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1000 results found for “Placental Lactogen”
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Name :
PCMT1 HumanDescription:
Protein-L-Isoaspartate O-Methyltransferase Human Recombinant
EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.
Product # :
ENZ-522Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PCMT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-227 a.a.) and having a molecular mass of 28.8 kDa. The PCMT1 is fused to a 36 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PCMT1 Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PCMT1 enzyme catalyses the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. PCMT1 is involved in the repair and/or degradation of damaged proteins.
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Synonyms
EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.
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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
RGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAWK SGGASHSELI HNLRKNGIIK TDKVFEVMLA TDRSHYAKCN PYMDSPQSIG FQATISAPHM HAYALELLFD QLHEGAKALD VGSGSGILTA CFARMVGCTG KVIGIDHIKE LVDDSINNVR KDDPTLLSSG RVQLVVGDGR MGYAEEAPYD AIHVGAAAPV VPQALIDQLK PGGRLILPVG PAGGNQMLEQ YDKLQDGSIK MKPLMGVIYV PLTDKEKQWS RWK.
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 :
LDHB Human, HisDescription:
Lactate Dehydrogenase B Human Recombinant, His Tag
LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.
Product # :
ENZ-539Price :
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Shipped with Ice Packs
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Description
LDHB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-334 a.a.) and having a molecular mass of 38.8 kDa. The LDHB is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LDHB Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 6 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.More Info
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Introduction
LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.
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Synonyms
LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.
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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 MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.
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 :
MMP14 HumanDescription:
Matrix Metalloproteinase-14 Recombinant Human
Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.
Product # :
ENZ-1101Price :
Quantity :
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Description
Matrix Metalloproteinase-14 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of 29.6kDa. MMP14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMP14 is supplied as a 0.2 μm filtered solution conteining 20mM Tris-HCl, pH 7.4, 30 % glycerol, 300mM NaCl, 3mM CaCl2 and 10μM ZnCl2.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.
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Synonyms
Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 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
ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG.
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 :
PLA2G5 HumanDescription:
Secreted Phospholipase A2-V Human Recombinant
Calcium-dependent phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, PLA2-10, Group V phospholipase A2, GV-PLA2, MGC46205, hVPLA(2), DKFZp686C2294, sPLA2-V, PLA2G5.
Product # :
ENZ-328Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Phospholipase A2-V Human Recombinant was produced with N-terminal His-Tag. PLA2G5 His-Tagged Fusion protein is 15.5 kDa containing 118 amino acid residues of the human secreted phospholipase A2-V and 16 additional amino acid residues – His-Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4um) and lyophilized in 0.5 mg/mL in 0.05M Acetate buffer pH4.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats. -
Synonyms
Calcium-dependent phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, PLA2-10, Group V phospholipase A2, GV-PLA2, MGC46205, hVPLA(2), DKFZp686C2294, sPLA2-V, PLA2G5.
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Physical Appearance
Lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMASHMGLLD LKSMIEKVTG KNALTNYGFY GCYCGWGGRG TPKDGTDWCC WAHDHCYGRLEEKGCNIRTQ SYKYRFAWGV VTCEPGPFCH VNLCACDRKL VYCLKRNLRS YNPQYQYFPN ILCS.
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 :
LDHA RatDescription:
Lactate Dehydrogenase A, Rat Recombinant
L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.
Product # :
ENZ-960Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LDHA Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-332 a.a) and having a molecular mass of 37.5kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). LDHA is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LDHA protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.
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Synonyms
L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.
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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
MAALKDQLIV NLLKEEQVPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG EMMDLQHGSL FLKTPKIVSS KDYSVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNVVKYSPQ CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPQLGT DADKEQWKDV HKQVVDSAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI SDVVKVTLTP DEEARLKKSA DTLWGIQKEL QFLEHHHHHH.
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 :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
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Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
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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
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD 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 :
GH Antagonist ChickenDescription:
Growth Hormone Antagonist Chicken Recombinant
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-538Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Somatotropin Chicken Antagonist Recombinant mutein G119R produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids with an additional Ala at the N-terminus and having a molecular mass of 22.3 kDa. The Chicken Growth-Hormone Antagonist Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.03% NaHCO3 pH-8.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Recombinant Chicken Growth Hormone G119R mutant did not bind to ovine GHR-ECD and was devoid of any biological activity in FDC-P1 3B9 cells.
However, in binding experiments that were carried out using chicken liver membranes, both ovine GH and chicken GH showed similar IC50 values in competition with 125I-ovine GH, while the IC50 of G119R mutein was 10-fold higher.
These results emphasize the importance of species specificity and indicate the possibility of antagonistic activity of chGH G119R in homologous system.More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth-Hormone Chicken antagonist although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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-Hormone Chicken antagonist in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Phe-Pro-Ala.
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Protein content
Protein quantitation was carried out by: UV spectroscopy at 280 nm using the absorbency value of 0.74 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).
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 :
TerlipressinDescription:
Terlipressin
Product # :
HOR-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Terlipressin contains 12 amino acids Gly-Gly-Gly-c[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2 and having a molecular weight of 1227.37 Dalton.
Formulation
The protein (1 mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Terlipressin is similar to a naturally occurring hormone present in the body, known as antidiuretic hormone (ADH) or vasopressin. ADH has two main effects in the body. Firstly, it causes narrowing of blood vessels (vasoconstriction), thereby limiting blood flow to a particular area of the body. It also acts on receptors in the kidney to retain water in the body, which helps to prevent excessive loss of water in the urine. Terlipressin is commonly used to stop bleeding of varices in the food pipe (oesophagus). Varices are fragile distended veins that can occur in various parts of the body such as the oesophagus. This is caused by an increase in blood pressure in certain diseases such as severe liver disease. These fragile varices can rupture and lead to life threatening bleeding. Terlipressin is therefore given to narrow blood vessels, and so restricting blood flow to the varices and stopping the bleeding.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Terlipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Terlipressin 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 Terlipressin18MΩ-cm H2O not less than 100 µg/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.
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Name :
CST3 Human, PichiaDescription:
Cystatin C Human Recombinant, Pichia
Product # :
PRO-2743Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Cystatin C is having a molecular mass of approximately 13kDa.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from 20mM NH4HCO3.
Purity
Greater than 96.0%.
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 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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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Human CST3 although stable at 4°C for 1 week, should be stored at -20°C.
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Solubility
It is recommended to reconstitute the lyophilized CST3 Human in sterile 18MΩ-cm H2O at a concentration of 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.
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Name :
T.Vaginalis P65 AntibodyDescription:
Polyclonal Rabbit Anti Trichomonas Vaginalis P65 Antibody
Product # :
ANT-494Price :
Quantity :
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Shipped with Ice Packs
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Description
The polyclonal antibody to Trichomonas vaginalis was collected from the rabbit igG and immunized with recombinant T. Vaginalis P65.
Formulation
50mM mg glycine, pH8.0.
Purity
Pure Rabbit IgG.
More Info
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Introduction
Trichomonas vaginalis, an anaerobic, flagellated protozoan parasite, is most dominant protozoan causing sexual transmitted disease. T. vaginalis induced vaginal tract infection occurs as multiple steps involving interactions between host macromolecules and protozoan virulent factor. Adhension protein P65 of T. vaginalis has a vital part in assisting the penetration into vaginal tract surface.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Purification Method
Purified by affinity 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 :
CSNK2A1 HumanDescription:
Casein Kinase 2 alpha 1 Human Recombinant
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.
Product # :
PKA-208Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Casein Kinase 2 alpha 1 Human Recombinant is a non-glycosylated polypeptide having a molecular mass of 45.1 kDa. Casein Kinase 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSNK2A1 is supplied in 25mM Tris-HCl, 500mM NaCl, 1mM DTT, 500μm PMSF, 50% glycerol, pH 8.5.
Purity
Greater than 99% as determined by SDS-PAGE.
More Info
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Introduction
The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes. Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.
Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm. -
Synonyms
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.
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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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Unit Definition
No protease activity detectable, specific activity > 1.320 U/mg (1U = 1µmol/min at 37 degree C) using the synthetic peptide RRRDDDSDDD.
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 :
HSA, Pichia PastorisDescription:
Human Serum Albumin Recombinant, Pichia
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-2149Price :
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Description
HSA Human Recombinant produced in Pichia Pastoris is a polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa.The recombinant Albumin is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
The Recombinant Albumin having a concentration of 200mg/ml contains 140mM sodium chloride and 0.16mM octanoate.
Purity
Greater than 97% as determined by HPLC.
More Info
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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood. -
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Yellowish gel like solution.
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Stability
Recombinant Albumin although stable at 15°C for 1 week, should be stored at 4°C for longer periods of time.Please prevent freeze-thaw cycles.
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Applications
Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.
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 :
Histone BovineDescription:
Bovine Histone
Product # :
PRO-2558Price :
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Description
Histone Bovine is purified from bovine tissues by proprietary protein-chemical techniques.
Source
Bovine tissues.
Formulation
Histone Bovine is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Histone is vastly alkaline protein exists in eukaryotic cell nuclei which set and direct the DNA into structural units named nucleosomes. 5 key families of histones are: H1/H5, H2A, H2B, H3, including H4. The core histones are H2A, H2B, H3 and H4, whereas histones H1/H5 are identified as the linker histones. Moreover the dynamics of chromatin structure depend on posttranslational modification of histones in addition to the appearance of different histone variants. Histone H3 as well as H4 are modified covalently at several residues. The histone code is constitute by these and the H2A/H2B modifications.
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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. Checkerboard/immunodot analysis of positive/negative samples.
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coating concentration
0.2-0.5 μg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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 :
FGF23 HumanDescription:
Fibroblast Growth Factor-23 Human Recombinant
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Product # :
CYT-020Price :
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Description
Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
More Info
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Introduction
FGF-23 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. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
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Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 FGF-23 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
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
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Background
Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.
Mechanism
Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.Interactions
Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.Function
Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.Structure
FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.What is the molecular weight/Mw of FGF23 HUMAN Protein?
FGF23 HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of FGF23 HUMAN Protein?
Escherichia Coli.
What is the Purity of FGF23 HUMAN Protein?
FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF23 HUMAN Protein?
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
What is the amino acid sequence of FGF23 HUMAN Protein?
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
What applications can FGF23 HUMAN Protein be used in?
FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF23 HUMAN Protein?
The endotoxin level is minimal, FGF23 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 :
LMNA HumanDescription:
Lamin A/C Human Recombinant
Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.
Product # :
PRO-2666Price :
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Description
LMNA Human Recombinant fused with a His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 614 amino acids and having a molecular mass of 68.0kDa. The LMNA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LMNA solution contains 20mM Tris-HCl pH 7.5, 1mM DTT, 0.5M NaCl, 1.5mM EDTA and 20%(v/v) glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. -
Synonyms
Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.
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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
MAHHHHHHVG TGSNDDDDKS PDMETPSQRR ATRSGAQASS TPLSPTRITR LQEKEDLQEL NDRLAVYIDR VRSLETENAG LRLRITESEE VVSREVSGI KAAYEAELGD ARKTLDSVAK ERARLQLELS KVREEFKELK ARNTKKEGDL IAAQARLKDL EALLNSKEAA LSTALSEKRT LEGELHDLRG QVAKLEAALG EAKKQLQDEM LRRVDAENRL QTMKEELDFQ KNIYSEELRE TKRRHETRLV EIDNGKQREF ESRLADALQE LRAQHEDQVE QYKKELEKTY SAKLDNARQS AERNSNLVGA AHEELQQSRI RIDSLSAQLS QLQKQLAAKE AKLRDLEDSL ARERDTSRRL LAEKEREMAE MRARMQQQLD EYQELLDIKL ALDMEIHAYR KLLEGEEERL RLSPSPTSQR SRGRASSHSS QTQGGGSVTK KRKLESTESR SSFSQHARTS GRVAVEEVDE EGKFVRLRNK SNEDQSMGNW QIKRQNGDDP LLTYRFPPKF TLKAGQVVTI WAAGAGATHS PPTDLVWKAQ NTWGCGNSLR TALINSTGEE VAMRKLVRSV TVVEDDEDED GDDLLHHHHG SHCSSSGDPA EYNLRSRTVL CGTCGQPADK ASASGSGAQS PQNCSIM
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 :
LIF Human, YeastDescription:
LIF Human Recombinant, Yeast
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-191Price :
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Description
LIF Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 58.5 kDa. The LIF is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from a 0.2 µm filtered PBS.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity of recombinant human LIF was measured by the ability to induce differentiation of murine M1 myeloid leukemic cells. The minimal detectable concentration of human LIF in this assay is <0.05 ng/mL. The specific activity is > 1 x 108 units/mg.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LIF 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 LIF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
S P L P I T P V N A T C A I R H P C H N N L M N Q I R S Q L A Q L N G S A N A L F I L Y Y T A Q G E P F P N N L D K L C G P N V T D F P P F H A N G T E K A K L V E L Y R I V V Y L G T S L G N I T R D Q K I L N P S A L S L H S K L N A T A D I L R G L L S N V L C R L C S K Y H V G H V D V T Y G P D T S G K D V F Q K K K L G C Q L L G K Y K Q I I A V L A Q A F.
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 :
Leptin PorcineDescription:
Leptin Porcine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-503Price :
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Shipped at Room temp
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Description
Leptin Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and additional Ala at N-terminus, having a molecular mass of 16kDa. The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 recombinant porcine leptin in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Trp.
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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 0.57 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 calibrated solution of Leptin Porcine 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.
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Name :
Thymosin beta 4Description:
Thymosin β4
Thymosin beta-4. TB500, TB-500
Product # :
HOR-275Price :
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Shipped at Room temp
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Description
Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Introduction
Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.
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Synonyms
Thymosin beta-4. TB500, TB-500
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
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 :
CSNK1A1 HumanDescription:
Casein Kinase 1 alpha 1 Human Recombinant
Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.
Product # :
PKA-056Price :
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Shipping Method :
Shipped with Ice Packs
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Description
CSNK1A1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337) and having a molecular mass of 41kDa. CSNK1A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CSNK1A1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Caseine Kinase 1 alpha belongs is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily. The CK1 isoforms - alpha, beta, gamma, delta, epsilon and their splice variants are involved in diverse cellular processes including membrane trafficking, circadian rhythm, cell cycle progression, chromosome segregation, apoptosis and cellular differentiation. Possibly CSNK1A1 can phosphorylate a large number of proteins and is involved in Wnt signaling where it phosphorylates CTNNB1 on Ser45. CSNK1A1 also interacts with the Axin complex.
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Synonyms
Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.
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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 MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF.
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 5 HumanDescription:
Bone Morphogenetic protein-5 Human Recombinant
Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.
Product # :
CYT-660Price :
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Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.BMP-5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BMP-5 solution contains 10mM Sodium Citrate buffer (pH3.5) and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors. -
Synonyms
Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.
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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
MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.
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Background
Bone Morphogenetic Protein-5 Human Recombinant: Unleashing the Potential for Tissue Engineering and Regenerative Medicine
Abstract:
Bone Morphogenetic Protein-5 (BMP-5) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, repair, and regeneration. This research paper provides an in-depth analysis of BMP-5, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-5 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.
Introduction:
Tissue engineering and regenerative medicine hold great promise for addressing the challenges of tissue repair and regeneration. BMP-5, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the unique features of BMP-5 and presents novel approaches for the production and optimization of BMP-5 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-5 is a secreted growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intracellular signaling cascades. BMP-5 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.
Production of BMP-5 Human Recombinant:
Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-5 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-5. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-5 recombinant protein.
Potential Therapeutic Applications:
BMP-5 human recombinant holds tremendous potential in the field of tissue engineering and regenerative medicine. It plays a crucial role in bone formation, cartilage regeneration, and wound healing, making it a promising candidate for the treatment of skeletal disorders, osteochondral defects, and tissue injuries. Furthermore, the ability of BMP-5 to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-5 human recombinant emerges as a key regulator in tissue engineering and regenerative medicine, with significant implications for tissue repair and regeneration. Optimizing production methodologies and further elucidating its signaling mechanisms will enhance its therapeutic applications. With its involvement in bone and cartilage formation, as well as wound healing, BMP-5 human recombinant represents a promising tool for promoting tissue regeneration and addressing the challenges of tissue repair in various clinical contexts.
What is the molecular weight/Mw of BMP5 Protein?
BMP5 Protein has a total Mw of 15.7kDa.
What is the source or expression system of BMP5 Protein?
Escherichia Coli.
What is the Purity of BMP5 Protein?
BMP5 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP5 Protein?
The biological functionality of BMP5 Protein will be determined in the future.
What is the amino acid sequence of BMP5 Protein?
MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.
What applications can BMP5 Protein be used in?
BMP5 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP5 Protein?
The endotoxin level is minimal, BMP5 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 :
GDF10 HumanDescription:
Growth differentiation factor 10 Human Recombinant
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
Product # :
CYT-659Price :
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- sds-page
Description
GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa. GDF10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF10 solution (1mg/ml) contains 10mM Sodium citrate (pH 3.5), 1mM DTT, 40% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.
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Synonyms
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
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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
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
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Background
What is the molecular weight/Mw of GDF10 HUMAN Protein?
GDF10 HUMAN Protein has a total Mw of 12.5kDa.
What is the source or expression system of GDF10 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF10 HUMAN Protein?
GDF10 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF10 HUMAN Protein?
The biological functionality of GDF10 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF10 HUMAN Protein?
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
What applications can GDF10 HUMAN Protein be used in?
GDF10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF10 HUMAN Protein?
The endotoxin level is minimal, GDF10 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 :
GM-CSF Human, PichiaDescription:
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Product # :
CYT-324Price :
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Shipped at Room temp
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Description
Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein. GM-CSF is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.
Purity
Greater than 97.0% as determined by1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
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Background
What is the molecular weight/Mw of GM-CSF HUMAN, PICHIA Protein?
GM-CSF HUMAN, PICHIA Protein has a total Mw of 29kDa.
What is the source or expression system of GM-CSF HUMAN, PICHIA Protein?
Pichia Pastoris.
What is the Purity of GM-CSF HUMAN, PICHIA Protein?
GM-CSF HUMAN, PICHIA Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF HUMAN, PICHIA Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.
What is the amino acid sequence of GM-CSF HUMAN, PICHIA Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
What applications can GM-CSF HUMAN, PICHIA Protein be used in?
GM-CSF HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF HUMAN, PICHIA Protein?
The endotoxin level is minimal, GM-CSF HUMAN, PICHIA 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 :
IL 1 alpha RatDescription:
Interleukin-1 alpha Rat Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Product # :
CYT-381Price :
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Shipped at Room temp
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Description
Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.More Info
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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.
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 :
PECAM1 HumanDescription:
Platelet Endothelial Cell Adhesion Molecule 1 Human Recombinant
Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.
Product # :
CYT-924Price :
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Description
PECAM1 Human Recombinant produced in Sf9 Baculovirus is a single, non-glycosylated polypeptide chain containing 582 amino acids (28-601a.a.) and having a molecular mass of 65.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions).PECAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PECAM1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet endothelial cell adhesion molecule (PECAM1) induces susceptibility to atherosclerosis. PECAM1 averts phagocyte ingestion of closely apposed viable cells by transmitting detachment signals, and transforms function upon apoptosis, thus promoting tethering of dying cells to phagocytes. The encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces as a result causing the viable cell's active repulsion from the phagocyte.
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Synonyms
Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 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
QENSFTINSV DMKSLPDWTV QNGKNLTLQC FADVSTTSHV KPQHQMLFYK DDVLFYNISS MKSTESYFIP EVRIYDSGTY KCTVIVNNKE KTTAEYQVLV EGVPSPRVTL DKKEAIQGGI VRVNCSVPEE KAPIHFTIEK LELNEKMVKL KREKNSRDQN FVILEFPVEE QDRVLSFRCQ ARIISGIHMQ TSESTKSELV TVTESFSTPK FHISPTGMIM EGAQLHIKCT IQVTHLAQEF PEIIIQKDKA IVAHNRHGNK AVYSVMAMVE HSGNYTCKVE SSRISKVSSI VVNITELFSK PELESSFTHL DQGERLNLSC SIPGAPPANF TIQKEDTIVS QTQDFTKIAS KSDSGTYICT AGIDKVVKKS NTVQIVVCEM LSQPRISYDA QFEVIKGQTI EVRCESISGT LPISYQLLKT SKVLENSTKN SNDPAVFKDN PTEDVEYQCV ADNCHSHAKM LSEVLRVKVI APVDEVQISI LSSKVVESGE DIVLQCAVNE GSGPITYKFY REKEGKPFYQ MTSNATQAFW TKQKASKEQE GEYYCTAFNR ANHASSVPRS KILTVRVILA PWKKVEHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.