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1000 results found for “Prolactin PRL”
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Name :
PCCDescription:
Prothrombin Complex
PCC, Prothrombin Complex.
Product # :
PRO-439Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prothrombin complex is a double virus–inactivated concentrate, containing equal concentrations of Factors II, VIII, IX, X and Heparin.
Formulation
Lyophilized Powder from 0.1M sodium chloride and 10mM sodium citrate buffer.
More Info
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Introduction
Prothrombin Complex Concentrate (PCC) is a combination of several blood clotting factors II, VII, IX and X. PCC is used in the treatment of the congenital bleeding disorders associated with Factors II, VII, IX, and X deficiencies. PCC reverses the effect of warfarin (a coumarin anti-coagulant) and is used in cases of significant bleeding in patients with a coagulopathy, for example, gastrointestinal haemorrhage or intracranial haemorrhage. The PCC is also extensively used in treating acquired coagulation abnormalities secondary to vitamin K deficiency, warfarin ingestion, and various types of liver disease.
Hepatitis, anaphylaxis and thrombosis have been reported as complications of prothrombin complex concentrates administration. -
Synonyms
PCC, Prothrombin Complex.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prothrombin-Complex although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prothrombin-Complex 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 Prothrombin Complex in sterile 18MΩ-cm H2O.
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 :
Cys-Protein-LDescription:
Cys-Protein L Recombinant
Product # :
PRO-1933Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.
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 :
GHBP Human, Sf9Description:
Growth Hormone Binding Protein Human Recombinant, Sf9
GHR, GHBP, GHIP.
Product # :
CYT-1152Price :
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Description
GHBP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (19-264aa) and having a molecular mass of 29.4kDa.GHBP is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The GHBP solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone. The ED50 for this effect is equal or less than 10ng/ml.
More Info
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Introduction
Growth Hormone Binding Protein or GHR, is a protein, part of the cytokine receptor superfamily. GHR binds to 2 receptors, therefore it enhances signal transduction via dimerization of receptors. In elevated levels, growth hormone operates as an antagonist due to high variance in the binding sites affinities. The antagonist operation can be embellished even more when the binding site is reduced its affinity.
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Synonyms
GHR, GHBP, GHIP.
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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
FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT
CEEDFYLEHH 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.
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Name :
POLR3H HumanDescription:
Polymerase (RNA) III (DNA directed) Polypeptide H Human Recombinant
DNA-directed RNA polymerase III subunit RPC8, RNA polymerase III subunit C8, DNA-directed RNA polymerase III subunit H, RNA polymerase III subunit 22.9 kDa subunit, RPC22.9, POLR3H, KIAA1665, RPC8.
Product # :
PRO-1250Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
POLR3H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a.) and having a molecular mass of 25.3kDa (Molecular size on SDS-PAGE will appear higher).POLR3H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POLR3H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Polymerase (RNA) III (DNA directed) Polypeptide H(POLR3H) is a member of the eukaryotic RPB7/RPC8 RNA polymerase subunit family. POLR3H is DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA utilizing the 4 ribonucleoside triphosphates as substrates. POLR3H has a central role in sensing and curbing infection by intracellular bacteria and DNA viruses. POLR3H functions as nuclear and cytosolic DNA sensor which is involved in innate immune response.
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Synonyms
DNA-directed RNA polymerase III subunit RPC8, RNA polymerase III subunit C8, DNA-directed RNA polymerase III subunit H, RNA polymerase III subunit 22.9 kDa subunit, RPC22.9, POLR3H, KIAA1665, RPC8.
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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 MGSMFVLVEM VDTVRIPPWQ FERKLNDSIA EELNKKLANK VVYNVGLCIC LFDITKLEDA YVFPGDGASHTKVHFRCVVF HPFLDEILIG KIKGCSPEGV HVSLGFFDDI LIPPESLQQP AKFDEAEQVW VWEYETEEGA HDLYMDTGEE IRFRVVDESF VDTSPTGPSS ADATTSSEEL PKKEAPYTLV GSISEPGLGL LSWWTSN.
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 :
MAD2L1BP HumanDescription:
MAD2L1 Binding Protein Human Recombinant
MAD2L1-binding protein, Caught by MAD2 protein, MAD2L1BP, CMT2, KIAA0110, RP1-261G23.6.
Product # :
PRO-1052Price :
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Shipped with Ice Packs
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Description
MAD2L1BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-274 a.a) and having a molecular mass of 33.6kDa (Molecular weight on SDS-PAGE will appear higher).MAD2L1BP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAD2L1BP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MAD2L1-binding protein (MAD2L1BP) is a member of the MAD2L1BP family.MAD2L1BP is a binding protein of the MAD2 mitotic arrest deficient-like 1 (MAD2/MAD2L1). MAD2 is a fundamental factor of the spindle checkpoint which delays the onset of anaphase until all the kinetochores are connected to the spindle. The MAD2L1BP protein acts to curb the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 once it dissociated from the MAD2L1-CDC20 complex. For the duration of the cell cycle, MAD2L1BP levels increase and then remain constant until late mitosis after which they drop.
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Synonyms
MAD2L1-binding protein, Caught by MAD2 protein, MAD2L1BP, CMT2, KIAA0110, RP1-261G23.6.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAPEA EVLSSAAVPD LEWYEKSEET HASQIELLET SSTQEPLNAS EAFCPRDCMV PVVFPGPVSQ EGCCQFTCEL LKHIMYQRQQ LPLPYEQLKH FYRKPSPQAE EMLKKKPRAT TEVSSRKCQQ ALAELESVLS HLEDFFARTL VPRVLILLGG
NALSPKEFYE LDLSLLAPYS VDQSLSTAAC LRRLFRAIFM ADAFSELQAP PLMGTVVMAQ GHRNCGEDWF RPKLNYRVPS RGHKLTVTLS CGRPSIRTTA WEDYIWFQAP VTFKGFRE.
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 :
RELM g MouseDescription:
RELM-Gamma Mouse Recombinant
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Product # :
CYT-1035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
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Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse 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 RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.
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 :
RLN3 HumanDescription:
Relaxin-3 Human Recombinant
Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.
Product # :
PRO-2176Price :
Quantity :
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Shipped at Room temp
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Description
Relaxin-3 Human Recombinant produced in E.Coli is a disulfide-linked heterodimeric, non-glycosylated, polypeptide chain containing 24 amino acids for A chain and 27 amino acids for B chain and having a molecular mass of 2.5kDa for A chain and 3kDa for B chain.The Relaxin-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by cAMP accumulation in human THP-1 cells, is less than 17.5ng/ml.More Info
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Introduction
Relaxin-3 (RLN3) belongs to the relaxin family. Relaxins are endocrine and autocrine/paracrine hormones. Relaxin, which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. Unlike human Relaxins 1 and 2, Relaxin 3 does not seem to have a role in reproduction; however it is involved in stress response in the brain stem. RLN3 is the only known ligand for the G-protein-coupled receptor GPCR135, titled RXFP3. In addition, RLN3 binds the LGR7 (RXFP1) receptor, however with lower affinity than Relaxin-2. Even though binding of RLN3 to LGR7 increases intracellular cAMP, binding to GPCR135 suppresses cAMP accumulation, indicating coupling to Gi, Go, or Gz by this receptor.
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Synonyms
Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RLN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Relaxin-3 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 RLN3 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
A chain: DVLAGLSSSC CKWGCSKSEI SSLC.
B chain: RAAPYGVRLCG REFIRAVIFT CGGSRW.
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 :
RPS18 HumanDescription:
Ribosomal Protein S18 Human Recombinant
Ribosomal Protein S18, D6S218E, 40S Ribosomal Protein S18, HKE3, KE-3, KE3, S18, Rhabdomyosarcoma Antigen MU-RMS-40.21, Ke-3, Ke3.
Product # :
PRO-984Price :
Quantity :
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Shipped with Ice Packs
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Description
RPS18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (1-152 a.a) and having a molecular mass of 20.1kDa.RPS18 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RPS18 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
40S ribosomal protein S18 (RPS18) is a member of the ribosomal protein S13P family.RPS18 is located in the cytoplasm. Ribosomes, the organelles which catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit.Jointly these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS18 encodes a ribosomal protein which is a component of the 40S subunit. RPS18 is a recognized binding partner of Cofilin and has been proposed to be a novel substrate for CaMKII. Among the diseases associated with RPS18 are bowen-conradi syndrome, and pasteurellosis.
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Synonyms
Ribosomal Protein S18, D6S218E, 40S Ribosomal Protein S18, HKE3, KE-3, KE3, S18, Rhabdomyosarcoma Antigen MU-RMS-40.21, Ke-3, Ke3.
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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 MGSMSLVIPE KFQHILRVLN TNIDGRRKIA FAITAIKGVG RRYAHVVLRK ADIDLTKRAG ELTEDEVERV ITIMQNPRQY KIPDWFLNRQ KDVKDGKYSQ VLANGLDNKL REDLERLKKI RAHRGLRHFW GLRVRGQHTK TTGRRGRTVG VSKKK
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 :
BNP HumanDescription:
B-type Natriuretic Peptide Human
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-369Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
B-type Natriuretic Peptide Human is a polypeptide chain containing 32 amino acids and having a molecular mass of 3464 Dalton. The molecular formula is:C143H244N50O42S4.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by RP-HPLC.
More Info
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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution B-type Natriuretic Peptide 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 B-type Natriuretic Peptide 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
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
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Background
What is the molecular weight / Mw of BNP Human?
BNP Human has a total Mw of 3.4kDa.
What is the source or expression system of BNP Human?
Synthetic.
What is the Purity of BNP Human?
BNP Human is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BNP Human?
The biological functionality of BNP Human will be determined in the future.
What is the amino acid sequence of BNP Human?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
What applications can BNP Human Protein be used in?
BNP Human can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BNP Human?
The endotoxin level is minimal, BNP Human 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 :
PF 4 ProteinDescription:
Platelet Factor-4 Human (CXCL4)
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-234Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human PF-4 a 7.8 kDa protein consisting of 70 amino acid residues.
Source
Human Platelets.
Formulation
The CXCL4 protein was lyophilized in PBS buffer pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL4 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 four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.
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 :
DarbepoetinDescription:
Darbepoetin-Alpha Human Recombinant
Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.
Product # :
CYT-1263Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells(CHO).
Formulation
Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.More Info
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Introduction
Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.
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Synonyms
NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Darbepoetin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Darbepoetin 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 Darbepoetin 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
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.
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Background
What is the molecular weight/Mw of DARBEPOETIN Protein?
DARBEPOETIN Protein has a total Mw of 38.5kDa.
What is the source or expression system of DARBEPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).
What is the Purity of DARBEPOETIN Protein?
DARBEPOETIN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of DARBEPOETIN Protein?
The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.
What is the amino acid sequence of DARBEPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD
What applications can DARBEPOETIN Protein be used in?
DARBEPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DARBEPOETIN Protein?
The endotoxin level is minimal, DARBEPOETIN 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 :
Aprotinin ProteinDescription:
Aprotinin
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Product # :
PRO-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Source
Bovine Lung.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
More Info
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Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
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Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin 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 Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/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.
- View Data Sheet
Name :
TAGLN HumanDescription:
Transgelin Human Recombinant
SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.
Product # :
PRO-851Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TAGLN Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201 a.a.) and having a molecular mass of 24.8 kDa. The TAGLN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TAGLN Human solution containing 20mM Tris-HCl pH-7.5, 1mM DTT & 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TAGLN is a transformation and form-change responsive actin cross-linking/gelling protein that is part of the calponin family. TAGLN is expressed abundantly in fibroblasts and smooth muscle. TAGLN participates in calcium interactions and contractile properties of the cell that contribute to replicative senescence. Throughout embryogenesis, TAGLN is expressed in smooth, cardiac and skeletal muscle, but is limited during late fetal growth and adulthood to all vascular and visceral smooth muscle cells and low levels of expression in heart. TAGLN is downregulated in several transformed cell lines, showing that a decrease of TAGLN expression is an premature indicator of the onset of transformation.
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Synonyms
SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.
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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 MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG SNRGASQAGM TGYGRPRQII S.
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 :
PFN4 HumanDescription:
Profilin-4 Human Recombinant
PFN-4, Profilin-IV, Profilin4.
Product # :
PRO-818Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFN4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-129 a.a.) and having a molecular mass of 16.4 kDa. PFN4 protein is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
PFN4 Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PFN4 is a small actin-binding protein that participates in the dynamic turnover and restructuring of the actin cytoskeleton. PFN4 is localized in all eukaryotic organisms in the majority of cells. PFN4 is crucial for spatially and temporally controlled growth of actin microfilaments, which is a necessary process in cellular locomotion and cell shape changes.
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Synonyms
PFN-4, Profilin-IV, Profilin4.
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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 MSHLQSLLLD TLLGTKHVDS AALIKIQERS LCVASPGFNV TPSDVRTLVN GFAKNPLQAR REGLYFKGKD YRCVRADEYS LYAKNENTGV VVVKTHLYLL VATYTEGMYP SICVEATESL GDYLRKKGS.
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 :
STC 2 Human, HisDescription:
Stanniocalcin-2 Human Recombinant, His Tag
Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.
Product # :
HOR-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STC 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (25-302 a.a.) and having a molecular mass of 33kDa. STC 2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STC 2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.25M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.
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Synonyms
Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.
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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 MGSTDATNPP EGPQDRSSQQ KGRLSLQNTA EIQHCLVNAG DVGCGVFECF ENNSCEIRGL HGICMTFLHN AGKFDAQGKS FIKDALKCKA HALRHRFGCI SRKCPAIREM VSQLQRECYL KHDLCAAAQE NTRVIVEMIH FKDLLLHEPY VDLVNLLLTC GEEVKEAITH SVQVQCEQNW GSLCSILSFC TSAIQKPPTA PPERQPQVDR TKLSRAHHGE AGHHLPEPSS RETGRGAKGE RGSKSHPNAH ARGRVGGLGA QGPSGSSEWE DEQSEYSDIR R.
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 :
Glucagon Human, HisDescription:
Glucagon Human Recombinant, His Tag
Glucagon, GCG, GLP1, GLP2, GRPP.
Product # :
HOR-301Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
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Description
Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (90-180 a.a.) and having a molecular mass of 12.8kDa.Glucagon is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glucagon protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract. -
Synonyms
Glucagon, GCG, GLP1, GLP2, GRPP.
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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 MKRHDEFERH AEGTFTSDVS SYLEGQAAKE FIAWLVKGRG RRDFPEEVAI VEELGRRHAD GSFSDEMNTI LDNLAARDFI NWLIQTKITD RK.
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 :
NCR3LG1 HumanDescription:
Natural Cytotoxicity Triggering Receptor 3 Ligand 1 Human Recombinant
B7H6, B7-H6, B7 Homolog 6
Product # :
PRO-2762Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NCR3LG1 Human Recombinant produced in HEK is a single, glycosylated polypeptide chain containing 477 amino acids (25-262 a.a) and having a molecular mass of 53.6 kDa. NCR3LG1 is fused to a 239 amino acid hIgG-His tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 Cells
Formulation
NCR3LG1 protein solution (0.5mg/ml) containing 1X PBS (pH-7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured in a functional ELISA with Human NCR3. The ED50 range ≤500 ng/ml.
More Info
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Introduction
The B7 proteins are crucial in the regulation of the adaptive immune system. Among them is NCR3LG1. NCR3LG1 is part of the B7 family and is expressed on tumor cells. NCR3LG1 Interaction with NKp30 protein results in cytotoxicity and natural killer cell activation.Humans and rats have a single NCR3LG1 gene; though, numerous B7H6 genes were detected in a single large cluster in the Xenopus genome. NCR3LG1, a ligand for the NK cell activating receptor NKp30, targest to produce CAR that targets multiple tumor types. NCR3LG1 is expressed on many primary human tumors, including leukemia, lymphoma and gastrointestinal stromal tumors, though it is not constitutively expressed on normal tissues.
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Synonyms
B7H6, B7-H6, B7 Homolog 6
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
DLKVEMMAGG TQITPLNDNV TIFCNIFYSQ PLNITSMGIT WFWKSLTFDK EVKVFEFFGD HQEAFRPGAI VSPWRLKSGD ASLRLPGIQL EEAGEYRCEV VVTPLKAQGT VQLEVVASPA SRLLLDQVGM KENEDKYMCE SSGFYPEAIN ITWEKQTQKF PHPIEISEDV ITGPTIKNMD GTFNVTSCLK LNSSQEDPGT VYQCVVRHAS LHTPLRSNFT LTAARHSLSE TEKTDNFS
LE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PRNP HumanDescription:
Prion Protein Human Recombinant
ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.
Product # :
PRO-1400Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
PRNP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (23-230a.a) and having a molecular mass of 25kDa. GOSR2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PRNP protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Prion protein (PRNP) is a ubiquitous membrane glycoprotein whose abnormal self-replicating, misfolded form is widely believed to cause several central nervous system disorders, together known as Transmissible Spongiform Encephalopathies (TSE). PRNP contains a highly unstable region of five tandem octapeptide repeat. Mutations in PRNP protein’s repeat region as well as elsewhere have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru.
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Synonyms
ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.
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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 MKKRPKPGGW NTGGSRYPGQ GSPGGNRYPP QGGGGWGQPH GGGWGQPHGG GWGQPHGGGW GQPHGGGWGQ GGGTHSQWNK PSKPKTNMKH MAGAAAAGAV VGGLGGYVLG SAMSRPIIHF GSDYEDRYYR ENMHRYPNQV YYRPMDEYSN QNNFVHDCVN ITIKQHTVTT TTKGENFTET DVKMMERVVE QMCITQYERE SQAYYQRGS.
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 :
LHRH ProteinDescription:
Luteinizing Hormone Releasing Hormone Human Recombinant
LHRH, GRH, GNRH, LNRH.
Product # :
HOR-268Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
LHRH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (24-92 a.a.) and having a molecular mass of 10.3kDa.LHRH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LHRH protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GNRH1 also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
At the pituitary, GNRH1 stimulates the synthesis and secretion of the follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male. -
Synonyms
LHRH, GRH, GNRH, LNRH.
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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 MGSQHWSYGL RPGGKRDAEN LIDSFQEIVK EVGQLAETQR FECTTHQPRS PLRDLKGALE SLIEEETGQK KI.
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 ProteinDescription:
Adiponectin Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-280Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- sds-page
Description
The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).
Source
Escherichia Coli.
Formulation
Acrp30 protein solution contains Phosphate buffered saline pH 7.4 and 1mM DTT.
Purity
Acrp30 purity is greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN. -
Background
Adiponectin Human Recombinant: Unraveling its Potential in Therapeutic Applications
1. Abstract
This paper aims to deliver an extensive exploration into Adiponectin Human Recombinant, a vital adipokine implicated in a multitude of metabolic processes. By delving into the structure, biological roles, and signaling pathways of adiponectin, we elucidate its contribution to pathophysiological conditions. Moreover, we examine the potential therapeutic application of adiponectin in metabolic and cardiovascular diseases.
2. Introduction
Adiponectin, a protein predominantly secreted by adipose tissue, plays an integral part in regulating metabolic processes such as glucose regulation and fatty acid oxidation. Understanding the intricacies of adiponectin's actions could pave the way for innovative therapeutic interventions in diseases like obesity, diabetes, and cardiovascular disease.
3. Structure and Signaling of Adiponectin
Adiponectin is a 30kDa protein consisting of a collagen-like domain and a C-terminal globular domain. It signals through adiponectin receptors AdipoR1 and AdipoR2, which then activate several intracellular signaling pathways, including AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-α), regulating various metabolic processes.
4. Biological Functions of Adiponectin
Adiponectin has been shown to enhance insulin sensitivity, stimulate fatty acid oxidation, and exert anti-inflammatory effects. Additionally, it is involved in regulating energy homeostasis and has been linked to the regulation of food intake and body weight.
5. Adiponectin in Disease Pathology
Reduced levels of adiponectin have been associated with obesity, insulin resistance, type 2 diabetes, and cardiovascular disease. Moreover, adiponectin deficiency has been observed in metabolic syndrome, emphasizing the adipokine's crucial role in metabolic health.
6. Therapeutic Potential of Adiponectin
Given adiponectin's role in metabolic regulation, its potential as a therapeutic target is of considerable interest. Approaches to increase circulating adiponectin levels or enhance adiponectin signaling could offer potential therapeutic strategies for managing metabolic diseases and cardiovascular conditions.
7. Conclusion and Future Perspectives
While our understanding of adiponectin and its role in health and disease has greatly advanced in recent years, there is still much to uncover. Further research on the precise molecular mechanisms of adiponectin could pave the way for novel therapeutic approaches.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% 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?
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN..
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 :
Myostatin Propeptide HumanDescription:
Myostatin Propeptide Human Recombinant
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-448Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- More Info
Description
Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.
Source
Escherichia Coli.
Formulation
Lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.More Info
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Introduction
Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.
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Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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Physical Appearance
Sterile 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.
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Solubility
It is recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRR.
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 ProteinDescription:
Leptin Human Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-228Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist 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
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist 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 Rat Leptin Pegylated Quadruple Antagonist 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 a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. 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.
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 :
STC 1 HumanDescription:
Stanniocalcin-1 Human Recombinant
Stanniocalcin-1, STC, STC-1.
Product # :
HOR-259Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Stanniocalcin-1 Human Recombinant produced in 293 cell line is a single, glycosylated, polypeptide chain containing 240 amino acids and having a total molecular mass of 25.9 kDa. The Stanniocalcin contains 10 residues form the C-Terminal Flag- tag. Stanniocalcin is purified by proprietary chromatographic techniques.
Source
293 cell line (Human embryonic kidney).
Formulation
Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Stanniocalcin 1 (STC1) is the mammalian homologue of STC, which was originally identified as a calcium/phosphate-regulating hormone in bony fishes. In contrast, STC1 may play an autocrine and paracrine role with pleiotropic effects in mammals. It is expressed in a wide variety of tissues, but unexpectedly is not detected in the circulation under normal circumstances, which is possibly caused by its attaching to soluble and tethered forms of a high-affinity binding protein. STC-1 can affect calcium homeostasis, bone and muscle mass and structure, and angiogenesis through effects on osteoblasts, osteoclasts, myoblasts/myocytes, and endothelial cells in mouse model. Differential regulation of myocardial STC1 protein expression was reported in heart failure. In addition, STC1 may regulate calcium currents in cardiomyocytes and may contribute to the alterations in calcium homeostasis of the failing heart. STC1 was found to be a selective modulator of hepatocyte growth factor (HGF)-induced endothelial migration and morphogenesis, an inhibitor of macrophage chemotaxis and chemokinesis, suppressor of progesterone and luteinization inhibitor. Together with STC-2, it may play important roles in the processes of implantation and decidualization in the rat. In terminally differentiated adipocytes, it may function as a "survival factor", which contributes to the maintenance of the integrity of mature adipose tissue. In context with its possible role in gestation, a Big STC, a three highermolecular- mass variant has been described. STC1 was identified as one of hypoxia-responsive genes coupled to hypoxia-driven angiogenesis.
Current research indicates that STC-1 might be a useful molecular marker to detect tumor cells in blood and bone marrow from patients with various types of malignancies. -
Synonyms
Stanniocalcin-1, STC, STC-1.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized STC-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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
Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
THEAEQNDSV SPRKSRVAAQ NSAEVVRCLN SALQVGCGAF ACLENSTCDT DGMYDICKSF LYSAAKFDTQ GKAFVKESLK CIANGVTSKV FLAIRRCSTF QRMIAEVQEE CYSKLNVCSI AKRNPEAITE VVQLPNHFSN RYYNRLVRSL LECDEDTVST IRDSLMEKIG PNMASLFHIL QTDHCAQTHP RADFNRRRTN EPQKLKVLLR NLRGEEDSPS HIKRTSHESA ASDYKDDDDK.
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.