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1000 results found for “Exendin”
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Name :
ESM1 Human, HEKDescription:
Endothelial Cell-Specific Molecule 1 Human Recombinant, HEK
Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.
Product # :
PRO-2476Price :
Quantity :
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Shipped at Room temp
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Description
ESM1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-184) containing 175 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 19.5kDa (calculated).
Source
HEK293 cells.
Formulation
ESM1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.
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Synonyms
Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.
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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. ESM1 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
WSNNYAVDCP QHCDSSECKS SPRCKRTVLD DCGCCRVCAA GRGETCYRTV SGMDGMKCGP GLRCQPSNGE DPFGEEFGIC KDCPYGTFGM DCRETCNCQS GICDRGTGKC LKFPFFQYSV TKSSNRFVSL TEHDMASGDG NIVREEVVKE NAAGSPVMRK WLNPR HHHHH HHHHH.
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 :
KLK10 Human, Sf9Description:
Kallikrein-10 Human Recombinant, Sf9
Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.
Product # :
ENZ-1090Price :
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Shipped with Ice Packs
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Description
KLK10 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 252 amino acids (34-276 a.a) and having a molecular mass of 27.8kDa. KLK10 protein is fused to a 6 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Sf9, Baculovirus cells.
Formulation
KLK10 protein solution (0.5mg/ml) contains 30% glycerol, 20mM Tris-HCl (pH 8.0), 0.15M NaCl & 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.
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Synonyms
Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.
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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
ADPALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSNHHHH HH.
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 :
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 :
Quantity :
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Shipped with Ice Packs
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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.Citations
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.
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Name :
CEACAM3 Human, Sf9Description:
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3 Human Recombinant, Sf9
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3, Carcinoembryonic Antigen CGM1, CD66d Antigen , CD66D, CGM1, Carcinoembryonic Antigen Gene Family Member 1, Nonspecific Cross-Reacting Antigen, W264, W282, CEA, CEACAM3.
Product # :
PRO-2443Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEACAM3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 130 amino acids (35-155a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CEACAM3 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CEACAM3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3, also known as CEACAM3, is a member of the immunoglobulin super family. The genes in this family encode cell adhesion proteins, which are expressed at higher levels in tumorous tissues rather than in normal tissues. CEACAM3 plays a significant part in the clearance of pathogens through the innate immune system. In addition, CEACAM3 is accountable for RAC1 stimulation in the course of pathogen phagocytosis.
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Synonyms
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3, Carcinoembryonic Antigen CGM1, CD66d Antigen , CD66D, CGM1, Carcinoembryonic Antigen Gene Family Member 1, Nonspecific Cross-Reacting Antigen, W264, W282, CEA, CEACAM3.
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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
ADPKLTIESM PLSVAEGKEV LLLVHNLPQH LFGYSWYKGE RVDGNSLIVG YVIGTQQATP GAAYSGRETI YTNASLLIQN VTQNDIGFYT LQVIKSDLVN EEATGQFHVY QENAPGLPVG AVAGHHHHHH.
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 :
Procalcitonin PorcineDescription:
Procalcitonin Porcine Recombinant
Calcitonin, Preprocalcitonin, Calca.
Product # :
HOR-018Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Procalcitonin Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Thr26-Asn141) containing 126 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 14.1kDa.
Source
Escherichia Coli.
Formulation
Procalcitonin was filtered (0.4µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Calcitonin, Preprocalcitonin, Calca.
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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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin 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
MKHHHHHHASTPLRSALETL PDPGPLSEKE GRLLLAALVK AYVQRKTNEL EQEQEQETEG SSLDSSRAKR CSNLSTCVLS AYWRNLNNFH RFSGMGFGPE TPGKKSDIAS SLERDLFPRG MPQDAN.
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 :
Tamm HorsfallDescription:
Recombinant Human Tamm Horsfall Glycoprotein
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-1206Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.
Source
HEK293
Formulation
The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE analysis.
SDS-PAGE
Citations
More Info
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Introduction
Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
Reduced Uromodulin levels is associated with chronic kidney disease.
UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.
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Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
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
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
DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH
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Background
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
What is the molecular weight/Mw of UMOD Protein?
UMOD Protein has a total Mw of 65kDa.
What is the source or expression system of UMOD Protein?
HEK293.
What is the Purity of UMOD Protein?
UMOD Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of UMOD Protein?
The biological functionality of UMOD Protein will be determined in the future.
What is the amino acid sequence of UMOD Protein?
UMOD Protein is composed from 595 amino acids.
What applications can UMOD Protein be used in?
UMOD Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for UMOD Protein?
The endotoxin level is minimal, UMOD 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 :
CXCL12 Rat betaDescription:
Stromal Cell-Derived Factor-1 beta Rat Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Product # :
CHM-248Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SDF-1 beta Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8.4 kDa. The Rat SDF-1b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Rat SDF1B protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phsophate buffer pH-7.4 and 0.15M NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.Citations
More Info
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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1b 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
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.
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Background
What is the molecular weight/Mw of CXCL12 RAT BETA Protein?
CXCL12 RAT BETA Protein has a total Mw of 8.4kDa.
What is the source or expression system of CXCL12 RAT BETA Protein?
Escherichia Coli.
What is the Purity of CXCL12 RAT BETA Protein?
CXCL12 RAT BETA Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL12 RAT BETA Protein?
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.
What is the amino acid sequence of CXCL12 RAT BETA Protein?
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.
What applications can CXCL12 RAT BETA Protein be used in?
CXCL12 RAT BETA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL12 RAT BETA Protein?
The endotoxin level is minimal, CXCL12 RAT BETA Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL12 RAT BETA that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL12 RAT BETA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
SERPIND1 HumanDescription:
Serpin Peptidase Inhibitor, Clade D Member 1 Human Recombinant
Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.
Product # :
PRO-2050Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SERPIND1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (58-499) and having a molecular mass of 53.3kDa.SERPIND1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SERPIND1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Serpin Peptidase Inhibitor, Clade D Member 1 (SERPIND1) is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate. SERPIND1 gene is a member of the serpin gene superfamily. SERPIND1 protein contains 5 exons and 4 introns. SERPIND1 shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. SERPIND1 gene mutations are linked with cofactor II deficiency. SERPIND1 protein is activated by dermatan sulfate, and glycosaminoglycans. Allelic variations in the SERPIND1 gene are linked with cofactor II deficiency.
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Synonyms
Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.
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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 MGSDFHKENT VTNDWIPEGE EDDDYLDLEK IFSEDDDYID IVDSLSVSPT DSDVSAGNIL QLFHGKSRIQ RLNILNAKFA FNLYRVLKDQ VNTFDNIFIA PVGISTAMGM ISLGLKGETH EQVHSILHFK DFVNASSKYE ITTIHNLFRK LTHRLFRRNF GYTLRSVNDL YIQKQFPILL DFKTKVREYY FAEAQIADFS DPAFISKTNN HIMKLTKGLI KDALENIDPA TQMMILNCIY FKGSWVNKFP VEMTHNHNFR LNEREVVKVS MMQTKGNFLA ANDQELDCDI LQLEYVGGIS MLIVVPHKMS GMKTLEAQLT PRVVERWQKS MTNRTREVLL PKFKLEKNYN LVESLKLMGI RMLFDKNGNM AGISDQRIAI DLFKHQGTIT VNEEGTQATT VTTVGFMPLS TQVRFTVDRP FLFLIYEHRT SCLLFMGRVA NPSRS.
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 :
SERPINI1 HumanDescription:
Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
Product # :
PRO-213Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
- purity
- biological activity
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Description
SERPINI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 394 amino acids and having a total molecular mass of 44.7kDa. SERPINI1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of rat C6 cells which is less than 0.5µg/ml, corresponding to a specific activity of >2000IU/mg.Citations
More Info
-
Introduction
SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).
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Synonyms
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SERPINI1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINI1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized SERPINI1 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
TGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG
STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN
GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL
VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM
MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT
LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF
IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL
YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.
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 :
EEF1A1 HumanDescription:
Eukaryotic Translation Elongation Factor 1 Alpha 1 Human Recombinant
Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.
Product # :
PRO-1910Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EEF1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (1-462 a.a) and having a molecular mass of 50kDa.
Source
Escherichia Coli.
Formulation
EEF1A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.
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Synonyms
Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.
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Physical Appearance
Sterile Filtered clear solution.
-
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
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK ITKSAQKAQK AK
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 :
EFNA3 Human, Sf9Description:
Ephrin A3 Human Recombinant, Sf9
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
Product # :
PRO-2614Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EFNA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (23-214aa) and having a molecular mass of 48.7kDaEFNA3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The Fractalkine solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.
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Synonyms
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
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Physical Appearance
Sterile Filtered colorless solution.
-
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
ADPQGPGGAL GNRHAVYWNS SNQHLRREGY TVQVNVNDYL DIYCPHYNSS GVGPGAGPGP
GGGAEQYVLY MVSRNGYRTC NASQGFKRWE CNRPHAPHSP IKFSEKFQRY SAFSLGYEFH
AGHEYYYIST PTHNLHWKCL RMKVFVCCAS TSHSGEKPVP TLPQFTMGPN VKINVLEDFE
GENPQVPKLE KSISGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV
TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY
KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV
EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH
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.
- View Data Sheet
Name :
CXCL5 HumanDescription:
Epithelial Neutrophil-Activating Protein 78 Human Recombinant (CXCL5)
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
Product # :
CHM-331Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- purity
- biological activity
- More Info
- sds-page
- Citations
Description
Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8020 Dalton. The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL5 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.sds-page
Citations
More Info
-
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, and can be inhibited with the type II IFN. 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
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized ENA78 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.
-
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
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
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Background
What is the molecular weight/Mw of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein has a total Mw of 8.02kDa.
What is the source or expression system of CXCL5 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 HUMAN Protein?
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.
What is the amino acid sequence of CXCL5 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
What applications can CXCL5 HUMAN Protein be used in?
CXCL5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 HUMAN Protein?
The endotoxin level is minimal, CXCL5 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL5 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL5 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
CXCL5 RatDescription:
Epithelial Neutrophil-Activating Protein 78 Rat 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-267Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Epithelial Neutrophil-Activating Protein 78 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 10.0kDa.The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.
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 10.0-100.0 ng/ml.Citations
More Info
-
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.
-
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.
-
Solubility
It is recommended to reconstitute the lyophilized ENA-78 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.
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Background
What is the molecular weight/Mw of CXCL5 RAT Protein?
CXCL5 RAT Protein has a total Mw of 10.0kDa.
What is the source or expression system of CXCL5 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL5 RAT Protein?
CXCL5 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 RAT Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
What is the amino acid sequence of CXCL5 RAT Protein?
APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.
What applications can CXCL5 RAT Protein be used in?
CXCL5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 RAT Protein?
The endotoxin level is minimal, CXCL5 RAT Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL5 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL5 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
Epigen HumanDescription:
Epigen Human Recombinant
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Product # :
CYT-601Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
Epigen Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9 kDa. Epigen is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EPGN was lyophilized from 20mM PBS buffer pH-7.4 .
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.
Citations
More Info
-
Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
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Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epigen although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPGN 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.
-
Solubility
It is recommended to reconstitute the lyophilized Epigen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA
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Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 7.9kDa.
What is the source or expression system of EPIGEN Protein?
Escherichia Coli.
What is the Purity of EPIGEN Protein?
EPIGEN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPIGEN Protein?
Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.
What is the amino acid sequence of EPIGEN Protein?
AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA
What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN 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 :
EPHB4 HumanDescription:
EPH Receptor B4 Human Recombinant
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
Product # :
PRO-2592Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EPHB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (16-539a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 532 amino acids and having a molecular mass of 58.1 kDa. EPHB4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPHB4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
EPHB4 or Ephrin type-B receptor 4 is encoded by the EPHB4 gene in humans. The receptor and its ligands (the ephrins) take part in different developmental stages, mainly in the nervous system. EPHB4 and other Ephrin receptors are the biggest subgroup of the RTK receptors. EPHB4 binds to ephrin B2 and has a crucial part in the development of the vascular system.
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Synonyms
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
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Physical Appearance
Sterile Filtered clear solution.
-
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
LEETLLNTKL ETADLKWVTF PQVDGQWEEL SGLDEEQHSV RTYEVCDVQR APGQAHWLRT GWVPRRGAVH VYATLRFTML ECLSLPRAGRSCKETFTVFY YESDADTATA LTPAWMENPY IKVDTVAAEH LTRKRPGAEA TGKVNVKTLR LGPLSKAGFY LAFQDQGACM ALLSLHLFYK KCAQLTVNLT RFPETVPREL VVPVAGSCVV DAVPAPGPSP SLYCREDGQW AEQPVTGCSC APGFEAAEGN TKCRACAQGT FKPLSGEGSC QPCPANSHSN TIGSAVCQCR VGYFRARTDP RGAPCTTPPS APRSVVSRLN GSSLHLEWSA PLESGGREDL TYALRCRECR PGGSCAPCGG DLTFDPGPRD LVEPWVVVRG LRPDFTYTFE VTALNGVSSL ATGPVPFEPV NVTTDREVPP AVSDIRVTRS SPSSLSLAWA VPRAPSGAVL DYEVKYHEKG AEGPSSVRFL KTSENRAELR GLKRGASYLV QVRARSEAGY GPFGQEHHSQ TQLDESEGWR EQLAVEHHHH HH.
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 :
TBCEL HumanDescription:
Tubulin Folding Cofactor E-Like Human Recombinant
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
Product # :
PRO-030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TBCEL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.
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Synonyms
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
-
Physical Appearance
Sterile filtered colorless solution.
-
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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.
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 :
CALB1 HumanDescription:
Calbindin-1 Human Recombinant
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
Product # :
PRO-721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CALB1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-261 a.a.) and having a molecular mass of 30kDa.The CALB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CALB1 protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 10% glycerol and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Calbindin 1 (CALB1) is a calcium binding protein that is a member of the troponin C superfamily. CALB1 plays a vital role in calcium regulation (including calcium transport and uptake, calcification of bone and teeth) and calcium associated signaling in neurons and transiently in embryological development. CALB1 also has a role in protecting neurons from apoptotic cell death. CALB1 buffers cytosolic calcium and may stimulate a membrane Ca2+-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. The biological function of CALB1 seems to be tied to the redox state of its five cysteine residues.
CALB1 has 4 active calcium-binding domains, and 2 modified domains that seemingly have lost their calcium-binding ability. CALB1 is expressed in neural tissues. In the brain, the CALB1 synthesis is independent of vitamin-D-derived hormones.
Disregulation of the CALB1 is associated with epilepsy, amyotrophic lateral sclerosis, Huntington's disease. The neurons in brains of Huntington disease patients are calbindin-depleted. -
Synonyms
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
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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
MAESHLQSSL ITASQFFEIW LHFDADGSGY LEGKELQNLI QELQQARKKA GLELSPEMKT FVDQYGQRDD GKIGIVELAH VLPTEENFLL LFRCQQLKSC EEFMKTWRKY DTDHSGFIET EELKNFLKDL LEKANKTVDD TKLAEYTDLM LKLFDSNNDG KLELTEMARL LPVQENFLLK FQGIKMCGKE FNKAFELYDQ DGNGYIDENE LDALLKDLCE KNKQDLDINN ITTYKKNIMA LSDGGKLYRT DLALILCAGD N.
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 :
CARD17 HumanDescription:
Caspase Recruitment Domain Family, Member 17 Human Recombinant
CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.
Product # :
PRO-1688Price :
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Description
CARD17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.3 kDa.CARD17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CARD17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Caspase Recruitment Domain Family, Member 17 (CARD17) is a regulator of procaspase-1/CASP1 activation involved in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release throughout inflammation. CARD17 inhibits the release of IL1B in reaction to LPS in monocytes. Though, unlike CASP1, CARD17 do not induce NF-kappa-B activation.
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Synonyms
CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.
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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 MGSMADKVLK EKRKQFIRSV GEGTINGLLG ELLETRVLSQ EEIEIVKCEN ATVMDKARAL LDSVIRKGAP ACQICITYIC EEDSHLAGTL GLSAGPTSGN HLTTQDSQIV LPS.
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 :
FilaminDescription:
Filamin
Product # :
PRO-521Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ultra Pure Filamin having a Molecular mass of 250 kDa.
Source
Chicken Gizzard.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 20mM Tris / acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT, 9M urea and 20mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Filamin is a large (270kd) dimeric actin crosslinking protein from a variety of sources, which helps to stabilize the 3D cortical actin network. The fundamental structure of filamin is well conserved and consists of an actin binding domain at the N-terminus followed by a C-terminal rod domain consisting of numerous repeat segments ranging from 4 in C. elegans to 24 in mammalian cells. Each repeat in the rod domain consists of roughly 100 residues and forms an immunoglobulin like fold. Such immunoglobulin folds have been found in a variety of proteins and are responsible for protein-protein interactions. Filamin Human actin-binding protein (ABP), aka filamin, crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Mammalian filamin interacts directly with at least 30 proteins such as transmembrane receptors, second messenger-associated proteins, protein kinases, phosphatases and cytoskeletal proteins and these interactions have been shown to require one or more of the repeat elements in the rod domain.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Filamin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Filamin 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 Filamin protein at a concentration of 0.5mg/ml in water.
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 :
LCN1 HumanDescription:
Lipocalin-1 Human Recombinant
Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.
Product # :
ENZ-825Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LCN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (19-176 a.a) and having a molecular mass of 20.1kDa. LCN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lipocalin-1 (LCN1) belongs to the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins, which bind to various hydrophobic ligands. LCN1 protein is the principal lipid binding protein in tears and is overproduced in response to numerous stimuli including infection and stress. LCN1 is a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome.
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Synonyms
Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.
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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 MGSHMHHLLA SDEEIQDVSG TWYLKAMTVD REFPEMNLES VTPMTLTTLE GGNLEAKVTM LISGRCQEVK AVLEKTDEPG KYTADGGKHV AYIIRSHVKD HYIFYCEGEL HGKPVRGVKL VGRDPKNNLE ALEDFEKAAG ARGLSTESIL IPRQSETCSP GSD.
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 :
GLK E.coliDescription:
Glucokinase E.coli Recombinant
Glucokinase, Glucose kinase, glk, b2388, JW2385.
Product # :
PKA-059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GLK E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.1kDa. GLK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
GLK protein solution (1.0 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glucokinase also known as GLK is a member of the bacterial glucokinase family. GLK is not highly significant in E.coli since glucoseis already transported into the cell through the PTS system as glucose 6-phosphate.
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Synonyms
Glucokinase, Glucose kinase, glk, b2388, JW2385.
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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 MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL.
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 :
PTGES2 HumanDescription:
Prostaglandin E Synthase 2 Human Recombinant
Prostaglandin E synthase 2, Microsomal prostaglandin E synthase 2, mPGES-2, PTGES2, C9orf15, PGES2, GBF1.
Product # :
ENZ-136Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTGES2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-186 a.a.) and having a molecular mass of 23.5kDa.PTGES2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTGES2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PTGES2 is a membrane-associated prostaglandin E synthase, which catalyzes the conversion of prostaglandin H2 to prostaglandin E2. Additionally, PTGES2 activates the transcription regulated by a gamma-INF-activated transcription element. PTGES2 is widely expressed- in the heart, including apex, inter-ventricular septum, both atria and ventricles, but not in the aorta. PTGES2 is also expressed in fetal heart. PTGES2 is detected in various regions of the brain: cerebellum; occipital, frontal and parietal lobes. It is also expressed in the lymph nodes, skeletal muscle, kidney and trachea, but not in the thymus or lung. PTGES2 is overexpressed in colorectal cancer.
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Synonyms
Prostaglandin E synthase 2, Microsomal prostaglandin E synthase 2, mPGES-2, PTGES2, C9orf15, PGES2, GBF1.
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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 MKAVNEQGKE VTEFGNKYWL MLNEKEAQQV YGGKEARTEE MKWRQWADDW LVHLISPNVY RTPTEALASF DYIVREGKFG AVEGAVAKYM GAAAMYLISK RLKSRHRLQD NVREDLYEAA DKWVAAVGKD RPFMGGQKPN LADLAVYGVL RVMEGLDAFD DLMQHTHIQP WYLRVERAIT EASPAH.
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 :
PTRHD1 HumanDescription:
Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant
C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.
Product # :
ENZ-826Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTRHD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (1-140 a.a) and having a molecular mass of 18.2kDa.PTRHD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTRHD1 protein solution (1mg/ml) containing Phosphate buffer saline (pH 7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Putative peptidyl-tRNA hydrolase PTRHD1 (PTRHD1) is a 140 amino acid protein, which is encoded by a gene located on human chromosome 2p23.3. Chromosome 2 is the second largest human chromosome; it consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. Several genetic diseases are linked to genes on chromosome 2.
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Synonyms
C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.
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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 MGSMHRGVGP AFRVVRKMAA SGAEPQVLVQ YLVLRKDLSQ APFSWPAGAL VAQACHAATA ALHTHRDHPH TAAYLQELGR MRKVVLEAPD ETTLKELAET LQQKNIDHML WLEQPENIAT CIALRPYPKE EVGQYLKKFR LFK.
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 :
GULP1 HumanDescription:
GULP1 Human Recombinant
GULP, Engulfment Adaptor PTB Domain Containing 1, PTB Domain Adapter Protein CED-6, Cell Death Protein 6 Homolog, CED6, GULP, PTB Domain Adaptor Protein CED-6 Engulfment Adapter Protein, Protein GULP, CED-6.
Product # :
PRO-1398Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GULP1 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-304a.a) and having a molecular mass of 36.9kDa.GULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GULP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PTB domain-containing engulfment adapter protein 1 (GULP1) is an evolutionarily conserved adaptor protein essential for efficient phagocytosis of apoptotic cells by phagocytes. Furthermore, GULP1 helps modulate cellular glycosphingolipid and cholesterol transport. In addition, GULP1 may have a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP. Increased cytoplasmic levels of GULP1 are linked with increases in cellular levels of GTP-bound ARF6.
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Synonyms
GULP, Engulfment Adaptor PTB Domain Containing 1, PTB Domain Adapter Protein CED-6, Cell Death Protein 6 Homolog, CED6, GULP, PTB Domain Adaptor Protein CED-6 Engulfment Adapter Protein, Protein GULP, CED-6.
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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 MGSMNRAFSR KKDKTWMHTP EALSKHFIPY NAKFLGSTEV EQPKGTEVVR DAVRKLKFAR HIKKSEGQKI PKVELQISIY GVKILEPKTK EVQHNCQLHR ISFCADDKTD KRIFTFICKD SESNKHLCYV FDSEKCAEEI TLTIGQAFDL AYRKFLESGG KDVETRKQIA GLQKRIQDLE TENMELKNKV QDLENQLRIT QVSAPPAGSM TPKSPSTDIF DMIPFSPISH QSSMPTRNGT QPPPVPSRST EIKRDLFGAE PFDPFNCGAA DFPPDIQSKL DEMQEGFKMG LTLEGTVFCL DPLDSRC.
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.