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Name :
LTF Holo HumanDescription:
Lactoferrin Holo Human Recombinant
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Product # :
PRO-592Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Holo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Holo Lactoferrin is purified by proprietary chromatographic techniques.
Source
Rice Flour.
Formulation
The Human Holo lactoferrin was lyophilized with no additives.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.
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Synonyms
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
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Physical Appearance
Pink lyophilized powder.
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Stability
Recombinant Holo Lactoferrin although stable at room temperature for 5 days, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized LTF Holo Human in sterile water at 10mg/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 :
Thymosin β4Description:
Thymosin-b4 Human Recombinant
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
Product # :
HOR-003Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
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Introduction
CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.
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Synonyms
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human 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 Thymosin B4 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
SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LysostaphinDescription:
Lysostaphin Recombinant
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
Product # :
ENZ-269Price :
Quantity :
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Shipped at Room temp
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Description
Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without any additives.
Purity
98% as determined by RP-HPLC.
Biological Activity
Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C. Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.
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Introduction
Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.
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Synonyms
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.
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Protein content
Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.
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Specific Activity
Determined to be 3,540 units/mg.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Adipsin Human, Sf9Description:
Complement Factor D Human Recombinant, Sf9
Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.
Product # :
PRO-2213Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Adipsin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 241 amino acids (21-253a.a.) and having a molecular mass of 26.01kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). Adipsin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Adipsin protein solution (1mg/ml) contains phosphate buffered saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.
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Synonyms
Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.
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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
PPRGRILGGR EAEAHARPYM ASVQLNGAHL CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS VLAVEHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SCRN1 HumanDescription:
Secernin 1 Human Recombinant
Secernin-1, SES1, KIAA0193, Secernin 1.
Product # :
PRO-2212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SCRN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 48.8kDa. SCRN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SCRN1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) , 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Secernin 1 (SCRN1) which is a member of the peptidase C69 family, regulates exocytosis in mast cells. SCRN1 increases both the level of secretion and the sensitivity of mast cells to stimulation with calcium.
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Synonyms
Secernin-1, SES1, KIAA0193, Secernin 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
GSSHHHHHH SSGLVPRGSH MGSMAAAPPS YCFVAFPPRA KDGLVVFGKN SARPRDEVQE VVYFSAADHE PESKVECTYI SIDQVPRTYA IMISRPAWLW GAEMGANEHG VCIANEAINT REPAAEIEAL LGMDLVRLGL ERGETAKEAL DVIVSLLEEH GQGGNYFEDA NSCHSFQSAY LIVDRDEAWV LETIGKYWAA EKVTEGVRCI CSQLSLTTKM DAEHPELRSY AQSQGWWTGE GEFNFSEVFS PVEDHLDCGA GKDSLEKQEE SITVQTMMNT LRDKASGVCI DSEFFLTTAS GVSVLPQNRS SPCIHYFTGT PDPSRSIFKP FIFVDDVKLV PKTQSPCFGD DDPAKKEPRF QEKPDRRHEL YKAHEWARAI IESDQEQGRK LRSTMLELEK QGLEAMEEIL TSSEPLDPAE VGDLFYDCVD TEIKFFK.
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 :
EFNB3 HumanDescription:
Ephrin- B3 Human Recombinant
Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.
Product # :
PRO-1169Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EFNB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-226 a.a) and having a molecular mass of 24.6kDa.EFNB3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
EFNB3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.
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Synonyms
Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.
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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 MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP.
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 :
OCM HumanDescription:
Oncomodulin-1 Human Recombinant
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
Product # :
PRO-143Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
More Info
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Introduction
Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.
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Synonyms
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. 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
MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.
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Applications
Western blotting.
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 :
OLR1 Human, HEKDescription:
Oxidized Low Density Lipoprotein Receptor 1 Human Recombinant, HEK
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1, SR-E1.
Product # :
PRO-2293Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
OLR1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser61-Gln273) containing a total of 221 amino acids, having a calculated molecular mass of 25.3kDa and fused to a 8 aa Flag tag at N-Terminus.
Source
HEK 293.
Formulation
OLR1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.
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Synonyms
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1, SR-E1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.
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Amino Acid Sequence
DYKDDDDKSQ VSDLLTQEQA NLTHQKKKLE GQISARQQAE EASQESENEL KEMIETLARK LNEKSKEQME LHHQNLNLQE TLKRVANCSA PCPQDWIWHG ENCYLFSSGS FNWEKSQEKC LSLDAKLLKI NSTADLDFIQ QAISYSSFPF WMGLSRRNPS YPWLWEDGSP LMPHLFRVRG AVSQTYPSGT CAYIQRGAVY AENCILAAFS ICQKKANLRA 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.
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Name :
ETHE1 HumanDescription:
Ethylmalonic Encephalopathy 1 Human Recombinant
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
Product # :
PRO-1027Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ETHE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (13-254) and having a molecular mass of 29.1kDa.ETHE1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ETHE1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ETHE1 is a mitochondrial sulfur dioxygenase involved in catabolism of sulfide that accumulates to toxic levels in ethylmalonic encephalopathy. Mutations of ETHE1 were detected in all the typical ethylmalonic encephalopathy patients analysed, but no ETHE1 mutations were identified in patients presenting with early onset progressive encephalopathy with ethylmalonic aciduria.
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Synonyms
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLSQRG GSGAPILLRQ MFEPVSCTFT YLLGDRESRE AVLIDPVLET APRDAQLIKE LGLRLLYAVN THCHADHITG SGLLRSLLPG CQSVISRLSG AQADLHIEDG DSIRFGRFAL ETRASPGHTP GCVTFVLNDH SMAFTGDALL IRGCGRTDFQ QGCAKTLYHS VHEKIFTLPG DCLIYPAHDY HGFTVSTVEE ERTLNPRLTL SCEEFVKIMG NLNLPKPQQI DFAVPANMRC GVQTPTA
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 :
C19ORF80 HumanDescription:
Chromosome 19 Open Reading Frame 80 Human Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-1575Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C19ORF80 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-198) containing 187 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.1kDa (calculated).
Source
Escherichia Coli.
Formulation
C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/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. C19ORF80 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
MKHHHHHHASAPMGGPELAQ HEELTLLFHG TLQLGQALNG VYRTTEGRLT KARNSLGLYG RTIELLGQEV SRGRDAAQEL RASLLETQME EDILQLQAEA TAEVLGEVAQ AQKVLRDSVQ RLEVQLRSAW LGPAYREFEV LKAHADKQSH ILWALTGHVQ RQRREMVAQQ HRLRQIQERL HTAALPA.
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 :
C19ORF80 RatDescription:
Chromosome 19 Open Reading Frame 80 Rat Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-2024Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C19ORF80 Rat Recombinant produced in E. coli is a polypeptide chain containing 193 amino acids and having a total molecular mass of 22.0 kDa. C19ORF80 has a N-Terminal His-tag (10 AA residue).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from a 0.5mg/ml solution containing 0.03M Acetate buffer pH 4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/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. C19ORF80 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
MKHHHHHHAS VRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYKA TEARLTEAGR NLGLFDQALE FLGREVNQGR DATRELRTSL SEIQAEEDTL HLRAEATARS LREVARAQHA LRNSVRRLQV QLRGAWLGQA HQEFENLKDR ADKQNHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHMAA LPA
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 :
TCEAL3 HumanDescription:
Transcription Elongation Factor A (SII)-Like 3 Human Recombinant
Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.
Product # :
PRO-1128Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TCEAL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 224 amino acids (1-200) and having a molecular mass of 25.0 kDa.TCEAL3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TCEAL3 solution (0.5mg/ml) contains 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
TCEAL3 belongs to the transcription elongation factor A (SII)-like (TCEAL) gene family. TCEAL family members hold TFA domains and operate as nuclear phosphoproteins which control transcription in a promoter context-dependent fashion. Various family members are situated in the X chromosome.
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Synonyms
Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.
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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 MGSHMEKPYN KNEGNLENEG KPEDEVEPDD EGKSDEEEKP DVEGKTECEG KREDEGEPGD EGQLEDEGSQ EKQGRSEGEG KPQGEGKPAS QAKPESQPRA AEKRPAEDYV PRKAKRKTDR GTDDSPKDSQ EDLQERHLSS EEMMRECGDV SRAQEELRKK QKMGGFHWMQ RDVQDPFAPR GQRGVRGVRG GGRGQRGLHD IPYL
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 :
TCEAL8 HumanDescription:
Transcription Elongation Factor A (SII)-Like 8 Human Recombinant
Transcription elongation factor A protein-like 8, TCEA-like protein 8, Transcription elongation factor S-II protein-like 8, TCEAL8.
Product # :
PRO-1188Price :
Quantity :
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Description
TCEAL8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-117 a.a) and having a molecular mass of 14.7kDa (Molecular weight on SDS-PAGE will appear higher).TCEAL8 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TCEAL8 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 20% glycerol, 1mM DTT and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Transcription elongation factor A protein-like 8 (TCEAL8) is a member of the TFS-II family and TFA subfamily. TCEAL8 is involved in transcriptional regulation and localized in nucleus. TFS-II family members contain TFA domains and act as nuclear phosphoproteins which control transcription in a promoter context-dependent mode. Numerous family members are found on the X chromosome.
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Synonyms
Transcription elongation factor A protein-like 8, TCEA-like protein 8, Transcription elongation factor S-II protein-like 8, TCEAL8.
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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
MQKSCEENEG KPQNMPKAEE DRPLEDVPQE AEGNPQPSEE GVSQEAEGNP RGGPNQPGQG FKEDTPVRHL DPEEMIRGVD ELERLREEIR RVRNKFVMMH WKQRHSRSRP YPVCFRPLEH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PHB HumanDescription:
Prohibitin Human Recombinant
PHB1, Prohibitin.
Product # :
PRO-1381Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 292 amino acids (1-272a.a) and having a molecular mass of 31.9kDa. PHB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PHB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Prohibitin (PHB) is an evolutionarily conserved gene that is ubiquitously expressed and which Mutations have been linked to sporadic breast cancer. PHB is thought to be a negative regulator of cell proliferation and may be a tumor suppressor. Prohibitin is expressed as two transcripts with changeable lengths of 3' untranslated region. The longer transcript is present at higher levels in proliferating tissues and cells, proposing that this longer 3' untranslated region functions as a trans-acting regulatory RNA.
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Synonyms
PHB1, Prohibitin.
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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 MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ.
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 :
LILRB1 HumanDescription:
Leukocyte Immunoglobulin Like Receptor B1 Human Recombinant
Leukocyte immunoglobulin-like receptor subfamily B member 1,Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B
Product # :
PRO-2668Price :
Quantity :
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Description
LILRB1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (24-461 a.a) and having a molecular mass of 48.5kDa.LILRB1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The LILRB1 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Biological activity is > 50%. It is defined by the ability of the immobilized protein to support the adhesion of HSB2 human peripheral blood acute lymphoblastic leukemia cells, while the cells are added to LILRB1 coated plates at 5ug/ml.
More Info
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Introduction
Leukocyte Immunoglobulin Like Receptor B1 (LILRB1) is a member of the leukocyteimmunoglobulinlike receptor (LIR) family. LILRB1is expressed on immune cells, binds to MHC classI molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immuneresponse. LILRB1 controls inflammatory responses and cytotoxicity to help focus the immune responseand limit autoreactivity. LILRB1 is also expressed on the surface of B cells and monocytes, subsets of NKcells, gamma δ T cells,memory/effector CD8+ T cells and monocyte-derived dendritic cells.
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Synonyms
Leukocyte immunoglobulin-like receptor subfamily B member 1,
Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B -
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
GHLPKPTLWA EPGSVITQGS PVTLRCQGGQ ETQEYRLYRE KKTAPWITRI PQELVKKGQF PIPSITWEHT GRYRCYYGSD TAGRSESSDP LELVVTGAYI KPTLSAQPSP VVNSGGNVTL QCDSQVAFDG FILCKEGEDE HPQCLNSQPH ARGSSRAIFS VGPVSPSRRW WYRCYAYDSN SPYEWSLPSD LLELLVLGVS KKPSLSVQPG PIVAPEETLT LQCGSDAGYN RFVLYKDGER DFLQLAGAQP QAGLSQANFT LGPVSRSYGG QYRCYGAHNL SSEWSAPSDP LDILIAGQFY DRVSLSVQPG PTVASGENVT LLCQSQGWMQ TFLLTKEGAA DDPWRLRSTY QSQKYQAEFP MGPVTSAHAG TYRCYGSQSS KPYLLTHPSD PLELVVSGPS GGPSSPTTGP TSTSGPEDQP LTPTGSDPQS GLGRHLGVLE 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 :
CHGB HumanDescription:
Chromogranin B Human Recombinant
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
Product # :
PRO-824Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.
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Synonyms
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
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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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.
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 :
LPL HumanDescription:
Lipoprotein Lipase Human Recombinant
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
Product # :
ENZ-086Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human LPL produced in E.coli has a molecular mass of 51.61kDa containing 458 amino acid residues of the human LPL and fused to a 10 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
LPL was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 50mM Acetate buffer, pH=4.
More Info
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Introduction
LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.
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Synonyms
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 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
MKHHHHHHAS ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA QEHYPVSAGY TKLVGQDVAR FINWMEEEFN YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCSSKEAF EKGLCLSCRK NRCNNLGYEI SKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESETH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV DIGELLMLKL KWKSDSYFSW SDWWSSPGFA IQKIRVKAGE TQKKVIFCSR EKVSHLQKGK APAVFVKCHD KSLNKKSG.
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 :
LRPAP1 MouseDescription:
Low Density Lipoprotein Receptor Related Protein Associated Protein 1 Mouse Recombinant
Low density lipoprotein-related protein-associated protein 1 (alpha-2-macroglobulin receptor-associated protein 1), A2MRAP, HBP44, RAP, A2RAP, Alpha-2-MRAP.
Product # :
PRO-2224Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LRPAP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (29-360 a.a) and having a molecular mass of 41.4kDa. LRPAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LRPAP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
LRPAP1 is a member of the alpha-2-MRAP family. LRPAP1 cooperates with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330. LRPAP1, located on the cell surface, creates a complex with the alpha 2 macroglobulin receptor light and heavy chains and has part in the pathogenesis of membrane glomerular nephritis.
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Synonyms
Low density lipoprotein-related protein-associated protein 1 (alpha-2-macroglobulin receptor-associated protein 1), A2MRAP, HBP44, RAP, A2RAP, Alpha-2-MRAP.
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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 MGSQPIAGHG GKYSREKNEP EMAAKRESGE EFRMEKLNQL WEKAKRLHLS PVRLAELHSD LKIQERDELN WKKLKVEGLD KDGEKEAKLI HNLNVILARY GLDGRKDAQM VHSNALNEDT QDELGDPRLE KLWHKAKTSG KFSSEELDKL WREFLHYKEK IQEYNVLLDT LSRAEEGYEN LLSPSDMAHI KSDTLISKHS ELKDRLRSIN QGLDRLRKVS HQGYGSTTEF EEPRVIDLWD LAQSANFTEK ELESFREELK HFEAKIEKHN HYQKQLEISH QKLKHVESIG DPEHISRNKE KYVLLEEKTK ELGYKVKKHL QDLSSRVSRA RHNEL.
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 :
Vaspin Human, HisDescription:
Vaspin Human Recombinant, His Tag
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Product # :
CYT-459Price :
Quantity :
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Shipped with Ice Packs
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Description
Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
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Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid Vaspin 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 MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.
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 :
REG3A HumanDescription:
Regenerating Islet-Derived 3 Alpha Human Recombinant
Regenerating islet-derived protein 3 alpha, Reg III-alpha, Pancreatitis-associated protein 1, REG3A, HIP, PAP, PAP1, REG3, INGAP, PAP-H, PBCGF, REG-III.
Product # :
PRO-421Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human REG3A protein is produced with N-terminal fusion of His Tag. The REG3A His -Tagged Fusion Protein is an 18.4 kDa protein containing 149 amino acid residues of the Human REG3A and 16 additional amino acid residues- His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Pancreatitis-associated protein (PAP) is a secretory protein not normally expressed in healthy pancreas but highly induced during acute pancreatitis. While PAP has been shown to be anti-bacterial and antiapoptotic in vitro, its definitive biological function in vivo is not clear. Using antisepse oligonucleotides, inhibition of PAP expression significantly worsened pancreatitis in a rat model. During pancreatitis, PAP released by the pancreas could mediate lung inflammation through induction of hepatic TNF- alpha expression and subsequent increase in circulating TNF-alpha.
PAP is activated in primary liver cancers. In normal liver, the protein is undetectable in normal mature hepatocytes and found only in some ductular cells, representing potential hepatic progenitor cells. PAP can be considered hepatic cytokine that combines mitogenic and anti-apoptotic functions regarding hepatocytes, and consequently acts as a growth factor in vivo to enhance liver regeneration. In pancreatic cancor, PAP was overexpressed in 79% (30 of 38) of pancreatic ductal adenocarcinoma, 19% (7 of 36) of chronic pancreatitis, and 29% (2 of 7) of mucinous cystadenoma. PAP was found in malignant ductular structures in pancreatic carcinomas as well as in benign proliferating ductules and acinar cells in chronic pancreatitis. Elevation of PAP in patients with pancreatic cancer is not merely explainable by concomitant pancreatitis, but seems to be due to increased PAP production by the cancer cells and is also correlated to tumour load as expressed by the UICC stages.
Epithelial expression of PAP was induced under intestinal mucosal inflammation initiated by exposure to commensal bacteria or DSS as well as inflamed IBD colon. Increased serum level of PAP diagnosed ileal location in active Crohn disease with a sensitivity of 60%, a specificity of 94%, a positive predictive value of 84% and a negative predictive value of 81%. Elevated serum PAP (> 50 ng/mL) is significantly associated with disease activity and ileal location of Crohn disease. -
Synonyms
Regenerating islet-derived protein 3 alpha, Reg III-alpha, Pancreatitis-associated protein 1, REG3A, HIP, PAP, PAP1, REG3, INGAP, PAP-H, PBCGF, REG-III.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/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 GMASHMEEPQ RELPSARIRC PKGSKAYGSH CYALFLSPKS WTDADLACQK RPSGNLVSVL SGAEGSFVSS LVKSIGNSYS YVWIGLHDPT QGTEPNGEGW EWSSSDVMNY FAWERNPSTI SSPGHCASLS RSTAFLRWKD YNCNVRLPYV CKFTD.
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Applications
Western blotting, ELISA.
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 :
Avidin ProteinDescription:
Avidin
Avidin, AVD, AVID.
Product # :
PRO-500Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).
Source
Hen's egg white.
Biological Activity
15.0 units/mg protein, 1 unit binds 1µg biotin.
More Info
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Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
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Synonyms
Avidin, AVD, AVID.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Avidin 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 Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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 :
RBP4 ProteinDescription:
Retinol Binding Protein-4 Human
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
Product # :
CYT-1218Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
RBP4 Human produced in Pooled human plasma can be used as a calibrator in immunoassays. Immunoreactivity was checked using monoclonal antibodies specific to RBP4.
Source
Human Plasma.
Formulation
RBP4 was lyophilized from PBS, 150mM NaCl, and 10mM K-phosphate, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Retinol Binding Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RBP4 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 RBP4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Retinol Binding Protein 4 (RBP4) is a multifunctional protein that plays a crucial role in the transport of retinol (vitamin A) in the bloodstream. Beyond its traditional role in vitamin A metabolism, RBP4 has emerged as a key player in various physiological processes and pathological conditions. This research endeavors to explore the diverse facets of RBP4 in human biology, shedding light on its physiological functions, regulatory mechanisms, and implications in health and disease.
Physiological Functions:
At its core, RBP4 acts as a carrier protein, shuttling retinol from the liver, where it is stored, to peripheral tissues where it is utilized. Retinol is vital for vision, immune function, growth, and development, making RBP4 an essential component in these processes. By regulating the availability of retinol, RBP4 contributes significantly to maintaining normal vision, immune responses, and cellular differentiation, particularly in epithelial tissues.
Metabolic Significance:
Research has unveiled RBP4’s role in metabolic regulation. It has been associated with insulin resistance, a hallmark of type 2 diabetes mellitus. Elevated RBP4 levels are observed in individuals with obesity and insulin resistance, implicating its involvement in metabolic disorders. Understanding the interplay between RBP4, insulin signaling, and glucose metabolism is crucial for deciphering the complexities of diabetes and metabolic syndrome.
Immunological Implications:
Beyond its metabolic functions, RBP4 has been implicated in immune responses. Studies have suggested its involvement in modulating inflammatory processes and immune cell functions. By influencing immune cell differentiation and cytokine production, RBP4 may play a role in both immune defense and autoimmune disorders. Investigating these immunological implications provides insights into the crosstalk between metabolic and immune pathways.
Genetic and Environmental Influences:
Genetic variations and environmental factors, such as diet and lifestyle, can impact RBP4 levels and functions. Research into these influences is essential for understanding individual susceptibility to metabolic disorders and inflammatory conditions. Genetic studies shed light on the hereditary aspects of RBP4 regulation, providing valuable information for personalized medicine approaches.
Clinical Relevance:
RBP4’s involvement in various diseases, including diabetes, cardiovascular diseases, and certain cancers, underscores its clinical relevance. It serves as a potential biomarker for metabolic dysregulation and a target for therapeutic interventions. Moreover, RBP4-targeted therapies are being explored for their potential in managing metabolic disorders and related complications.
Conclusion:
RBP4, once primarily recognized for its role in vitamin A transport, has evolved into a multifaceted protein with intricate roles in metabolism, immunity, and disease. Its functions extend far beyond being a mere carrier of retinol, influencing diverse physiological processes and serving as a nexus between metabolic health and immunological responses. Unraveling the complexities of RBP4 opens avenues for understanding diseases like diabetes and offers promising prospects for innovative therapies, emphasizing its significance in human biology and medicine.
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 :
SEMAXDescription:
SEMAX
Product # :
HOR-033Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SEMAX Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 813.92 Dalton and a Molecular formula of C37H51N19O1S.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SEMAX although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SEMAX 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 SEMAX 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
H-Met-Glu-His-Phe-Pro-Gly-Pro-OH.
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Background
Semax, also known as ACTH(4-10) Pro-Gly-Pro, is a synthetic peptide that has been the subject of extensive research due to its potential neuroprotective and nootropic effects. This heptapeptide, derived from the adrenocorticotropic hormone (ACTH), has been shown to possess a wide range of biological activities, including enhancing memory, learning, and neurogenesis.
Semax is unique in its ability to cross the blood-brain barrier and exert its effects directly on the central nervous system. It has been shown to stimulate the release of brain-derived neurotrophic factor (BDNF), a protein that plays a crucial role in the survival of neurons and the growth of new neurons and synapses. Studies by Dolotov et al. (2006) have demonstrated that Semax can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its nootropic effects, Semax has been shown to possess neuroprotective properties. Research by Stavchansky et al. (2008) found that Semax could protect neurons from oxidative stress and apoptosis, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its nootropic and neuroprotective effects, Semax has been proposed as a potential therapeutic agent for a variety of conditions, including cognitive disorders, stroke, and optic nerve disease. For instance, a study by Myasoedov et al. (2010) found that Semax could improve outcomes in patients with ischemic stroke, indicating its potential as a therapeutic agent in stroke recovery.
While research on Semax is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of Semax in humans. However, the existing body of research suggests that Semax could be a promising tool in the treatment of cognitive disorders and neurodegenerative diseases.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.