
Cytosolic acyl coenzyme A thioester hydrolase, Acyl-CoA thioesterase 7, Brain acyl-CoA hydrolase, BACH, CTE-IIa, CTE-II, Long chain acyl-CoA thioester hydrolase, ACOT7, ACT, ACH1, LACH, LACH1, hBACH, RP1-120G22.10.
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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 MARPGLIHSA PGLPDTCALL QPPAASAAAA PSMSGPDVET PSAIQICRIM RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP.
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 :
MMAB HumanDescription:
Methylmalonic Aciduria Type B Human Recombinant
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
Product # :
ENZ-248Price :
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Description
MMAB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (33-250 a.a.) and having a molecular mass of 26.3 kDa. The MMAB is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMAB 1mg/ml protein solution contains 20mM Tris pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MMAB protein catalyzes the last step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12 containing coenzyme for methylmalonyl-CoA mutase(MCM). Decreased MMAB activity leads to the inherited disorder vitamin B12 dependent methylmalonic aciduria linked to the cblB complementation group.
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Synonyms
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
MMAB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQSRGPQGVE DGDRPQPSSK TPRIPKIYTK TGDKGFSSTF TGERRPKDDQ VFEAVGTTDE LSSAIGFALE LVTEKGHTFA EELQKIQCTL QDVGSALATP CSSAREAHLK YTTFKAGPIL ELEQWIDKYT SQLPPLTAFI LPSGGKISSA LHFCRAVCRR AERRVVPLVQ MGETDANVAK FLNRLSDYLF TLARYAAMKE GNQEKIYKKN DPSAESEGL.
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 :
TYMP HumanDescription:
Thymidine Phosphorylase Human Recombinant
Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.
Product # :
ENZ-005Price :
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Description
TYMP Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 493 amino acids (11-482 a.a.) and having a molecular mass of 51.3kDa. The TYMP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TYMP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Thymidine phosphorylase precursor (TYMP) is a platelet-derived endothelial cell growth factor that catalyzes the formation of thymine and 2-deoxy-D-ribose-1-phosphate from thymidine and orthophosphate. TYMP is an angiogenic inducer that potently stimulates the growth of endothelial cells and induces chemotaxis. TYMP has a highly restricted target cell specificity acting only on endothelial cells. An increased expression of TYMP is found in a broad array of different solid tumors and inflammatory diseases and is frequently associated with poor prognosis. Mutations in the TYMP gene are linked to mitochondrial neurogastrointestinal encephalomyopathy.
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Synonyms
Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.
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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 MAPPAPGDFS GEGSQGLPDP SPEPKQLPEL IRMKRDGGRL SEADIRGFVA AVVNGSAQGA QIGAMLMAIR LRGMDLEETS VLTQALAQSG QQLEWPEAWR QQLVDKHSTG GVGDKVSLVL APALAACGCK VPMISGRGLG HTGGTLDKLE SIPGFNVIQS PEQMQVLLDQ AGCCIVGQSE QLVPADGILY AARDVTATVD SLPLITASIL SKKLVEGLSA LVVDVKFGGA AVFPNQEQAR ELAKTLVGVG ASLGLRVAAA LTAMDKPLGR CVGHALEVEE ALLCMDGAGP PDLRDLVTTL GGALLWLSGH AGTQAQGAAR VAAALDDGSA LGRFERMLAA QGVDPGLARA LCSGSPAERR QLLPRAREQE ELLAPADGTV ELVRALPLAL VLHELGAGRS RAGEPLRLGV GAELLVDVGQ RLRRGTPWLR VHRDGPALSG PQSRALQEAL VLSDRAPFAA PSPFAELVLP PQQ.
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 :
HARS HumanDescription:
Histidyl-tRNA Synthetase Human Recombinant
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.
Product # :
ENZ-268Price :
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Description
Histidyl-tRNA Synthetase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 55 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 500mM NaCl and 10mM Tris (pH 8.0) and 6M Urea.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
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Synonyms
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored below -18°C.Please prevent freeze-thaw cycles.
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Applications
Western Blot: Strongly reactive with human anti Histidyl-tRNA Synthetase antisera.
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 :
PDIA3 AntibodyDescription:
Protein Disulfide Isomerase A3, Mouse Anti Human
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
Product # :
ANT-633Price :
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
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Introduction
PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.
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Synonyms
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human PDIA3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PDIA3 protein 25-505 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and k light chain.
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Clone
PAT9E9AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
PDIA3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
CoV-2 3CLDescription:
Coronavirus 2019 3CL Protease Recombinant
Product # :
SARS-058Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant Coronavirus 2019 3CL Protease having a Mw of approximately 33.8 kDa was purified from E. coli. The CoV-2 3CL contains 306 amino acids and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
CoV-2 3CL solution contains 5 % Trehalose, 0.02 % Tween-20 and PBS, pH 7.4.
Purity
Protein is >98% pure as determined by SDS-PAGE and HPLC analyses.
Biological Activity
CoV-2 3CL is a cysteine protease that cleaves proteins with sequences including LQ(S/A/G). The cleavage takes c-terminal to the glutamine residue.
More Info
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Introduction
The SARS CoV-2 3CL protease (C30 Endopeptidase) derived from human SARS-CoV-2 is a C30-type cysteine protease situated in the NS3 segment. SARS CoV-2 3CL protease biological functionality is needed to process viral polyproteins to functional complete units. SARS CoV-2 3CL protease (main protease) is the core protease protein in CoV and corresponds to non-structural protein 5. SARS CoV-2 3CL cleaves the CoV polyprotein at 11 locations. SARS CoV-2 3CL protease has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. SARS CoV-2 3CL protease at position P1 cleaves the bond between the glutamine and serine/alanine/glycine. SARS CoV-2 3CL protease is necessary in the processing of the CoV replicase polyprotein.
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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. CoV-2 3CL 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
SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDVVYCPR HVICTSEDML NPNYEDLLIR KSNHNFLVQA GNVQLRVIGH SMQNCVLKLK VDTANPKTPK YKFVRIQPGQ TFSVLACYNG SPSGVYQCAM RPNFTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGN FYGPFVDRQT AQAAGTDTTI TVNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA VLDMCASLKE LLQNGMNGRT ILGSALLEDE FTPFDVVRQC SGVTFQ
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 :
OmpADescription:
Outer Membrane Protein-A Bacterial Recombinant
Outer Membrane Protein-A, OmpA.
Product # :
PRO-571Price :
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Shipped at Room temp
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Description
The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.More Info
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Introduction
The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
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Synonyms
Outer Membrane Protein-A, OmpA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. 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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Solubility
It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.
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 :
PAPP-A HumanDescription:
Pregnancy-Associated Plasma Protein-1 Human Recombinant
Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.
Product # :
ENZ-441Price :
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Description
PAPP-A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 191 amino acids fragment (81-271) corresponding to the PAPP-A “Jelly-Roll” domain fragment, having a total molecular mass of 25.75kDa and fused with an amino-terminal hexahistidine tag. The PAPP-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PAPP-A protein is supplied in 20mM Tris Hcl PH 8.0, 4M Urea and 50% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PAPPA is a large zinc binding protein, which acts as a metalloprotease and specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. PAPP-A can also act as a regulator of IGF bioactivity in a number of biological systems, including the human ovary and cardiovascular systems. It was shown that PAPP A levels are elevated in patients with unstable angina or acute myocardial infarction. Furthermore, PAPPA is believed to be involved in local proliferative processes such as wound healing and bone remodeling. Moreover, PAPP-A is produced in high concentrations during pregnancy and is released into the maternal circulation. In placenta, PAPP A is expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi.
Lower levels of PAPPA are found in an array of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow, colon, fibroblasts and osteoblasts. PAPP-A is present in serum and placenta during pregnancy; with levels increasing throughout pregnancy. Low levels of PAPP A are associated with a number of foetal chromosomal abnormalities, as well as pre-eclampsia and stillbirth.
PAPPA levels may be a potentially highly specific marker for heart disease.
PAPP-A proteolytic activity is inhibited by targeting substrate exosite binding. -
Synonyms
Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.
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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. Please avoid freeze thaw cycles.
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 :
FNDC5 Human, YeastDescription:
Fibronectin Type III Domain Containing 5 Human Recombinant, Yeast
Fibronectin type III domain-containing protein 5, Fibronectin type III repeat-containing protein 2, Irisin, FRCP2, FNDC5.
Product # :
PRO-1663Price :
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Shipped at Room temp
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Description
Fibronectin Type III Domain Containing 5 Human Recombinant produced in yeast is a glycosylated, polypeptide chain containing 110 amino acids and having a molecular mass of 20-25 kDa.FNDC5 is purified by proprietary chromatographic techniques.
Source
Yeast.
Formulation
The FNDC5 was lyophilized from 0.45 µm filtered solution in PBS.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The biological activity of recombinant human irisin was measured by the ability to induce UCP-1 expression of adipocytes. The specific activity is 10ng/ml.More Info
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Introduction
Fibronectin Type III Domain Containing 5 (Irisin) is a newly discovered hormone, secreted into circulation by muscle, which acts on white adipocytes and promotes WAT “browning”. r-Irisin can reduce body weight and cause induction of brown adipocyte in vivo, including a capacity for thermogenic energy expenditure mediated by uncoupling protein 1 (UCP-1). Irisin mature protein is comprised of 110 amino acid residues and two potential glycosylation sites. High levels of Irisin can be found in the heart whereas Very low expression is found in the colon, pancreas and spleen, if any.
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Synonyms
Fibronectin type III domain-containing protein 5, Fibronectin type III repeat-containing protein 2, Irisin, FRCP2, FNDC5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin Type III Domain Containing 5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FNDC5 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 Fibronectin Type III Domain Containing 5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
S_P__S__A__P__V__N__V__T__V__R__H__L__K__A__N__S__A__V__V__S_
W__D__V__L__E__D__E__V__V__I__G__F__A__I__S__Q__Q__K__K__D _V__R__M__L__R__F__I__Q__E__V__N__T__T__T__R__S__C__A__L__W_
_ D__L__E__E__D__T__E__Y__I__V__H__V__Q__A__I__S__I__Q__G__Q_
S__P__A__S__E__P__V__L__F__K__T__P__R__E__A__E__K__M__A__S_ K
__N__K__D__E__V__T__M__K__E.
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 :
CFL1 HumanDescription:
Cofilin-1 Human Recombinant
CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.
Product # :
PRO-591Price :
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Shipped with Ice Packs
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Description
Cofilin1 Human Recombinant (aa 1-166) fused to a 20 aa N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 186 amino acids and having a molecular mass of 20kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Cofilin is a family of actin-binding proteins which disassembles actin filaments. It is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.
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Synonyms
CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCLSEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLVFIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL.
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 :
GOPC HumanDescription:
Golgi-Associated PDZ and Coiled-Coil Motif Containing Human Recombinant
CAL, dJ94G16.2, FIG, GOPC1, PIST, Golgi-associated PDZ and coiled-coil motif-containing protein, PDZ protein interacting specifically with TC10, CFTR-associated ligand, Fused in glioblastoma, GOPC.
Product # :
PRO-793Price :
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Description
GOPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (278-454 a.a.) and having a molecular mass of 21.5 kDa. The GOPC is fused to a 20 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The GOPC protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GOPC is a PDZ domain-containing Golgi protein which binds the extreme C terminus of proteins in a sequence-specific manner. GOPC participates in intracellular protein trafficking and degradation. GOPC regulates CFTR chloride currents and acid-induced ACCN3 currents by modulating cell surface expression of both channels. GOPC regulates the intracellular trafficking of the ADR1B receptor. GOPC takes part in autophagy. GOPC over expression results in CFTR intracellular retention and degradation in the lysosomes.
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Synonyms
CAL, dJ94G16.2, FIG, GOPC1, PIST, Golgi-associated PDZ and coiled-coil motif-containing protein, PDZ protein interacting specifically with TC10, CFTR-associated ligand, Fused in glioblastoma, GOPC.
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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 MIRKVLLLKE DHEGLGISIT GGKEHGVPIL ISEIHPGQPA DRCGGLHVGD AILAVNGVNL RDTKHKEAVT ILSQQRGEIE FEVVYVAPEV DSDDENVEYE DESGHRYRLY LDELEGGGNP GASCKDTSGE IKVLQGFNKK AVTDTHENGD LGTASETPLD DGASKLDDLH TLYHKKSY.
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 :
CLTA HumanDescription:
Clathrin, Light Chain A Human Recombinant
Clathrin light chain A, Lca, CLTA.
Product # :
PRO-1144Price :
Quantity :
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Description
CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.
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Synonyms
Clathrin light chain A, Lca, CLTA.
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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 MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.
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 :
RCHY1 HumanDescription:
Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
Product # :
PRO-1536Price :
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Description
RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.
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Synonyms
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
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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 MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.
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 :
CXCL5 MouseDescription:
Epithelial Neutrophil-Activating Protein 78 Mouse Recombinant (CXCL5)
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
Product # :
CHM-365Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epithelial Neutrophil-Activating Protein 78 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 9.8kDa. The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM sodium phosphate buffer, pH 7.4 & 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
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Synonyms
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ENA-78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APSSVIAATE LRCVCLTVTP KINPKLIANL EVIPAGPQCP TVEVIAKLKN QKEVCLDPEA PVIKKIIIQK ILGSDKKKAK RNALAVERTA SVQ.
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Background
What is the molecular weight/Mw of CXCL5 MOUSE Protein?
CXCL5 MOUSE Protein has a total Mw of 9.8kDa.
What is the source or expression system of CXCL5 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL5 MOUSE Protein?
CXCL5 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL5 MOUSE Protein?
APSSVIAATE LRCVCLTVTP KINPKLIANL EVIPAGPQCP TVEVIAKLKN QKEVCLDPEA PVIKKIIIQK ILGSDKKKAK RNALAVERTA SVQ.
What applications can CXCL5 MOUSE Protein be used in?
CXCL5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 MOUSE Protein?
The endotoxin level is minimal, CXCL5 MOUSE 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 :
PALM HumanDescription:
Paralemmin Human Recombinant
Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 1.
Product # :
PRO-2053Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PALM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (1-387) and having a molecular mass of 44.5kDa.PALM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PALM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Paralemmin (PALM) belongs to the paralemmin protein family which takes part in plasma membrane dynamics and cell process formation. The product of PALM is related with the cytoplasmic face of plasma membranes and is implicated in plasma membrane dynamics in neurons and other cell types.
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Synonyms
Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 1.
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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 MGSMEVLAAE TTSQQERLQA IAEKRKRQAE IENKRRQLED ERRQLQHLKS KALRERWLLE GTPSSASEGD EDLRRQMQDD EQKTRLLEDS VSRLEKEIEV LERGDSAPAT AKENAAAPSP VRAPAPSPAK EERKTEVVMN SQQTPVGTPK DKRVSNTPLR TVDGSPMMKA AMYSVEITVE KDKVTGETRV LSSTTLLPRQ PLPLGIKVYE DETKVVHAVD GTAENGIHPL SSSEVDELIH KADEVTLSEA GSTAGAAETR GAVEGAARTT PSRREITGVQ AQPGEATSGP PGIQPGQEPP VTMIFMGYQN VEDEAETKKV LGLQDTITAE LVVIEDAAEP KEPAPPNGSA AEPPTEAASR EENQAGPEAT TSDPQDLDMK KHRCKCCSIM.
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 :
CRTAP HumanDescription:
Cartilage Associated Protein Human Recombinant
CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.
Product # :
PRO-1862Price :
Quantity :
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Shipped with Ice Packs
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Description
CRTAP Human Recombinant produced in E. coli is. a single polypeptide chain containing 398 amino acids (27-401) and having a molecular mass of 46.4kDa. CRTAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRTAP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cartilage-associated protein (CRTAP) is a secreted protein localizing to the extracellular space which takes part in collagen post-translational modifications, extracellular fibril assembly and intracellular trafficking. CRTAP which is mainly expressed with predominant expression in articular chondrocytes is essential for efficient 3-hydroxylation of fibrillar collagen prolyl residues. Mutations in the gene encoding CRTAP might cause to autosomal recessive osteogenesis imperfecta (OI) type 7 and type 2B.
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Synonyms
CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.
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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 MGSQYERYSF RSFPRDELMP LESAYRHALD KYSGEHWAES VGYLEISLRL HRLLRDSEAF CHRNCSAAPQ PEPAAGLASY PELRLFGGLL RRAHCLKRCK QGLPAFRQSQ PSREVLADFQ RREPYKFLQF AYFKANNLPK AIAAAHTFLL KHPDDEMMKR NMAYYKSLPG AEDYIKDLET KSYESLFIRA VRAYNGENWR TSITDMELAL PDFFKAFYEC LAACEGSREI KDFKDFYLSI ADHYVEVLEC KIQCEENLTP VIGGYPVEKF VATMYHYLQF AYYKLNDLKN AAPCAVSYLL FDQNDKVMQQ NLVYYQYHRD TWGLSDEHFQ PRPEAVQFFN VTTLQKELYD FAKENIMDDD EGEVVEYVDD LLELEETS.
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 :
SCGB1A1 HumanDescription:
Uteroglobin Human Recombinant
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Product # :
CYT-743Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Uteroglobin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 15.8kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.More Info
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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
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Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.
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 :
HPGDS HumanDescription:
Hematopoietic Prostaglandin D Synthase Human Recombinant
Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.
Product # :
ENZ-616Price :
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Shipped with Ice Packs
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Description
HPGDS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-199 a.a.) and having a molecular mass of 25.9kDa.HPGDS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HPGDS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.
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Synonyms
Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.
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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 MGSHMPNYKL TYFNMRGRAE IIRYIFAYLD IQYEDHRIEQ ADWPEIKSTL PFGKIPILEV DGLTLHQSLA IARYLTKNTD LAGNTEMEQC HVDAIVDTLD DFMSCFPWAE KKQDVKEQMF NELLTYNAPH LMQDLDTYLG GREWLIGNSV TWADFYWEIC
STTLLVFKPD LLDNHPRLVT LRKKVQAIPA VANWIKRRPQ TKL.
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 :
CXCL14 MouseDescription:
BRAK (CXCL14) Mouse Recombinant
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
Product # :
CHM-007Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
CXCL14 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 500mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of CXCL14 as determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
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Background
What is the molecular weight/Mw of CXCL14 MOUSE Protein?
CXCL14 MOUSE Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL14 MOUSE Protein?
CXCL14 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 MOUSE Protein?
The ED50 of CXCL14 as determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 MOUSE Protein?
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 MOUSE Protein be used in?
CXCL14 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 MOUSE Protein?
The endotoxin level is minimal, CXCL14 MOUSE 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 :
TDP2 HumanDescription:
Tyrosyl-DNA Phosphodiesterase 2 Human Recombinant
AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein II.
Product # :
ENZ-698Price :
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Description
TDP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362) and having a molecular mass of 43.3kDa. TDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TDP2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.
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Synonyms
AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein II.
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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 MGSMELGSCL EGGREAAEEE GEPEVKKRRL LCVEFASVAS CDAAVAQCFL AENDWEMERA LNSYFEPPVE ESALERRPET ISEPKTYVDL TNEETTDSTT SKISPSEDTQ QENGSMFSLI TWNIDGLDLN NLSERARGVC SYLALYSPDV IFLQEVIPPY YSYLKKRSSN YEIITGHEEG YFTAIMLKKS RVKLKSQEII PFPSTKMMRN LLCVHVNVSG NELCLMTSHL ESTRGHAAER MNQLKMVLKK MQEAPESATV IFAGDTNLRD REVTRCGGLP NNIVDVWEFL GKPKHCQYTW DTQMNSNLGI TAACKLRFDR IFFRAAAEEG HIIPRSLDLL GLEKLDCGRF PSDHWGLLCN LDIIL.
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 :
PPIL2 HumanDescription:
Cyclophilin-60 Human Recombinant
CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.
Product # :
ENZ-497Price :
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Description
PPIL2 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 547 amino acids (1-527 a.a.) and having a molecular mass of 61.6 kDa. The PPIL2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPIL2 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 290 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
PPIL2 is part of the cyclophilin family of peptidylprolyl isomerases which are highly conserved ubiquitous proteins that play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL2 interacts with the proteinase inhibitor eglin c and is localized in the nucleus. PPIL2 increases folding of proteins andcatalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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Synonyms
CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.
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Physical Appearance
Sterile Filtered clear 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 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT NAETRETLQE YKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF TSTAMVPETT EAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH.
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 :
SERPINA7 HumanDescription:
Serpin Peptidase Inhibitor, Clade A Member 7 Human
Product # :
PRO-2739Price :
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Shipped at Room temp
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Description
Human Serpin Peptidase Inhibitor, Clade A Member 7 Protein produced in Human plasma having a molecular mass of approximately 55kD.
Source
Human serum.
Formulation
The protein was lyophilized (0.2 µm filtered) from 20mM NH4HCO3.
Purity
Greater than 98.0%.
More Info
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Introduction
Thyroxine binding globulin, also known as SERPINA7, is synthesized in the liver and carried in the blood.
SERPINA7 may be decreased or increased in a number of diseases. Its main value in diagnosis is to assess thyroid function by determining the amount of free T3/T4.
Thyroxine binding globulin, binds and transports thyroid hormones in the circulation. SERPINA7 carries the majority of the T3/T4 in the blood. SERPINA7 has only one binding site for T3/T4 and about 25% of Thyroxine binding globulin is usually saturated. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
SERPINA7 Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized SERPINA7 Human in phosphate buffer containing 0.15M NaCl.
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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Parvovirus B19, Syphilis and HIV/HBV/HCV (PCR).
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 :
SARS MatrixDescription:
SARS-Associated Coronavirus Matrix Recombinant
Product # :
SARS-251Price :
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Shipped with Ice Packs
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Description
The E.Coli derived 30kDa recombinant protein contains the Matrix protein 182-216 amino acids immunodominant regions.
Formulation
50mM Tris-HCl, 60mM NaCl and 50% glycerol.
Purity
SARS Matrix Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.
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Stability
SARS Matrix protein is shipped at ambient temperature. Upon arrival, store at -20C.
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Applications
SARS Matrix antigen can be used for ELISA and Western blots, excellent antigen for detection of SARS with minimal specificity problems.
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Specificity
SARS Matrix protein is Immunoreactive with sera of SARS-infected individuals.
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Purification Method
SARS Matrix protein was purified by proprietary chromatographic technique.
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 :
tPA HumanDescription:
Tissue Plasminogen Activator Human Recombinant
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.
Product # :
ENZ-263Price :
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Shipped at Room temp
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Description
Tissue Plasminogen Activator Human Recombinant produced in CHO cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a molecular mass of 59008.71 Dalton. tPA is a serine protease enzyme that converts plasminogen to plasmin. The tPA is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells (CHO)
Formulation
Each mg of t-PA contains 1.7 gr L-arginine, 0.5 gr phosphoric acid and 4 mg tween 80.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. -
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized t-PA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution tPA 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 t-PA in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Enzymatic Activity
580,000 IU/mg.
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.