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1000 results found for “MANF”
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Name :
MCM7 HumanDescription:
Minichromosome Maintenance Complex Component 7 Human Recombinant
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
Product # :
PRO-1847Price :
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Description
MCM7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414) and having a molecular mass of 48.6 kDa. MCM7 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The MCM7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.
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Synonyms
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
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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 MGSMVVATYT CDQCGAETYQ PIQSPTFMPL IMCPSQECQT NRSGGRLYLQ TRGSRFIKFQ EMKMQEHSDQ VPVGNIPRSI TVLVEGENTR IAQPGDHVSV TGIFLPILRT GFRQVVQGLL SETYLEAHRI VKMNKSEDDE SGAGELTREE LRQIAEEDFY EKLAASIAPE IYGHEDVKKA LLLLLVGGVD QSPRGMKIRG NINICLMGDP GVAKSQLLSY IDRLAPRSQY TTGRGSSGVG LTAAVLRDSV SGELTLEGGA LVLADQGVCC IDEFDKMAEA DRTAIHEVME QQTISIAKAG ILTTLNARCS ILAAANPAYG RYNPRRSLEQ NIQLPAALLS RFDLLWLIQD RPDRDNDLRL AQHITYVHQH SRQPPSQFEP LDMKLMRRYI AMCREKQPMV PESLADYITA AYVEMRR
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 :
BTF3L4 HumanDescription:
Basic Transcription Factor 3-Like 4 Human Recombinant
Basic transcription factor 3-like 4, BTF3L4.
Product # :
PRO-1870Price :
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Description
BTF3L4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 11.3kDa. BTF3L4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BTF3L4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
BTF3L4 is a part of the NAC-beta family which contains 1 NAC-A/B (NAC-alpha/beta) domain and required for the initiation of transcription. BTF3L4 binds to polypeptide chains as they emerge from the ribosome and prevents their interaction with the SRP, which usually targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor which forms a stable complex with RNA polymerase II.
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Synonyms
Basic transcription factor 3-like 4, BTF3L4.
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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 MGSMNQEKLA KLQAQVRIGG KGTARRKKKV VHRTATADDK KLQSSLKKLA VNNIAGIEES WTVKHQNQKT LMRKMMMFQI 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.
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Name :
FGFR4 Human, HisDescription:
Fibroblast Growth Factor Receptor-4 Human Recombinant, His Tag
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
Product # :
PKA-090Price :
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Description
Fibroblast Growth Factor Receptor-4 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (22-369a.a.) and having a molecular mass of 39.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).FGFR4 is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FGFR4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.
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Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
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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
LEASEEVELE PCLAPSLEQQ EQELTVALGQ PVRLCCGRAE RGGHWYKEGS RLAPAGRVRG WRGRLEIASF LPEDAGRYLC LARGSMIVLQ NLTLITGDSL TSSNDDEDPK SHRDPSNRHS YPQQAPYWTH PQRMEKKLHA VPAGNTVKFR CPAAGNPTPT IRWLKDGQAF HGENRIGGIR LRHQHWSLVM ESVVPSDRGT YTCLVENAVG SIRYNYLLDV LERSPHRPIL QAGLPANTTA VVGSDVELLC KVYSDAQPHI QWLKHIVING SSFGADGFPY VQVLKTADIN SSEVEVLYLR NVSAEDAGEY TCLAGNSIGL SYQSAWLTVL PEEDPTWTAA APEARYTDLE 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.
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Name :
CNPY4 HumanDescription:
Canopy FGF Signaling Regulator 4 Human Recombinant
PRAT4B, Protein canopy homolog 4, CNPY4.
Product # :
PRO-1976Price :
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Shipped with Ice Packs
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Description
CNPY4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (22-248 a.a) and having a molecular mass of 28.6kDa. CNPY4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques..
Source
Escherichia Coli.
Formulation
CNPY4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 5mM DTT and 2mM EDTA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Canopy FGF Signaling Regulator 4 (CNPY4) is a part of the canopy family which owns one saposin B-type domain. CNPY4 takes part in the regulation process of the cell surface expression of TLR4.
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Synonyms
PRAT4B, Protein canopy homolog 4, CNPY4.
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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 MGSEFGMLKE EDDDTERLPS KCEVCKLLST ELQAELSRTG RSREVLELGQ VLDTGKRKRH VPYSVSETRL EEALENLCER ILDYSVHAER KGSLRYAKGQ SQTMATLKGL VQKGVKVDLG IPLELWDEPS VEVTYLKKQC ETMLEEFEDI VGDWYFHHQE QPLQNFLCEG HVLPAAETAC LQETWTGKEI TDGEEKTEGE EEQEEEEEEE EEEGGDKMTK TGSHPKLDRE DL.
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 :
APIP HumanDescription:
APAF1 interacting protein Human Recombinant
APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.
Product # :
PRO-1186Price :
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Description
APIP Human Recombinant produced E. coli is a single polypeptide chain containing 266 amino acids (1-242) and having a molecular mass of 29.7kDa.APIP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The APIP solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
APIP catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). APIP has an anti-apoptotic function and inhibits muscle ischemic impairment. APIP inhibits the cytochrome c-dependent and APAF1-mediated cell death.
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Synonyms
APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.
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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 MGSHMSGCDA REGDCCSRRC GAQDKEHPRY LIPELCKQFY HLGWVTGTGG GISLKHGDEI YIAPSGVQKE RIQPEDMFVC DINEKDISGP SPSKKLKKSQ CTPLFMNAYT MRGAGAVIHT HSKAAVMATL LFPGREFKIT HQEMIKGIKK CTSGGYYRYD DMLVVPIIEN TPEEKDLKDR MAHAMNEYPD SCAVLVRRHG VYVWGETWEK AKTMCECYDY LFDIAVSMKK VGLDPSQLPV GENGIV
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 Human, Sf9Description:
Sulfatase Modifying Factor 1 Human Recombinant, Sf9
SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1.
Product # :
PRO-2619Price :
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Description
SUMF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 347 amino acids (34-374.a.) and having a molecular mass of 38.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). SUMF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
SUMF1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SUMF1 is a part of the SUMF protein 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. Mutations in this gene will cause multiple sulfatase deficiency meaning a lysosomal storage disorder.
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Synonyms
SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
SQEAGTGAGA GSLAGSCGCG TPQRPGAHGS SAAAHRYSRE ANAPGPVPGE RQLAHSKMVP IPAGVFTMGT DDPQIKQDGE APARRVTIDA FYMDAYEVSN TEFEKFVNST GYLTEAEKFG DSFVFEGMLS EQVKTNIQQA VAAAPWWLPV KGANWRHPEG PDSTILHRPD HPVLHVSWND AVAYCTWAGK RLPTEAEWEY SCRGGLHNRL FPWGNKLQPK GQHYANIWQG EFPVTNTGED GFQGTAPVDA FPPNGYGLYN IVGNAWEWTS DWWTVHHSVE ETLNPKGPPS GKDRVKKGGS YMCHRSYCYR YRCAARSQNT PDSSASNLGF RCAADRLPTM DHHHHHH.
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 :
EGF HumanDescription:
Epidermal Growth Factor Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-217Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor 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
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
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Background
About EGF:
In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).
Description:
Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.
Function:
By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.
Mechanism:
EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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 :
KLF7 HumanDescription:
Kruppel-Like Factor 7 Human Recombinant
UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.
Product # :
PRO-1527Price :
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Description
KLF7 Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-302) and having a molecular mass of 35.8kDa. KLF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLF7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Kruppel-Like Factor 7 (KLF7) is a part of the Kruppel-like transcriptional regulator family whose members regulate cell proliferation, differentiation and survival and contain 3 C2H2 zinc fingers at the C-terminus that mediate binding to GC-rich sites. KLF7 contributes to the progression of type 2 diabetes by inhibiting hormone expression and secretion in pancreatic beta-cells and also by deregulating adipocytokine secretion in adipocytes.
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Synonyms
UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.
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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 MGSMDVLASY SIFQELQLVH DTGYFSALPS LEETWQQTCL ELERYLQTEP RRISETFGED LDCFLHASPP PCIEESFRRL DPLLLPVEAA ICEKSSAVDI LLSRDKLLSE TCLSLQPASS SLDSYTAVNQ AQLNAVTSLT PPSSPELSRH LVKTSQTLSA VDGTVTLKLV AKKAALSSVK VGGVATAAAA VTAAGAVKSG QSDSDQGGLG AEACPENKKR VHRCQFNGCR KVYTKSSHLK AHQRTHTGEK PYKCSWEGCE WRFARSDELT RHYRKHTGAK PFKCNHCDRC FSRSDHLALH MKRHI.
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 :
FGF 1 HumanDescription:
Fibroblast Growth Factor-Acidic Human Recombinant
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Product # :
CYT-264Price :
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Shipping Method :
Shipped at Room temp
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Description
Fibroblast Growth Factor-acidic Human Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15.8kDa.The FGF acidic is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 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, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.More Info
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Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis.
Three alternatively spliced variants encoding different isoforms have been described.
The hep-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors. -
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibroblast Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-a 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 Fibroblast Growth Factor-acidic in sterile 18MΩ-cm H2O at 4 degrees Celsius at a concentration of 0.1mg-0.25mg per 1ml. Allow sample to sit for 5 min. at 4 degrees, spin to remove precipitant.
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Amino Acid Sequence
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
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Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.8kDa.
What is the source or expression system of FGF 1 Protein?
Escherichia Coli.
What is the Purity of FGF 1 Protein?
FGF 1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 1 Protein?
The ED50, calculated by the dose-dependant proliferation of mouse BALB/c 3T3 cells is <0.5 ng/ml, corresponding to a specific activity of > 2,000,000IU/mg.
What is the amino acid sequence of FGF 1 Protein?
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 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 :
SDF 1a HumanDescription:
Stromal Cell-Derived Factor-1 Alpha Human Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
Product # :
CHM-262Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Stromal Cell-Derived Factor-1 alpha Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 8004 Dalton. The SDF-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.
Purity
Greater than 98.0% 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 T cells activated with PHA and IL-2 using a concentation of 20-80 ng/ml corresponding to a Specific Activity of 12,500-50,000IU/mg.More Info
-
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, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SDF-1a 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.
-
Solubility
It is recommended to reconstitute the lyophilized Stromal Cell-Derived Factor-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK
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 :
MBL2 HumanDescription:
Mannose-Binding Lectin 2 Human Recombinant
COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.
Product # :
PRO-1285Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
MBL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (108-248) and having a molecular mass of 18 kDa. MBL2 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MBL2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M Nacl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Mannose-binding protein C (MBL2),belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.
-
Synonyms
COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAASERKA LQTEMARIKK WLTFSLGKQV GNKFFLTNGE IMTFEKVKAL CVKFQASVAT PRNAAENGAI QNLIKEEAFL GITDEKTEGQ FVDLTGNRLT YTNWNEGEPN NAGSDEDCVL LLKNGQWNDV PCSTSHLAVC EFPI.
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 :
IGF1 E3R HumanDescription:
Insulin Like Growth Factor-1, Mutant E3R Human Recombinant
Insulin-Like Growth Factor-1.
Product # :
CYT-1217Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
- More Info
Description
IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Synonyms
Insulin-Like Growth Factor-1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
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.
-
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. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.
-
Background
Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.
The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.
The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.
The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.
By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related diseases.
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 :
PI3 Human, Sf9Description:
Peptidase Inhibitor 3 Human Recombinant, Sf9
Elafin, ESI, SKALP, WAP3, WFDC14.
Product # :
PRO-2653Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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- More Info
Description
PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The PI3 solution (0.2mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.
-
Synonyms
Elafin, ESI, SKALP, WAP3, WFDC14.
-
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.
-
Amino Acid Sequence
AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH 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 :
FGF 1 Human, Sf9Description:
Fibroblast Growth Factor-Acidic Human Recombinant, Sf9
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Product # :
CYT-364Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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- purity
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- More Info
Description
Fibroblast Growth Factor-1 Human Recombinant (FGF-1) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of 15803 Dalton. The FGF-a is purified by proprietary chromatographic techniques.
Source
Baculovirus.
Formulation
The sterile protein solution (1.8mg/ml) contains 20mM Tris HCl pH=7.9, 100mM KCl, 0.2mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <10 ng/ml, corresponding to a specific activity of 100,000IU/mg.More Info
-
Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
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Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
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Physical Appearance
Sterile Filtered liquid formulation.
-
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.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids as determined and was found to be Met-Phe-Asn-Leu-Pro.
-
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.8kDa.
What is the source or expression system of FGF 1 Protein?
Baculovirus.
What is the Purity of FGF 1 Protein?
FGF 1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 1 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <10 ng/ml, corresponding to a specific activity of 100,000IU/mg.
What is the amino acid sequence of FGF 1 Protein?
FGF 1 Protein is composed from 140 amino acids.
What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 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 :
TNFRSF17 Human, Sf9Description:
B-Cell Maturation Antigen, Sf9 Human Recombinant
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen
Product # :
CYT-1148Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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- purity
- More Info
Description
TNFRSF17 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 296 amino acids (1-54 aa) and having a molecular mass of 33.1Da.TNFRSF17 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF17 protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
B-Cell Maturation Antigen or TNFRSF17 or tumor necrosis factor receptor superfamily member 17, is part of the TNF receptor protein family. This protein is a TNFSF13B/BLyS/BAFF, TNFSF13/APRIL & promotes B-cell survival receptor. TNFRSF17 has a crucial part in the humoral immunity regulation. This protein is responsible for the activation of NF-kappa-B & JNK.
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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 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.
-
Amino Acid Sequence
ADPMLQMAGQ CSQNEYFDSL LHACIPCQLR CSSNTPPLTC QRYCNASVTN SVKGTNALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 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 :
GDF3 HumanDescription:
Growth Differentiation Factor-3 Human Recombinant
Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.
Product # :
CYT-694Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.
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Synonyms
Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 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 GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.
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Background
What is the molecular weight/Mw of GDF3 HUMAN Protein?
GDF3 HUMAN Protein has a total Mw of 14.15XkDa.
What is the source or expression system of GDF3 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF3 HUMAN Protein?
GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF3 HUMAN Protein?
The biological functionality of GDF3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF3 HUMAN Protein?
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.
What applications can GDF3 HUMAN Protein be used in?
GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF3 HUMAN Protein?
The endotoxin level is minimal, GDF3 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 :
ARF1 HumanDescription:
ADP-Ribosylation Factor 1 Human Recombinant
ARF-1, ADP-ribosylation factor 1.
Product # :
PRO-867Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
- purity
- More Info
Description
ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.
-
Synonyms
ARF-1, ADP-ribosylation factor 1.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K.
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 :
LR3 IGF1 HumanDescription:
LR3 Insulin Like Growth Factor-1 Human Recombinant
R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.
Product # :
CYT-022Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
- sds-page
Description
The LR3 is a long-term analog of human IGF-1, specifically designed and manufactured for mammalian cell culture to support large-scale manufacturing of recombinant biopharmaceuticals. Recombinant Human LR3 Insulin Like Growth Factor-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9.1kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.2.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the stimulation of protein synthesis in L6 myoblasts is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.sds-page
More Info
-
Introduction
IGF-1 (Insulin-like growth factor-1) is a major hormonal mediator of statural growth. Under regular circumstances, GH (growth hormone) binds to its receptor in the liver, and other tissues, and stimulates the synthesis/secretion of IGF-1. In target tissues, the Type 1 IGF receptor, that is homologous to the insulin receptor, is activated by IGF-1, leading to intracellular signaling which stimulates multiple processes leading to statural growth. IGF-1 metabolic actions are partly directed at stimulating the uptake of glucose, fatty acids, and amino acids so that metabolism supports growing tissues.
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Synonyms
R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized LR3 IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution the LR3 IGF1 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 LR3 IGF1 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIV DECCFRSCDLRRLEMYCAPLKPAKSA.
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 :
CD116 HumanDescription:
GM-CSF Receptor Alpha Human Recombinant
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.
Product # :
CYT-796Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
- sds-page
Description
CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSF2RA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
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Synonyms
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.
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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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Background
Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.
Therapeutic Applications:
Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.
Challenges and Future Directions:
While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 37.2kDa.
What is the source or expression system of CD116 Protein?
Escherichia Coli.
What is the Purity of CD116 Protein?
CD116 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CD116 Protein?
The biological functionality of CD116 Protein will be determined in the future.
What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 324 amino acids.
What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 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 :
MAGOH HumanDescription:
Mago-Nashi Homolog Human Recombinant
MAGOH1, MAGOHA, Protein mago nashi homolog, MAGOH, proliferation-associated (Drosophila).
Product # :
PRO-810Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
MAGOH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids (1-146 a.a.) and having a molecular mass of 18.2 kDa. MAGOH protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
MAGOH Human solution containing 20mM Tris-HCl pH-8, 2mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Drosophila that have mutations in their MAGOH gene produce progeny with defects in germplasm assembly and germline development. MAGOH, the human homolog of Drosophila mago nashi, is necessary for embryo development. In mammals, mRNA expression is not limited to the germ plasm, but is expressed ubiquitously in adult tissues and is induced by serum stimulation of quiescent fibroblast.
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Synonyms
MAGOH1, MAGOHA, Protein mago nashi homolog, MAGOH, proliferation-associated (Drosophila).
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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
MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA YVHKSVMEEL KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT TSKIGSLIDV NQSKDPEGLR VFYYLVQDLK CLVFSLIGLH FKIKPILEHH 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 :
MTHFS HumanDescription:
5,10-Methenyltetrahydrofolate Synthetase Human Recombinant
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
Product # :
ENZ-096Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MTHFS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203a.a.) and having a molecular mass of 25.4 kDa. MTHFS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHFS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).
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Synonyms
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAAVSSAK RSLRGELKQR LRAMSAEERL RQSRVLSQKV IAHSEYQKSK RISIFLSMQD EIETEEIIKD IFQRGKICFI PRYRFQSNHM DMVRIESPEE ISLLPKTSWN IPQPGEGDVR EEALSTGGLD LIFMPGLGFD KHGNRLGRGK GYYDAYLKRC LQHQEVKPYT LALAFKEQIC LQVPVNENDM KVDEVLYEDS STA
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 :
HMGB1 Human, Sf9Description:
High-Mobility Group Box 1 Human Recombinant, Sf9
HMG1, HMG3, SBP-1, Amphoterin, HMGB1, High-Mobility Group Box 1.
Product # :
PRO-610Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
HMG1 Human Recombinant fused to an 8 aa His-Tag at C-terminus produced in baculovirus insect cells is a single, glycosylated, polypeptide chain (amino acids 1-215) containing 223 amino acids and having a molecular mass of 25kDa. The HMGB1 is purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
The HMG1 solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM EDTA, 0.5mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
HMGB1 is an abundant chromatin-binding protein found in eukaryotic cell nucleus and acts in the assembly of nucleoprotein complexes. Inside the cell, HMGB1 binds to DNA and is involved in transcriptional regulation. Outside the cell, HMGB1 acts as a cytokine with activities that resemble those of tumor necrosis factor (TNF). HMGB1 is elevated significantly in chronic kidney disease patients and correlates with glomerular filtration rate as well as with markers of inflammation and malnutrition. HMGB1 is involved in Gram-negative sepsis by catalyzing movement of LPS monomers from LPS aggregates to CD14 to initiate a TLR4-mediated proinflammatory response. HMGB1 plays an important role in the relationship between necrosis and malignancy in glioma tumours. HMG1 protein is induced by Mycobacterium bovis BCG. Overexpression of HMGB1 is common in gastrointestinal stromal tumors and is related to the KIT mutation. HMG1 induces growth inhibition and apoptosis in macrophages through RAGE intracellular signaling pathway. The increase of extracellular HMGB1 observed in salivary glands of Sjogren's syndrome patients indicates that HMGB-1 is involved in the inflammatory process of the disease. HMGB-1 together with estrogen increase cell cycle progression in tumor cell lines.
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Synonyms
HMG1, HMG3, SBP-1, Amphoterin, HMGB1, High-Mobility Group Box 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK SKKKKEEEED EEDEEDEEEE EDEEDEDEEE DDDDELEHHH HHH.
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 :
PEDF Human, HisDescription:
Pigment Epithelium-Derived Factor Human Recombinant, His Tag
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Product # :
CYT-552Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PEDF Human Recombinant produced in E.Coli containing a natural variant M72T is a single, non-glycosylated, polypeptide chain containing 420 amino acids (20-418 a.a.) and having a total molecular mass of 46.7 kDa. PEDF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PEDF solution contains 20mM Tris-HCl buffer(pH 8.0), 0.1M NaCl , and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties. -
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
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 :
GDF5 HumanDescription:
Growth Differentiation Factor-5 Human Recombinant
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
Product # :
CYT-442Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Growth Differentiation Factor 5 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 120 amino acids and having a total molecular mass of 27.4kDa. To enable bacterial expression the N-terminal sequence of Ala-Pro-Leu-Thr was replaced with a Lys.GDF5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without any additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.More Info
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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
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Synonyms
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Differentiation Factor 5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Differentiation Factor-5 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 Growth Differentiation Factor-5 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
APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
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Background
What is the molecular weight/Mw of GDF5 HUMAN Protein?
GDF5 HUMAN Protein has a total Mw of 27.4kDa.
What is the source or expression system of GDF5 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF5 HUMAN Protein?
GDF5 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF5 HUMAN Protein?
GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.
What is the amino acid sequence of GDF5 HUMAN Protein?
APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
What applications can GDF5 HUMAN Protein be used in?
GDF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF5 HUMAN Protein?
The endotoxin level is minimal, GDF5 HUMAN Protein was purified using conventional chromatography techniques.
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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 1.15 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 by RP-HPLC, using a standard solution of GDF5 as a Reference Standard.
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.