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1000 results found for “EGF”
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Name :
ENTPD6 HumanDescription:
Ectonucleoside Triphosphate Diphosphohydrolase 6 Recombinant
ectonucleoside triphosphate diphosphohydrolase 6 isoform 1, CD39L2, dJ738P15.3, IL-6SAG, IL6ST2, NTPDase-6.
Product # :
PRO-2629Price :
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Description
ENTPD6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447amino acids (61-484a.a.) and having a molecular mass of 48.7kDa. ENTPD6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ENTPD6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 6 or ENTPD6 is an enzyme, akin to E-type nucleotidases. E-type nucleotidases, for instance CD39, are responsible for extracellular nucleotides catabolism. ENTPD6 has four apyrase-conserved areas like all to E-type nucleotidases. Rather spliced transcript agents that codes various isoforms were discovered for the DNA segment.
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Synonyms
ectonucleoside triphosphate diphosphohydrolase 6 isoform 1, CD39L2, dJ738P15.3, IL-6SAG, IL6ST2, NTPDase-6.
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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 MGSKWHRATA TQAFFSITRA APGARWGQQA HSPLGTAADG HEVFYGIMFD AGSTGTRVHV FQFTRPPRET PTLTHETFKA LKPGLSAYAD DVEKSAQGIR ELLDVAKQDI PFDFWKATPL VLKATAGLRL LPGEKAQKLL QKVKEVFKAS PFLVGDDCVS IMNGTDEGVS AWITINFLTG SLKTPGGSSV GMLDLGGGST QIAFLPRVEG TLQASPPGYL TALRMFNRTY KLYSYSYLGL GLMSARLAIL GGVEGQPAKD GKELVSPCLS PSFKGEWEHA EVTYRVSGQK AAASLHELCA ARVSEVLQNR VHRTEEVKHV DFYAFSYYYD LAAGVGLIDA EKGGSLVVGD FEIAAKYVCR TLETQPQSSP FSCMDLTYVS LLLQEFGFPR SKVLKLTRKI DNVETSWALG AIFHYIDSLN RQKSPAS
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 :
MREG HumanDescription:
Melanoregulin Human Recombinant
Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.
Product # :
PRO-1885Price :
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Description
MREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 27.3kDa.MREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Melanoregulin (MREG) takes part in membrane fusion and in regulating the biogenesis of disk membranes of photoreceptor rods. MREG is expressed in photoreceptor cells as two isoforms as a result of alternative splicing. MREG interacts with Peripherin-2, a photoreceptor specific tetraspanin protein which is required to preserve normal cell structure during the renewal process of membrane fusion. Moreover, MREG plays a part in the incorporation of pigments into hair.
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Synonyms
Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGLRDWL RTVCCCCGCE CLEERALPEK EPLVSDNNPY SSFGATLVRD DEKNLWSMPH DVSHTEADDD RTLYNLIVIR NQQAKDSEEW QKLNYDIHTL RQVRREVRNR WKCILEDLGF QKEADSLLSV TKLSTISDSK NTRKAREMLL KLAEETNIFP TSWELSERYL FVVDRLIALD AAEEFFKLAR RTYPKKPGVP CLADGQKELH YLPFPSP
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 :
SUMF1 HumanDescription:
Sulfatase Modifying Factor 1 Human Recombinant
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
Product # :
PRO-986Price :
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Description
SUMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (91-374 a.a.) and having a molecular mass of 34.1kDa.SUMF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SUMF1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2M UREA, 2mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SUMF1 is a member of the SUMF family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Alterations in this gene result in multiple sulfatase deficiency which is a lysosomal storage disorder.
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Synonyms
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
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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 MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE TSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS QNTPDSSASN LGFRCAADRL PTMD
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 :
EXOSC10 HumanDescription:
Exosome Component 10 Human Recombinant
Exosome component 10, Polymyositis/scleroderma autoantigen 2, Autoantigen PM/Scl 2, Polymyositis/scleroderma autoantigen 100 kDa, PM/Scl-100, P100 polymyositis-scleroderma overlap syndrome-associated autoantigen, EXOSC10, PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl.
Product # :
PRO-444Price :
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Shipped with Ice Packs
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Description
EXOSC10 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 102 kDa. EXOSC10 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
EXOSC10 is supplied in 20mM HEPES, pH-7.5, 100mM NaCl, 0.01mM EDTA, 0.02% SDS.
Purity
Greater than 93% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EXOSC10 is a nucleolar protein and represents one crucial component of the so-called "PM/Scl complex" or "nuclear exosome", which is an RNA-processing complex consisting of a number of exoribonucleases (not to be confused with certain multivesicular bodies which are shed by cultured cells into the culture fluid and are also called exosomes).
Autoantibodies against EXOSC10 occur in patients suffering from polymyositis, scleroderma or polymyositis/scleroderma overlap syndromes. While antibodies to other components of the exosome complex (PM/Scl 75, several Rrp proteins) can be found in some sera, practically all patients with autoantibodies against the PM/Scl complex are positive for EXOSC10 antibodies, making this specificity an important marker. The presence of EXOSC10 autoantibodies is a comparatively "good" prognostic sign in polymyositis/scleroderma overlap syndrome unlike the poor prognosis seen when other myositis and systemic sclerosis specific autoantibodies are present. -
Synonyms
Exosome component 10, Polymyositis/scleroderma autoantigen 2, Autoantigen PM/Scl 2, Polymyositis/scleroderma autoantigen 100 kDa, PM/Scl-100, P100 polymyositis-scleroderma overlap syndrome-associated autoantigen, EXOSC10, PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels).
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coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.
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Applications
Western-Blot with monoclonal anti-hexa-His-tag antibody & polymyositis patient sera.
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 :
FSTL1 Human, HEKDescription:
Follistatin Like 1 Human Recombinant, HEK
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.
Product # :
CYT-1027Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FSTL1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-308) containing 296 amino acids including a 8 a.a C-terminal His tag. The total molecular mass is 33.8kDa (calculated).
Source
HEK293 cells.
Formulation
FSTL1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FSTL1 protein resembles follistatin, an activin-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
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Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.
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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 one week 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. FSTL1 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
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.
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Background
What is the molecular weight/Mw of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein has a total Mw of 33.8kDa.
What is the source or expression system of FSTL1 HUMAN, HEK Protein?
HEK293 cells.
What is the Purity of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FSTL1 HUMAN, HEK Protein?
The biological functionality of FSTL1 HUMAN, HEK Protein will be determined in the future.
What is the amino acid sequence of FSTL1 HUMAN, HEK Protein?
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.
What applications can FSTL1 HUMAN, HEK Protein be used in?
FSTL1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FSTL1 HUMAN, HEK Protein?
The endotoxin level is minimal, FSTL1 HUMAN, HEK 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 :
LGALS8 HumanDescription:
Galectin-8 Human Recombinant
Galectin-8, Gal-8, Po66 carbohydrate-binding protein, Po66-CBP, Prostate carcinoma tumor antigen 1, PCTA-1, LGALS8.
Product # :
CYT-017Price :
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Shipped at Room temp
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Description
Galectin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 317 amino acids and having a molecular mass of 35.8kDa.The LGALS8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LGALS8 was lyophilized from a concentrated (1mg/ml) solution in 20mM PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of Galectin-8 as determined by its ability to agglutinate human red blood cells is 0.8~4 µg/ml.Citations
More Info
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Introduction
Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Galectin-8 is a tandem-repeat-type member of the galectin family, consisting of 2 CRDs attached by a linker peptide. Galectin-8 is greatly expressed in lung carcinomas, a number of forms of prostate carcinomas, in addition to other tumor cells. Galectin-8 attaches to a subset of cell surface integrins to modulate ECM-integrin interactions. Once immobilized, Galectin-8 promotes cell adhesion by ligation and clustering of cell surface integrin receptors. On the other hand, as a soluble ligand, Galectin-8 can inhibit cell adhesion.
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Synonyms
Galectin-8, Gal-8, Po66 carbohydrate-binding protein, Po66-CBP, Prostate carcinoma tumor antigen 1, PCTA-1, LGALS8.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LGALS8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-8 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 Galectin-8 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Met-Leu-Ser-Leu.
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Background
What is the molecular weight/Mw of LGALS8 HUMAN Protein?
LGALS8 HUMAN Protein has a total Mw of 35.8kDa.
What is the source or expression system of LGALS8 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS8 HUMAN Protein?
LGALS8 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS8 HUMAN Protein?
The ED50 of Galectin-8 as determined by its ability to agglutinate human red blood cells is 0.8~4 µg/ml.
What is the amino acid sequence of LGALS8 HUMAN Protein?
LGALS8 HUMAN Protein is composed from 317 amino acids.
What applications can LGALS8 HUMAN Protein be used in?
LGALS8 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS8 HUMAN Protein?
The endotoxin level is minimal, LGALS8 HUMAN 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 :
CHGA Human, HisDescription:
Chromogranin-A Human Recombinant, His Tag
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-699Price :
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 80.0% as determined by Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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 MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.
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 :
EBV p18Description:
Epstein-Barr Virus (HHV-4) p18 Recombinant
Product # :
EBV-273Price :
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Description
The E.Coli derived recombinant mosaic protein contains the HHV-4 p18 regions, 1-119 amino acids and fused to a GST-Tag at C-terminus.
Formulation
Containing 25mM Tris-HCl pH 8.0, 1.5M urea and 50% glycerol.
Purity
EBV-p18 protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virusof the herpes family(which includes Herpes simplex virusand Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expressionwhich can be broadly categorized as being lytic cycle or latent cycle. The lytic cycleor productive infection results in staged expression of a host of viral proteinswith the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cellas EBV virions are produced by budding from the infected cell. The latent cycle(lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen(EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins(LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs(EBERs).
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Stability
EBV p18 M although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
EBV-p18 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HHV-4 (EBV) with minimal specificity problems.
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Specificity
Immunoreactive with sera of EBV-infected individuals.
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Purification Method
EBV-p18 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.
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Name :
LysostaphinDescription:
Lysostaphin Recombinant
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
Product # :
ENZ-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without any additives.
Purity
98% as determined by RP-HPLC.
Biological Activity
Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C. Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.
Citations
More Info
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Introduction
Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.
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Synonyms
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.
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Protein content
Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.
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Specific Activity
Determined to be 3,540 units/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.
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Name :
MIA2 HumanDescription:
Melanoma Inhibitory Activity 2 Human Recombinant
MIA-2, MIA2, Melanoma Inhibitory Activity 2, FLJ22404.
Product # :
CYT-638Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MIA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain consisting of 101 amino having a total molecular mass of 11.5 kDa.The MIA2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MIA2 protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Phosphate buffer pH=7.4 and 150mM NaCl.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
MIA2 performs as a tumour suppressor in hepatocellular carcinoma. MIA2is a novel acute phase protein which its expression is found in the liver and reacts to liver damage in chronic liver diseases and is considerably higher in severe fibrosis patients . MIA2 is induced by IL6, TGF-B & and conditioned medium from activated hepatic stellate cells. MIA2 is is mainly expressed in hepatocytes.
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Synonyms
MIA-2, MIA2, Melanoma Inhibitory Activity 2, FLJ22404.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIA2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIA2 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 MIA2 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
MLESTKLLAD LKKCGDLECE ALINRVSAMR DYRGPDCRYL NFTKGEEISV YVKLAGERED LWAGSKGKEF GYFPRDAVQI EEVFISEEIQ MSTKESDFLC L.
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 :
TNFRSF17 Human, HisDescription:
B-Cell Maturation Antigen Human Recombinant, His Tag
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
Product # :
CYT-190Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (78-184 a.a) and having a molecular mass of 14.1kDa.TNFRSF17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFRSF17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.
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Synonyms
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
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Physical Appearance
Sterile Filtered colorless liquid.
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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 MGSRKINSEP LKDEFKNTGS GLLGMANIDL EKSRTGDEII LPRGLEYTVE ECTCEDCIKS KPKVDSDHCF PLPAMEEGAT ILVTTKTNDY CKSLPAALSA TEIEKSISAR.
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 :
TNFSF7 HumanDescription:
CD70 Human Recombinant
CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.
Product # :
CYT-880Price :
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Description
TNFSF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (39-193 a.a) and having a molecular mass of 19.5kDa. TNFSF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFSF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CD70 also known as TNFSF7 is a cytokine which binds to CD27. TNFSF7 takes part in T-cell activation as well as induces the proliferation of costimulated T-cells. Moreover, TNFSF7 enhances the generation of cytolytic T-cells. Among the diseases which are associated with TNFSF7: Include acute myocarditis & Myocarditis.
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Synonyms
CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.
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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
MGSSHHHHHH SSGLVPRGSH MGSQRFAQAQ QQLPLESLGW DVAELQLNHT GPQQDPRLYW QGGPALGRSF LHGPELDKGQ LRIHRDGIYM VHIQVTLAIC SSTTASRHHP TTLAVGICSP ASRSISLLRL SFHQGCTIAS QRLTPLARGD TLCTNLTGTL LPSRNTDETF FGVQWVRP.
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 :
MAX HumanDescription:
MYC Associated Factor X Human Recombinant
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
Product # :
PRO-811Price :
Quantity :
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Shipped with Ice Packs
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Description
MAX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
MAX Human solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
MAX protein is part of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. MAX forms homodimers and heterodimers with Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms offers a complex system of transcriptional regulation. In contrast to Myc, which is exceedingly regulated throughout progression during the cell cycle, Max is very stable and is much more abundant than Myc.
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Synonyms
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
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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
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH.
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 :
TRAIL HumanDescription:
TRAIL / APO2 Ligand Human Recombinant
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Product # :
CYT-443Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED50 for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.Citations
More Info
-
Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. -
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL 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
MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.
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 :
CST3 Mouse, ActiveDescription:
Cystatin-C Mouse Recombinant, Active
Cystatin-C, Cystatin-3, Cst3, CST3
Product # :
PRO-2433Price :
Quantity :
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Shipped with Ice Packs
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Description
CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25°C.
Citations
More Info
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Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
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Synonyms
Cystatin-C, Cystatin-3, Cst3, CST3
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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
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA HHHHHH
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 :
TNFRSF14 MouseDescription:
HVEM Mouse Recombinant
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
Product # :
CYT-1145Price :
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Description
TNFRSF14 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 407 amino acids (39-206 aa) and having a molecular mass of 45.3kDa.TNFRSF14 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The TNFRSF14 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Herpesvirus entry mediator or HVEM or tumour necrosis factor receptor superfamily member 14 or TNFRSF14, is part of the TNF receptors family that is a receptor located on the cell surface. The cytoplasmic area of this receptor can bind all sorts of TNF receptor associated factor (TRAF) protein. Those proteins can mediate pathways activating an immune response. The MITF is regulating TNFRSF14 gene expression.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
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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
QPSCRQEEFL VGDECCPMCN PGYHVKQVCS EHTGTVCAPC PPQTYTAHAN GLSKCLPCGV
CDPDMGLLTW QECSSWKDTV CRCIPGYFCE NQDGSHCSTC LQHTTCPPGQ RVEKRGTHDQ
DTVCADCLTG TFSLGGTQEE CLPWTNCSAF QQEVRRGTNS TDTTCSSQLE PKSCDKTHTC
PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN
AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP
QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL
YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH
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 :
TNFSF8 Human, Sf9Description:
CD30 Ligand Human Recombinant, Sf9
Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.
Product # :
CYT-954Price :
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Description
TNFSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 181 amino acids (63-234a.a.) and having a molecular mass of 20.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). TNFSF8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
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Synonyms
Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.
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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
ADPQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSDHHHHH H.
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 :
Zika EctodomainDescription:
Zika Ectodomain Recombinant
Product # :
ZKV-006Price :
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Description
Recombinant Zika Ectodomain is a glycosylated protein, produced using baculovirus vectors in insect cells and its Mw is approximately 45kDa.The Zika Ectodomain is a recombinant protein of the ectodomain of the envelope protein from the Suriname Zika virus strain.
Source
Baculovirus Insect Cells.
Formulation
The Zika Ectodomain solution 10mM Sodium phosphate, pH 7.2, 150mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Zika virus (ZIKV) belongs to the family Flaviviridae and the genus Flavivirus, it is transmitted by daytime-active Aedes mosquitoes, such as A. aegypti and A. albopictus. The Zika virus is related to the dengue, yellow fever, Japanese encephalitis, and West Nile viruses. Much like the other flaviviruses, Zika virus is enveloped and icosahedral and has a nonsegmented, single-stranded, positive-sense RNA genome. Zika fever is an infection, which often causes no symptoms or only mild ones, like a mild form of dengue fever, and it is treated by rest. As of February 2016, there has been mounting evidence that Zika fever in pregnant women can cause abnormal brain development in their fetuses by mother-to-child transmission, which may result in miscarriage or microcephaly, however it is not yet known whether Zika virus causes microcephaly. Furthermore, a connection has been established with neurologic conditions in infected adults, including Guillain–Barre syndrome.
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Physical Appearance
Sterile Filtered solution.
-
Stability
Zika Ectodomain should be stored at 4°C. Do not freeze!
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 :
BMP 2 Human, HEKDescription:
Bone Morphogenetic protein-2 Human Recombinant, HEK
BMP-2, BMP2A.
Product # :
CYT-080Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BMP-2 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 28kDa due to glycosylation. The BMP2 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The BMP2 was lyophilized from 0.67mg/ml in 2xPBS + 6% ethanol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.
Citations
More Info
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Introduction
BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
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Synonyms
BMP-2, BMP2A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-2 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 BMP-2 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.
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Amino Acid Sequence
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.
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Background
What is the molecular weight/Mw of BMP2 Protein?
BMP2 Protein has a total Mw of 28kDa.
What is the source or expression system of BMP2 Protein?
Hek.
What is the Purity of BMP2 Protein?
BMP2 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP2 Protein?
The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.
What is the amino acid sequence of BMP2 Protein?
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.
What applications can BMP2 Protein be used in?
BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP2 Protein?
The endotoxin level is minimal, BMP2 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 :
LGALS14 HumanDescription:
Galectin-14 Human Recombinant
Placental protein 13-like, Charcot-Leyden crystal protein 2, CLC2, Galectin-14, Gal-14, LGALS14, PPL13, MGC22235.
Product # :
CYT-003Price :
Quantity :
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Shipped with Ice Packs
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Description
LGALS14 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids (1-139 a.a.) and having a molecular mass of 18.5kDa. The LGALS14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS14 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Galectin14, aka LGALS14, is a member of the galectin family of carbohydrate binding proteins. Galectin family members contain one or two carbohydrate recognition domains, which can bind beta-galactoside. The LGALS14 gene is predominantly expressed in the placenta. LGALS14 is expressed intracellularly in the placenta and eosinophils and is released by eosinophils following allergen stimulation. LGALS14 may be involved in the development of allergic inflammation.
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Synonyms
Placental protein 13-like, Charcot-Leyden crystal protein 2, CLC2, Galectin-14, Gal-14, LGALS14, PPL13, MGC22235.
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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 MGSMSSLPVP YTLPVSLPVG SCVIITGTPI LTFVKDPQLE VNFYTGMDED SDIAFQFRLH FGHPAIMNSR VFGIWRYEEK CYYLPFEDGK PFELCIYVRH KEYKVMVNGQ RIYNFAHRFP PASVKMLQVL RDISLTRVLI SD.
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Background
What is the molecular weight/Mw of LGALS14 HUMAN Protein?
LGALS14 HUMAN Protein has a total Mw of 18.5kDa.
What is the source or expression system of LGALS14 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS14 HUMAN Protein?
LGALS14 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS14 HUMAN Protein?
The biological functionality of LGALS14 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS14 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSSLPVP YTLPVSLPVG SCVIITGTPI LTFVKDPQLE VNFYTGMDED SDIAFQFRLH FGHPAIMNSR VFGIWRYEEK CYYLPFEDGK PFELCIYVRH KEYKVMVNGQ RIYNFAHRFP PASVKMLQVL RDISLTRVLI SD.
What applications can LGALS14 HUMAN Protein be used in?
LGALS14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS14 HUMAN Protein?
The endotoxin level is minimal, LGALS14 HUMAN 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 :
NT 3 MouseDescription:
Neurotrophin-3 Mouse Recombinant
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.
Product # :
CYT-688Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Neurotrophin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids and having a molecular mass of 13.6kDa. The NT-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.02% TFA.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity, as determined by the dose-dependent proliferation of BaF3 cells transfected with the TrkB receptor, is typically in the range of 1-10 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.
Citations
More Info
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Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
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Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 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
YAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
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 :
Prolactin Human, PEGDescription:
Prolactin Pegylated Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1063Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Prolactin Human Recombinant Pegylated produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids + an additional Ala at n-terminal. Pegylated Prolactin is mono-pegylated having a molecular mass of ~ 39 kDa, however under non-denaturing conditions it behaves as 220 kDa protein due to its increased hydrodynamic volume. The Pegylated Prolactin protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Human Prolactin was tested for its biological functionality in-vitro by inducing proliferation of Nb2 cells or Baf/3 cells that were stably transfected with Human Prolactin receptors, though its activity is lower than human Prolactin. However, it is anticipated that its biological activity in vivo will be higher than human Prolactin due to prolonged persistence in circulation.
Citations
More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Prolactin is secreted when eating, nursing, mating, estrogen treatment and during ovulation. Prolactin's primary role is to promote and maintain lactation but also plays a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin in sterile 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
ATG3 HumanDescription:
Autophagy Related 3 Human Recombinant
APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.
Product # :
PRO-1987Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
ATG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a) and having a molecular mass of 38.3kDa. ATG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATG3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.
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Synonyms
APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.
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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 MGSMQNVINT VKGKALEVAE YLTPVLKESK FKETGVITPE EFVAAGDHLV HHCPTWQWAT GEELKVKAYL PTGKQFLVTK NVPCYKRCKQ MEYSDELEAI IEEDDGDGGW VDTYHNTGIT GITEAVKEIT LENKDNIRLQ DCSALCEEEE DEDEGEAADM EEYEESGLLE TDEATLDTRK IVEACKAKTD AGGEDAILQT RTYDLYITYD KYYQTPRLWL FGYDEQRQPL TVEHMYEDIS QDHVKKTVTI ENHPHLPPPP MCSVHPCRHA EVMKKIIETV AEGGGELGVH MYLLIFLKFV QAVIPTIEYD YTRHFTM.
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 :
BATF HumanDescription:
Basic Leucine Zipper Transcription Factor Human Recombinant
Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.
Product # :
PRO-119Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
BATF Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids (1-125 a.a.) and having a molecular mass of 16.2kDa. The BATF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BATF solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl and 40% glycerol.
Purity
BATF purity was found to be greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
BATF is a nuclear basic leucine zipper protein which is a member of the AP-1/ATF superfamily of transcription factors. BATF is intensely expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I. BATF acts as a tissue-specific modulator of the AP-1 transcription complex in human cells. Furthermore, BATF connects with IFP35 which is a leucine zipper protein that translocates to the nucleus following IFN treatment.
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Synonyms
Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.
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Physical Appearance
BATF is supplied as a 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 MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS PRFQP.
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.