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Name :
HirudinDescription:
Hirudin Recombinant
Product # :
PRO-362Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Hirudin is derived from yeast and the polypeptide chain contains 65 amino acids and its Mw is 6979.5 Dalton which is identical to natural Hirudin except for the substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63.The Recombinant Hirudin is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Each mg of protein was lyophilized from a sterile solution containing 20mM PBS pH-7 and 2% mannitol.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity was found to be >14,000ATU/mg.More Info
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Introduction
Recombinant Hirudin is a potent thrombin inhibitor originally derived from the medicinal leech. Hirudin acts directly on thrombin rather than through other clotting factors. The mechanism of Hirudin-thrombin appears to be unique. The conversion of fibrinogen into fibrin by the serine protease enzyme thrombin is a major event in the final stages of blood coagulation. In the final stages of coagulation prothrombinase converts prothrombin into thrombin. Fibrin is subsequently cross linked by factor XIII to form a blood clot. The primary inhibitor of thrombin in normal blood circulation is antithrombin III. The anticoagulatant activity of hirudin is derived from its ability to inhibit the pro-coagulant activity of thrombin (similar to antithrombin III activity). Hirudin is the strongest natural inhibitor of thrombin. Hirudin binds to and inhibits only the activity of thrombin forms with a specific activity on fibrinogen contrasting to antithrombin III activity. Therefore, hirudin has a thrombolytic activity since it prevents or dissolves the formation of clots and thrombi. Hirudin also has therapeutic significance in blood coagulation disorders, in the treatment of skin hematomas and of superficial varicose veins. Hirudin does not hinder with the biological activity of other serum proteins and can also act on complexed thrombin, thus having an advantage over more common anticoagulants and thrombolytics. It is complicated to extract large quantities of hirudin from natural sources; therefore a method for producing and purifying hirudin using recombinant biotechnology has been developed.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hirudin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hirudin 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 Hirudin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Placental Lactogen OvineDescription:
Placental Lactogen Ovine Recombinant
Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.
Product # :
CYT-512Price :
Quantity :
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Shipped at Room temp
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Description
Placental Lactogen Ovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Placental Lactogen Ovine is biologically active as evidenced by inducing proliferation of Nb2 cells.More Info
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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Ovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors. -
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Placental Lactogen Ovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Gln-His-Pro-Pro.
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Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LDL HumanDescription:
Low-Density Lipoprotein Human
Low Density Lipoprotein, LDL.
Product # :
PRO-562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Human Low Density Lipoprotein (LDL) produced in Human plasma.
Source
Human plasma.
More Info
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Introduction
LDL is a low-density lipoprotein that transports cholesterol and triglycerides from the liver to peripheral tissues. LDL (like all lipoproteins) facilitates the movement of fats and cholesterol within the water based solution of the blood stream. Each natural LDL particle contains a single Apo B-100 molecule (apolipoprotein B-100 is a protein with 4536 amino acid residues) that circulates the fatty acids and keeps them soluble in the aqueous environment. Additionally, the LDL core is highly-hydrophobic, consisting of linoleate (a polyunsaturated fatty acid) and about 1500 esterified cholesterol molecules. This core is enclosed by a shell of phospholipids and unesterified cholesterol in addition to a single copy of B-100 large protein (514 kD). Even though the LDL particles are approximately 22 nm in diameter and have a mass of about 3 million Daltons, they have a mass and size distribution since the LDL particles contain a varying number of fatty acids. LDL receptors are synthesized and placed in the plasma membrane when a cell requires cholesterol. The LDL receptors scatter freely until they link to clathrin-coated pits. LDL particles in the blood stream attach to these extracellular LDL receptors. The clathrin-coated pits at that time form vesicles that are endocytosed into the cell. Once the clathrin coat is dropped, the vesicles transport the LDL and their receptors to early endosomes, onto late endosomes to lysosomes. At this point the cholesterol esters in the LDL are hydrolysed. The LDL receptors are recovered back to the plasma membrane. Since LDLs convey cholesterol to the arteries and can be retained there by arterial proteoglycans initializing the formation of plaques, increased levels are linked to atherosclerosis, and thus heart attack, stroke, and peripheral vascular disease. And so, cholesterol within LDL lipoproteins is habitually called "bad" cholesterol. This is a misconception since the cholesterol transported on LDL is the same as the one transported on other lipoprotein particles, it is in itself not "bad", rather it is how and where the cholesterol is being transported, and in what amounts ultimately, which causes adverse effects. HDL / LDL ratio can give an indication of risk for arteriosclerosis.
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Synonyms
Low Density Lipoprotein, LDL.
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Physical Appearance
Yellow to orange liquid.
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Stability
Human LDL although stable at 4°C for 1 week, should be stored below -15°C (short term i.e. < 3 months) and below -70°C for long term.Human LDL can be further diluted with saline + 15% sucrose.
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Human Virus Test
Starting material donor tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies and Syphilis, HIV1 / HCV / HBV NAT.
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 b MouseDescription:
RELM-Beta Mouse Recombinant
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
Product # :
CYT-413Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Mouse RELM-b Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 8.9kDa. The Mouse RETNLB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) protein solution containing 10mM Acetic Acid with 2:1 mannitol to protein.
Purity
Greater than 97% as determined by SDS-PAGE.
More Info
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Introduction
RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice. -
Synonyms
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
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Physical Appearance
Brownish lyophilized powder.
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Stability
Lyophilized RETNLB is stable at -20°C. After reconstitution the protein should be kept at all times at -20°C. It is recommended to add a carrier protein (0.1% HSA or BSA) for long term storage.
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Solubility
Reconstitute at 0.1 mg/ml with sterile pyrogen free water.
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Amino Acid Sequence
MQCSFESLVD QRIKEALSRQ EPKTISCTSV TSSGRLASCP AGMVVTGCAC GYGCGSWDIR NGNTCHCQCS VMDWASARCC RMA.
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 :
CLEC7A HumanDescription:
C-Type Lectin Domain Family 7, Member A Human Recombinant
BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.
Product # :
PRO-2634Price :
Quantity :
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Shipped with Ice Packs
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Description
CLEC7A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 183 amino acids (71-244 a.a) and having a molecular mass of 21kDa. CLEC7A is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CLEC7A solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
C-type lectin domain family 7 member A 1 or CLEC7A is a protein, that in the innate immune system, acts against fungal pathogens. CLEC7A can be found in the immune system response cells such as monocytes, macrophages & neutrophils, or in dendritic and T cells. The protein is enhanced by macrophages by using GM-CSF, IL-4, or IL-13, or diminishes by dexamethasone, IL-10 and LPS.
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Synonyms
BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.
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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
ADPRHNSGRN PEEKDNFLSR NKENHKPTES SLDEKVAPSK ASQTTGGFSQ SCLPNWIMHG KSCYLFSFSG NSWYGSKRHC SQLGAHLLKI DNSKEFEFIE SQTSSHRINA FWIGLSRNQS EGPWFWEDGS AFFPNSFQVR NTVPQESLLH NCVWIHGSEV YNQICNTSSY SICEKELHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACTHDescription:
Adrenocorticotropic Hormone
Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.
Product # :
HOR-279Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Molecular formula of Adrenocorticotropic Hormone is C136H210N40O31S and the molecular weight is 2933.5 Dalton.
Formulation
The ACTH hormone was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Adrenocorticotropic hormone, as its name implies, stimulates the adrenal cortex. More specifically, it stimulates secretion of glucocorticoids such as cortisol, and has little control over secretion of aldosterone, the other major steroid hormone from the adrenal cortex. Stimulates secretion of adrenal corticosteroids and induces growth of adrenal cortex. ACTH also called Tetracosactide directly activates G-proteins. A stimulator of adenylate cyclase and cAMP formation.
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Synonyms
Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Adrenocorticotropic Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACTH 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 ACTH 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
Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-OH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAOC LeishmaniaDescription:
Maoc Family Dehydratase-Like Protein Recombinant
Product # :
PRO-2761Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Leishmania Donovani Maoc Family Dehydratase-Like Protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids having a molecular mass of 18 kDa. The Maoc Family Dehydratase-Like Protein is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PBS.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Maoc Family Dehydratase-Like Protein Recombinant although although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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 :
CRHBP HumanDescription:
Corticotropin Releasing Hormone Binding Protein Human Recombinant
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
Product # :
HOR-267Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CRHBP Human Recombinant is a 34.58 kDa protein containing 308 aa and fused to a 10 aa N-Terminal His-tag. CRHBP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRHBP Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.
More Info
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Introduction
CRH is a powerful stimulator of synthesis and secretion of preopiomelanocortin-derived peptides. CRH concentration in the human peripheral circulation is usually low. The concentration rises during pregnancy and fall back quickly after parturition. Maternal plasma CRH most likely originates from the placenta. Human plasma has a CRH-binding protein that inactivates CRH and can inhibit inappropriate pituitary-adrenal stimulation in pregnancy.
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Synonyms
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
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Physical Appearance
Filtered white lyophilized powder.
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Stability
Store lyophilized protein at -20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL
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Applications
ELISA, 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 :
LIF MouseDescription:
Leukemia Inhibitory Factor Mouse Recombinant
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-645Price :
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Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.02% Tween-20.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Activity of murine LIF was determined by the M1 cell differentiation assay which was found to be < 0.01 ng/ml, corresponding to a specific activity of 100,000,000 IU/mg.
A standard of 50 Units is defined as the concentration of mouse LIF in 1.0 mL of tissue culture medium that induces the differentiation of 50% of M1 colonies.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFP NNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNP TAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQR KKLGCQLLGTYKQVISVVVQAF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
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Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GH CarpDescription:
Growth Hormone Carp Recombinant
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-297Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Carp Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids & having a molecular mass of 21,408 Dalton. Growth Hormone Carp is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GH Carp was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Carp GH is biologically active in rat 3T3 F442A preadipocytes, though its activity is 15-fold lower compared to bovine GH, but it is equally potent in vivo in promoting carp growth (Fine et al.1993). Furthermore, carp GH forms 1:2 complex with the extra cellular domain of ovine growth hormone receptor.More Info
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Introduction
Growth-Hormone is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Carp recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Hormone Carp should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Growth Hormone Carp recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and found to be Ser-Asp-Asn-Gln-Arg.
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 :
GH HumanDescription:
Growth Hormone Human Recombinant
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-202Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids and having a molecular mass of 22kDa. Growth Hormone is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GH protein lyophilized from a 0.2µm filtered concentrated solution containing mannitol, and glycine.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation assay of rat lymphoma NB2-11 cells and was found to be less than 0.1ng/ml.
More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGH 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 HGH 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
FPTIPLSRLF DNAMLRAHRL HQLAFDTYQE FEEAYIPKEQ KYSFLQNPQT SLCFSESIPT PSNREETQQK SNLELLRISL LLIQSWLEPV QFLRSVFANS LVYGASDSNV YDLLKDLEEG IQTLMGRLED GSPRTGQIFK QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FSTL1 HumanDescription:
Follistatin Like 1 Human Recombinant
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.
Product # :
CYT-792Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
FSTL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 309 amino acids (21-308) and having a molecular mass of 34.9 kDa.FSTL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The FSTL1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
FSTL1 protein resembles follistatin, an ACTV-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
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Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.
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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 MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.
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Background
What is the molecular weight/Mw of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein has a total Mw of 34.9kDa.
What is the source or expression system of FSTL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FSTL1 HUMAN Protein?
The biological functionality of FSTL1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of FSTL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.
What applications can FSTL1 HUMAN Protein be used in?
FSTL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FSTL1 HUMAN Protein?
The endotoxin level is minimal, FSTL1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LYVE1 Human 25-235 a.a.Description:
Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1 (25-235 a.a) Human Recombinant
HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
Product # :
PKA-349Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LYVE1 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 229 amino acids and having a molecular mass of 24.8 kDa. As a result of glycosylation, the LYVE1 migrates on SDS-PAGE at approximately 50 kDa. LYVE1 is expressed with 15 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
High Five insect cells.
Formulation
The LYVE1 protein solution contains 20mM Tris buffer pH-7.5 and 10% Glycerol.
Purity
Greater than 90.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
More Info
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Introduction
LYVE1 is a selective marker of the lymphatic endothelium & a surface endocytic receptor for both soluble and immobilized hyaluronan, LYVE1 is an extracellular glycosaminoglycan that plays a role in cell adhesion and migration. LYVE1 functions in lympathic hyaluronan transport and is involved in tumor metastasis. Recombinant human LYVE1 was expressed in and purified by conventional chromatography techniques. The normal adult human choroid is endowed with a significant number of LYVE-1 positive macrophages. LYVE-1 is expressed in a reticulum cell neoplasm in an axillary lymph node. This reticulum cell sarcoma is a lymphatic sinus lining cell sarcoma which might represent another subtype of reticulum cell sarcomas.
LYVE-1 immunohistochemistry is a functional method for detecting lymphatics invaded by cancer cells, and detailed examination of the submucosa around the tumor is important for predicting LN metastasis. -
Synonyms
HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing 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
DPLRAEELS IQVSCRIMGI TLVSKKANQQ LNFTEAKEAC RLLGLSLAGK DQVETALKAS FETCSYGWVG DGFVVISRIS PNPKCGKNGV GVLIRKVPVS RQFAAYCYNS SDTWTNSCIP EIITTKDPIF NTQTATQTTE FIVSDSTYSV ASPYSTIPAP TTTPPAPAST SIPRRKKLIC VTEVFMETST MSTETEPFVE NKAAFKNEAA GFGGSGRLVP RGSHHHHHH.
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 :
GHBP OvineDescription:
Growth Hormone Binding Protein Ovine Recombinant
GHR, GHBP, GH receptor, Somatotropin receptor.
Product # :
CYT-470Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Binding Protein Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 244 amino acids and having a molecular mass of 28 kDa. GHBP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GHBP was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
fully biologically active as evidenced by its ability of forming 2:1 complex with Human GH.
More Info
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Introduction
GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.
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Synonyms
GHR, GHBP, GH receptor, Somatotropin receptor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Binding Protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHBP 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 GHBP Ovine in DDW or sterile 0.4% NaHCO3 adjusted to pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions preferably in presence of carrier proteins such as BSA or HSA.
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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-Phe-Ser-Gly-Ser.
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 :
KRT18 BovineDescription:
Cytokeratin-18 Bovine
Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.
Product # :
PRO-2785Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
KRT18 Bovine having a calculated molecular mass of 45 kDa, pI-5.4.
Source
Bovine liver.
Formulation
KRT18 was lyophilized from a 1mg/ml solution containing 30mM Tris/HCI pH 8, 9M urea, 2mM EDTA, 2mM DTT and 10mM methylammonium chloride.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized KRT18 between 2-8°C, do not freeze. Upon reconstitution KRT18 should be stored at -20°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized KRT18 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
Keratin-18 (K18) is an intermediate filament protein that plays a vital role in maintaining the structural integrity of epithelial cells. Extensive research has been conducted on K18 in human and murine models, shedding light on its functions and implications for various epithelial tissues.
However, the study of K18 in bovine tissues is an emerging area with potential for advancing our understanding of epithelial cell biology and its applications in veterinary medicine and biotechnology. Bovine tissues, such as the liver and gastrointestinal tract, are of particular interest due to their relevance in cattle production and food safety.
This research aims to provide a comprehensive exploration of K18 in bovine tissues, elucidating its functions, structural significance, and potential applications.
The primary objective of this research is to elucidate the role of K18 in bovine tissues, particularly in maintaining the structural integrity of epithelial cells.In vitro and ex vivo experiments, utilizing bovine epithelial cell cultures and tissue specimens, will be conducted to investigate how K18 contributes to cellular morphology, cytoskeletal organization, and tissue resilience. Understanding these mechanisms is fundamental for deciphering the complexities of epithelial cell biology in bovine species.
The second objective is to assess the relevance of bovine K18 in veterinary medicine and cattle production. Studies involving bovine models will be conducted to evaluate the impact of K18 mutations or variations on tissue health, disease susceptibility, and meat quality. These investigations may provide valuable insights into potential applications in cattle breeding and food safety.
The third objective is to explore the potential biotechnological applications of bovine K18. Research will investigate the use of K18-expressing bovine cells as models for studying epithelial-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.
By delving into the functions and roles of K18 in bovine tissues, this research aims to expand our knowledge of epithelial cell biology, its implications for veterinary medicine, and its potential applications in biotechnology and cattle production.
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 :
EledoisinDescription:
Eledoisin
Product # :
PRO-281Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Eledoisin’s molecular weight is 1188.4 having an amino acid sequence of Glp-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2 and a molecular formula of C54H85N13O15S.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Eledoisin is an undecapeptide formed in the venom gland of several species of octopuses and is used as a vasodilator and a contraction agent of extravascular smooth muscle.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eledoisin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Eledoisin 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 Eledoisin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Procalcitonin RhesusDescription:
Procalcitonin Rhesus Recombinant
Calcitonin.
Product # :
HOR-016Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Procalcitonin Rhesus Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Asn140) containing 125 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 14kDa.
Source
Escherichia Coli.
Formulation
Procalcitonin was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Calcitonin.
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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. Procalcitonin 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
MKHHHHHHASAPFRSALESS PDPATLSEEE ARLLLAALVQ DYVQMKASEL EQEQETEGSS LDSPRSKRCG NLSTCMLGTY TQDFNKFHTF PQTAIGVGAP GKKRDMSSDL ERNRRRYVSM PQDAN.
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 :
Prealbumin HumanDescription:
Transthyretin Human
TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.
Product # :
PRO-2740Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Transthyretin dimer protein produced in Human plasma having a molecular mass of 30kD. Under certain conditions it may be shown as a monomer (15kD) or a tetramer (60kD).
Source
Human serum.
Formulation
The protein was lyophilized (0.2 µm filtered) from 20mM NH4HCO3.
Purity
Greater than 96.0%.
More Info
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Introduction
Prealbumin is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. Prealbumin is a carrier protein which transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Transthyretin consists of a tetramer of identical subunits and is dominantly produced in the liver. Mutations in Prealbumin are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, and carpal tunnel syndrome. Prealbumin is an indicator of protein-energy malnutrition since it has a circulating half life of 2 days and reacts swiftly to changes in nutritional status.
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Synonyms
TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Prealbumin Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized Prealbumin Human in phosphate buffer pH > 7 containing 0.15M NaCl.
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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Parvovirus B19, Syphilis and HIV/HBV/HCV (PCR).
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 :
OT HumanDescription:
Oxytocin Human
OT, OXT, OT-NPI, Neurophysin 1, MGC126890, MGC126892.
Product # :
HOR-254Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Oxytocin Human Synthetic is a single, non-glycosylated, polypeptide chain containing 9 amino acids and having a molecular mass of 1007.2 Dalton. Oxytocin has a molecular formula of C43H66N12O12S2. The OT is purified by proprietary chromatographic techniques.
Formulation
The Oxytocin was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Introduction
Human Oxytocin stimulates uterine smooth muscle contractions indirectly and stimulates the mammary glands to increase lactation without increasing the production of milk.
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Synonyms
OT, OXT, OT-NPI, Neurophysin 1, MGC126890, MGC126892.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oxytocin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neurophysin 1 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 Oxytocin 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-Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2.
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 :
LanreotideDescription:
Lanreotide
Product # :
HOR-282Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lanreotide is an octapeptide, an analogue of a naturally occurring hormone, somatostatin.
Formulation
The protein (1mg/ml) was lyophilized with 5mg manntitol and 0.04mg tween-80.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Lanreotide is a peptide inhibitor of a number of endocrine, neuroendocrine, exocrine and paracrine functions. It shows good affinity for peripheral somatostatin receptors (anterior pituitary and pancreatic). In contrast, its affinity for central receptors is much lower. This profile confers a good specificity of action at the level of growth hormone and digestive hormone secretion. Lanreotide shows a much longer duration of action than natural somatostatin. In addition, its marked selectivity for the secretion of growth hormone, compared to that of insulin, makes it a suitable candidate for the treatment of acromegaly. By inhibiting the synthesis of thyroid stimulating hormone (TSH), lanreotide also normalised thyroid function of patients with thyrotrophin secreting adenomas in 50% (8/16) of the per-protocol population treated for 6 months. There was no significant reduction in the size of the adenoma. Furthermore, the inhibitory action of lanreotide on intestinal exocrine secretion, d
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Lanreotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lanreotide 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 Lanreotide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Adipsin HumanDescription:
Complement Factor D Human Recombinant
Complement factor D, EC 3.4.21.46, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD, ADN.
Product # :
PRO-1360Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Adipsin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (26-253 a.a) and having a molecular mass of 26.6kDa.Adipsin is fused to a 21 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
Adipsin protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% 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, EC 3.4.21.46, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD, ADN.
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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 MILGGREAEA HARPYMASVQ LNGAHLCGGV LVAEQWVLSA AHCLEDAADG KVQVLLGAHS LSQPEPSKRL YDVLRAVPHP DSQPDTIDHD LLLLQLSEKA TLGPAVRPLP WQRVDRDVAP GTLCDVAGWG IVNHAGRRPD SLQHVLLPVL DRATCNRRTH HDGAITERLM CAESNRRDSC KGDSGGPLVC GGVLEGVVTS GSRVCGNRKK PGIYTRVASY AAWIDSVLA.
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 :
SIGLEC6 HumanDescription:
Sialic Acid Binding Ig Like Lectin 6 Human Recombinant
Sialic Acid Binding Ig Like Lectin 6, Obesity-Binding Protein 1, CD33 Antigen-Like 1, CDW327, CD33L1, CD33L, OBBP1, Sialic Acid Binding Ig-Like Lectin 6, Sialic Acid-Binding Ig-Like Lectin 6, CD327 Antigen, Siglec-6, CD33L2, OB-BP1, CD327, SIGLEC6.
Product # :
PRO-2450Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
SIGLEC6 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-347a.a.) and having a molecular mass of 62.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC6 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SIGLEC6 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Sialic acid-binding Ig-like lectin 6 isoform 1 (SIGLEC6) is a member of immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC6 mediates sialic-acid dependent binding to cells and binds to alpha-2, 6-linked sialic acid. The SIGLEC6 protein localizes in numerous compartments such as membrane fraction, extracellular region and so on. The SIGLEC6 receptor binds sialyl-TN glycans and leptin. Placental expression SIGLEC6 is upregulated in preeclampsia.
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Synonyms
Sialic Acid Binding Ig Like Lectin 6, Obesity-Binding Protein 1, CD33 Antigen-Like 1, CDW327, CD33L1, CD33L, OBBP1, Sialic Acid Binding Ig-Like Lectin 6, Sialic Acid-Binding Ig-Like Lectin 6, CD327 Antigen, Siglec-6, CD33L2, OB-BP1, CD327, SIGLEC6.
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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
ADLQERRFQL EGPESLTVQE GLCVLVPCRL PTTLPASYYG YGYWFLEGAD VPVATNDPDE EVQEETRGRF HLLWDPRRKN CSLSIRDARR RDNAAYFFRL KSKWMKYGYT SSKLSVRVMA LTHRPNISIP GTLESGHPSN LTCSVPWVCE QGTPPIFSWM SAAPTSLGPR TTQSSVLTIT PRPQDHSTNL TCQVTFPGAG VTMERTIQLN VSYAPQKVAI SIFQGNSAAF KILQNTSSLP VLEGQALRLL CDADGNPPAH LSWFQGFPAL NATPISNTGV LELPQVGSAE EGDFTCRAQH PLGSLQISLS LFVHWKPEGR AGGVLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EG VEGF HumanDescription:
Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant
PK1, PRK1, Prokineticin 1, EG-VEGF.
Product # :
CYT-338Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
More Info
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Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
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Synonyms
PK1, PRK1, Prokineticin 1, EG-VEGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF 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 Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
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Background
Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications
Abstract:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.Introduction:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.Production and Characterization:
Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.Role in Endocrine Disorders:
EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.Therapeutic Implications:
Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.Conclusion:
Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.7kDa.
What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.
What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EG-VEGF Protein?
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF 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.