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1000 results found for “Lactoferrin”
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Name :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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 :
Cystatin-C ProteinDescription:
Cystatin-C Human Recombinant
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-2601Price :
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Shipped with Ice Packs
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Description
Cystatin-C Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13.3kDa. Cystatin-C is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cystatin-C is supplied as a 0.2 μm filtered solution containing 20mM Tris-HCl, 50 % glycerol, pH 8.0 and 300mM NaCl.
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
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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Synonyms
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
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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
SSPGKPPRLV GGPMDASVEE EGVRRALDFA VGEYNKASND MYHSRALQVV RARKQIVAGV NYFLDVELGR TTCTKTQPNL DNCPFHDQPH LKRKAFCSFQ IYAVPWQGTM TLSKSTCQDA.
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 :
TNFRSF10A Human FcDescription:
TRAIL Receptor-1 Human Recombinant Fc
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
Product # :
CYT-877Price :
Quantity :
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Shipped at Room temp
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Description
TRAIL R1 Fc Human Recombinant (24-240) produced in E.Coli is a non-glycosylated, disulfide-linked homodimer containing two polypeptide chains of 217 amino acids each and having a molecular mass of 41kDa [including tag] each chain. TRAILR1 is fused to a 236 amino acid Fc tag at C-terminal and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to inhibit Trail-mediated cytotoxicity in mouse L-929 cells, is less than 1.25ng/ml.More Info
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Introduction
Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFRSF10A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL-R1 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 TNFRSF10A 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
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSERPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSTGCPR GMVKVKDCTP WSDIECVHKE SGNGHNIEGR MDPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK.
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 :
Cyclophilin F Rat BioactiveDescription:
Cyclophilin-F Rat Recombinant Bioactive
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
Product # :
ENZ-1019Price :
Quantity :
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Shipped with Ice Packs
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Description
Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206 a.a) and having a molecular mass of 21.2Da. Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin F protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,300 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmol of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.More Info
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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
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Synonyms
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
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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 MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.
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 :
PLAC8 HumanDescription:
Placenta-Specific 8 Human Recombinant
Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.
Product # :
PRO-1725Price :
Quantity :
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Shipped with Ice Packs
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Description
PLAC8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa.PLAC8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLAC8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0),0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Placenta-Specific 8 (PLAC8) is a member of the cornifelin family. The PLAC8 protein is expressed at high levels in the plasmacytoid dendritic cells, spleen, lymph nodes, peripheral blood leukocytes, and bone marrow.
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Synonyms
Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.
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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 MGSMQAQAPV VVVTQPGVGP GPAPQNSNWQ TGMCDCFSDC GVCLCGTFCF PCLGCQVAAD MNECCLCGTS VAMRTLYRTR YGIPGSICDD YMATLCCPHC TLCQIKRDIN RRRAMRTF.
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 :
FURIN HumanDescription:
Furin Human Recombinant
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
Product # :
PRO-2199Price :
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Shipped with Ice Packs
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Description
FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.
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Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.
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 :
Betacellulin His HumanDescription:
Betacellulin Human Recombinant, His Tag
Betacellulin, Probetacellulin.
Product # :
CYT-077Price :
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Shipped with Ice Packs
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- sds-page
Description
BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Synonyms
Betacellulin, Probetacellulin.
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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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
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Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 11.3kDa.
What is the source or expression system of BETACELLULIN Protein?
Escherichia Coli.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
The biological functionality of BETACELLULIN Protein will be determined in the future.
What is the amino acid sequence of BETACELLULIN Protein?
MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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 :
AIFM1 HumanDescription:
Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 Human Recombinant
Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.
Product # :
PRO-1898Price :
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Shipped with Ice Packs
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Description
AIFM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (98-609) and having a molecular mass of 58.5 kDa.AIFM1 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AIFM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 (AIFM1) is a mitochondrial protein which translocates to the nucleus once apoptosis has been initiated. AIFM1 causes DNA fragmentation and chromatin condensation and also triggers the release of cytochrome c and caspase-9 from mitochondria. Bcl-2 overexpression prevents the release of AIFM1 from mitochondria, but doesn’t block its apoptogenic activity.
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Synonyms
Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFLGLTP EQKQKKAALS ASEGEEVPQD KAPSHVPFLL IGGGTAAFAA ARSIRARDPG ARVLIVSEDP ELPYMRPPLS KELWFSDDPN VTKTLRFKQW NGKERSIYFQ PPSFYVSAQD LPHIENGGVA VLTGKKVVQL DVRDNMVKLN DGSQITYEKC LIATGGTPRS LSAIDRAGAE VKSRTTLFRK IGDFRSLEKI SREVKSITII GGGFLGSELA CALGRKARAL GTEVIQLFPE KGNMGKILPE YLSNWTMEKV RREGVKVMPN AIVQSVGVSS GKLLIKLKDG RKVETDHIVA AVGLEPNVEL AKTGGLEIDS DFGGFRVNAE LQARSNIWVA GDAACFYDIK LGRRRVEHHD HAVVSGRLAG ENMTGAAKPY WHQSMFWSDL GPDVGYEAIG LVDSSLPTVG VFAKATAQDN PKSATEQSGT GIRSESETES EASEITIPPS TPAVPQAPVQ GEDYGKGVIF YLRDKVVVGI VLWNIFNRMP IARKIIKDGE QHEDLNEVAK LFNIHED.
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 :
IL17F HumanDescription:
Interleukin 17F Human Recombinant
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Product # :
CYT-587Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-17F Human Recombinant produced in E.Coli is a homodimeric, cysteine linked, non-glycosylated polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 30.1 kDa.The IL-17F Human is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium citrate buffer pH-3.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM_CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway. -
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin Human IL17F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human IL-17F 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 Human IL17F in sterile water not more than 1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MRKIPKVGHT FFQKPESCPP VPGGSMKLDI GIINENQRVS MSRNIESRST SPWNYTVTWD PNRYPSEVVQ AQCRNLGCIN AQGKEDISMN SVPIQQETLV VRRKHQGCSV SFQLEKVLVT VGCTCVTPVI HHVQ.
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 :
TFF3 HumanDescription:
Trefoil Factor-3 Human Recombinant
TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.
Product # :
CYT-005Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TFF-3 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 59 amino acid chains which includes a 40 amino acid trefoil motif containing 3 conserved interamolecular disulfide bonds and having a total molecular mass of 13.2kDa. TFF-3 Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by RP-HPLC and SDS-PAGE analysis.
Biological Activity
The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of > 100IU/mg.More Info
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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.
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Synonyms
TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TFF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF3 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 TFF3 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
EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF.
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 :
IRF1 HumanDescription:
IFN Regulatory Factor-1 Human Recombinant
IRF-1, IRF1, MAR.
Product # :
CYT-449Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml in 20mM Tris pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.
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Synonyms
IRF-1, IRF1, MAR.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid IRF1 although stable at 10°C for 1 week, should be stored 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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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
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Background
What is the molecular weight/Mw of IRF1 HUMAN Protein?
IRF1 HUMAN Protein has a total Mw of XX15kDa.
What is the source or expression system of IRF1 HUMAN Protein?
Escherichia Coli.
What is the Purity of IRF1 HUMAN Protein?
IRF1 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IRF1 HUMAN Protein?
The biological functionality of IRF1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IRF1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
What applications can IRF1 HUMAN Protein be used in?
IRF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IRF1 HUMAN Protein?
The endotoxin level is minimal, IRF1 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 :
TNFRSF17 Human, HisDescription:
B-Cell Maturation Antigen Human Recombinant, His Tag
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
Product # :
CYT-190Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (78-184 a.a) and having a molecular mass of 14.1kDa.TNFRSF17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFRSF17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.
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Synonyms
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
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Physical Appearance
Sterile Filtered colorless liquid.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRKINSEP LKDEFKNTGS GLLGMANIDL EKSRTGDEII LPRGLEYTVE ECTCEDCIKS KPKVDSDHCF PLPAMEEGAT ILVTTKTNDY CKSLPAALSA TEIEKSISAR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin tA OvineDescription:
Leptin Antagonist Triple Mutant Ovine Recombinant
Product # :
CYT-356Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2 mM and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, 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-Arg.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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.
- View Data Sheet
Name :
CFH HumanDescription:
Complement Factor H Human
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
Product # :
PRO-2700Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Human Complement Factor H produced in Human plasma having a total molecular mass of 155kDa.
Source
Human Plasma.
Formulation
CFH protein solution contains PBS, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.
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Synonyms
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
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Physical Appearance
Sterile filtered solution.
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Stability
CFH Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
Adiponectin Human, TrimericDescription:
Adiponectin Human Recombinant, Trimeric form
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-233Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Trimeric form of Adiponectin Human trimeric form was expressed in HEK293 cells. The cysteine 39 was replaced with Alanine (C39A) 9. hAd-C39A can only form a trimer, but not a hexamer or an HMW form.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl, pH 7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.
More Info
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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue.
Many studies demonstrate that Adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle. Attenuate hepatic lipogenesis and gluconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, Adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of Adiponectin activates different signaling pathways and exerts distinct functions. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Adiponectin 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 deionized water to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25 kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
HIF1A Human, HisDescription:
Hypoxia-Inducible Factor-1 Alpha Human Recombinant, His Tag
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
Product # :
PRO-415Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (576-785 a.a.) and having a molecular mass of 25.1 kDa. The HIF1A is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HIF1A Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
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Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSFDQLSPLE SSSASPESAS PQSTVTVFQQ TQIQEPTANA TTTTATTDEL KTVTKDRMED IKILIASPSP THIHKETTSA TSSPYRDTQS RTASPNRAGK GVIEQTEKSH PRSPNVLSVA LSQRTTVPEE ELNPKILALQ NAQRKRKMEH DGSLFQAVGI GTLLQQPDDH AATTSLSWKR VKGCKSSEQN GMEQKTIILI PSDLACRLLG Q.
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 :
OSM RatDescription:
Oncostatin-M Rat Recombinant
Oncostatin-M, OSM, OncoM.
Product # :
CYT-169Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, 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 as determined by the dose-dependent stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
Oncostatin-M, OSM, OncoM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M 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
KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.
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 :
Procalcitonin HumanDescription:
Procalcitonin Human Recombinant
Procalcitonin, PCT.
Product # :
HOR-304Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids and having a molecular mass of 12.8 kDa.The Procalcitonin is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Procalcitonin, PCT.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized procalcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution procalcitonin 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 procalcitonin sterile 18MΩ-cm H2O at 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN.
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 :
Adiponectin Human, HisDescription:
Adiponectin Human Recombinant, His tag
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-433Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The Acrp30 Human is created as a recombinant protein with N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is 26.4 kDa protein containing 230 amino acid residues of the Acrp30 Human and 12 additional amino acid residues - HisTag (underlined).
Source
Escherichia Coli.
Formulation
Acrp30 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.02M Tris buffer pH7.5, 0.15M NaCl.
Purity
Acrp30 Human purity is greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.
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Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26.4kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
SCF HumanDescription:
Stem Cell Factor Human Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-255Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Stem Cell Factor Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18409 Dalton. The SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
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Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell 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 Met-Glu-Gly-Ile-Cys.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.52 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 Stem Cell Factor 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.
- View Data Sheet
Name :
EFNA3 Human, Sf9Description:
Ephrin A3 Human Recombinant, Sf9
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
Product # :
PRO-2614Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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Description
EFNA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (23-214aa) and having a molecular mass of 48.7kDaEFNA3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The Fractalkine solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.
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Synonyms
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
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Physical Appearance
Sterile Filtered colorless solution.
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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
ADPQGPGGAL GNRHAVYWNS SNQHLRREGY TVQVNVNDYL DIYCPHYNSS GVGPGAGPGP
GGGAEQYVLY MVSRNGYRTC NASQGFKRWE CNRPHAPHSP IKFSEKFQRY SAFSLGYEFH
AGHEYYYIST PTHNLHWKCL RMKVFVCCAS TSHSGEKPVP TLPQFTMGPN VKINVLEDFE
GENPQVPKLE KSISGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV
TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY
KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV
EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH
HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
F11R HumanDescription:
F11 Receptor Human Recombinant
Junctional adhesion molecule A, JAM-A, Junctional adhesion molecule 1, JAM-1, Platelet F11 receptor, Platelet adhesion molecule 1, PAM-1, CD321, F11R, JAM1, JCAM, JAM, KAT, JAMA.
Product # :
PRO-1112Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- purity
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Description
F11R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (26-238 a.a) and having a molecular mass of 25.8kDa.F11R is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
F11R protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
F11R (CD321) is a member of the immunoglobulin superfamily. F11R has a role in epithelial tight junction formation. Tight junctions exemplify one type of cell-to-cell adhesion in epithelial or endothelial cell sheets, establishing continuous seals around cells and acting as a physical barrier to thwart solutes and water from passing easily through the paracellular space. F11R protein can function as a receptor for reovirus, or as a ligand for the integrin LFA1, involved in leukocyte transmigration, or a platelet receptor.
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Synonyms
Junctional adhesion molecule A, JAM-A, Junctional adhesion molecule 1, JAM-1, Platelet F11 receptor, Platelet adhesion molecule 1, PAM-1, CD321, F11R, JAM1, JCAM, JAM, KAT, JAMA.
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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 MGSHMLGSVT VHSSEPEVRI PENNPVKLSC AYSGFSSPRV EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT REDTGTYTCM VSEEGGNSYG EVKVKLIVLV PPSKPTVNIP SSATIGNRAV LTCSEQDGSP PSEYTWFKDG IVMPTNPKST
RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGV.
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 :
CACYBP HumanDescription:
Calcyclin Binding Protein Human Recombinant
S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.
Product # :
PRO-831Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
CACYBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-185a.a.) and having a molecular mass of 23.4 kDa. CACYBP protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CACYBP Human solution containing 20mM Tris HCL pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CACYBP (calcyclin binding protein) participates in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. CACYBP acts as a molecular bridge in ubiquitin E3 complexes. CACYBP is involved in the ubiquitin-mediated degradation of beta-catenin.
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Synonyms
S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.
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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 MQQKSQKKAE LLDNEKPAAV VAPITTGYTV KISNYGWDQS DKFVKIYITL TGVHQVPTEN VQVHFTERSF DLLVKNLNGK SYSMIVNNLL KPISVEGSSK KVKTDTVLIL CRKKVENTRW DYLTQVEKEC KEKEKPSYDT ETDPSEGLMN VLKKIYEDGD DDMKRTINKA WVESREKQAK GDTEF.
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 :
KLF4 Human, HisDescription:
Kruppel-Like Factor 4 Human Recombinant, His Tag
Kruppel-Like Factor 4 (Gut), GKLF, EZF, Epithelial Zinc Finger Protein EZF, Gut-Enriched Krueppel-Like Factor, Endothelial Kruppel-Like Zinc Finger Protein, Krueppel-Like Factor 4, Krueppel-like factor 4, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor.
Product # :
PRO-2186Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
KLF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (11-395 a.a) and having a molecular mass of 44.2kDa. KLF4 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
KLF4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.
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Synonyms
Kruppel-Like Factor 4 (Gut), GKLF, EZF, Epithelial Zinc Finger Protein EZF, Gut-Enriched Krueppel-Like Factor, Endothelial Kruppel-Like Zinc Finger Protein, Krueppel-Like Factor 4, Krueppel-like factor 4, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAVS DALLPSFSTF ASGPAGREKT LRQAGAPNNR WREELSHMKR LPPVLPGRPY DLAAATVATD LESGGAGAAC GGSNLAPLPR RETEEFNDLL DLDFILSNSL THPPESVAAT VSSSASASSS SSPSSSGPAS APSTCSFTYP IRAGNDPGVA PGGTGGGLLY GRESAPPPTA PFNLADINDV SPSGGFVAEL LRPELDPVYI PPQQPQPPGG GLMGKFVLKA SLSAPGSEYG SPSVISVSKG SPDGSHPVVV APYNGGPPRT CPKIKQEAVS SCTHLGAGPP LSNGHRPAAH DFPLGRQLPS RTTPTLGLEE VLSSRDCHPA LPLPPGFHPH PGPNYPSFLP DQMQPQVPPL HYQELMPPGS CMPEEPKPKR GRRSWPRKRT AT.
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.