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1000 results found for “Erythropoietin”
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Name :
PTH (7-84) HumanDescription:
Parathyroid Hormone (7-84) Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-011Price :
Quantity :
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Shipped at Room temp
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Description
PTH (7-84) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids, having an MW of 8.8kDa. The PTH (7-84) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
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Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTH (7-84) although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTH (7-84) should be stored at 4C between 2-7 days and for future use below -18C.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 PTH (7-84) 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
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 6 HumanDescription:
Interleukin-6 Human Recombinant
B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Product # :
CYT-213Price :
Quantity :
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Shipped at Room temp
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Description
Interleukin-6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 21000 Dalton. The IL6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine 7TD1 cells is less than 0.1 ng/ml, corresponding to the specific activity of 1.0 x 10,000,000 Units per mg.More Info
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Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
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Synonyms
B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-6 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Val-Pro-Pro.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.47 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-6 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
il 18 HumanDescription:
Interleukin-18 Human Recombinant
IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
Product # :
CYT-269Price :
Quantity :
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Shipped at Room temp
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Description
Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 18.2 kDa. The IL-18 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
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Synonyms
IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin 18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL18 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin 18 in sterile PBS at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED
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Background
Also known as IFN-gamma inducing factor, Interleukin-18 or IL18 is a protein. In humans this protein is encoded by the IL18 gene. The protein is a proinflammatory cytokine.
Mechanism
The levels of IL-18 in the human body are increased at sites of inflammation. This includes cases of rheumatoid arthritis as well as other similar conditions. Osteoblastic cells express the protein and it is capable of inhibiting osteoclast formation. It is able to do this through a variety of mechanisms.
For instance, it is able to stimulate GM-CSF. This is created by T cells and is a response to treatment using IL-18. As well as this, the cytokine does stimulate INF-y production through vivo in bone. Furthermore, the impact on bone resorption and osteoclastogenesis is increased when used in conjunction with IL-12 treatment. Studies have shown that IL-18 provides an indirect stimulus on osteoclastogenesis due to the effect it has on T lymphocytes.
Furthermore, evidence has shown that IL-18 does increase the production of OPG. This was studied in research on transgenic mice that overexpressed IL-18. In these cases osteoclasts decreased as did bone mass. This suggested that IL-18 also has an impact on bone growth.
Interactions
Research has also explored the different interactions of IL-18 on other proteins. This includes the interaction between IL-18 and IL-18R. This has been shown to decrease the power of protective immunity and increase pathogenic responses during an infection involving intracellular bacteria. This interaction suggests that the presence or absence of IL-18R signal does impact the pathogenic compared to protective immunity.
Another interaction between interleukin 19 and Astrocyte has shown that it can improve neuropathic pain processing following nerve injury. It is proposed this is due to the fact that the nociceptive signals in the spinal cord are augmented due to this reaction.
Function
Belonging to the IL-1 superfamily, this cytokine is produced by macrophages as well as various other cells. It operates after binding with the interleukin-18 receptor. Working with IL-12, the protein is then able to induce-cell mediated immunity after an infection from lipopolysaccharide and other microbial products.
Once stimulated by IL-18 other cells including natural killer and T cells then release IFN-y. This type II IFN plays a crucial part in activating the macrophages of various other cells.
Together IL12 and IL-18 are able to successfully inhibit IgE and IG1 production that is dependent on IL-4. As well as this, the protein is also able to increase IgG2a production through B cells. IL-18 will interact specifically with this type of cytokine and has a negative impact on regulation of biological activity.
Structure
Many researchers have suggested that the structure of IL-18 is a key way to understand it’s receptor activation mechanism. The structure of IL-18 closely resembles of IL-1 and has various similarities. It is folded into a beta-trefoil structure and three sites have been shown to be important for receptor activation. These were revealed through extensive mutagenesis. Two of the sites provide binding sites for the IL-18 receptor and are located in positions similar to IL-1. The third structure seems to be used for IL-18 receptor beta binding.
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 :
GDF11 Human, HisDescription:
Growth and Differentiation factor 11 Human Recombinant, His Tag
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
Product # :
CYT-887Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
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Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
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Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.
What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 12 p40 Human BaculovirusDescription:
Interleukin-12 p40 Human Recombinant, Baculovirus
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
Product # :
CYT-134Price :
Quantity :
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Shipped with Ice Packs
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Description
IL 12 p40 Human Recombinant produced in Hi-5 cell using Baculovirus is a single polypeptide chain containing 315 amino acids (23-328) and having a molecular mass of 35.8kDa.IL 12 p40 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Baculovirus
Formulation
The IL 12 p40 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT, 100mM PMSF and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
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Synonyms
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
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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
ADPIWELKKD VYVVELDWYP DAPGEMVVLT CDTPEEDGIT WTLDQSSEVL GSGKTLTIQV KEFGDAGQYT CHKGGEVLSH SLLLLHKKED GIWSTDILKD QKEPKNKTFL RCEAKNYSGR FTCWWLTTIS TDLTFSVKSS RGSSDPQGVT CGAATLSAER VRGDNKEYEY SVECQEDSAC PAAEESLPIE VMVDAVHKLK YENYTSSFFI RDIIKPDPPK NLQLKPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KSKREKKDRV FTDKTSATVI CRKNASISVR AQDRYYSSSW SEWASVPCSH HHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Adiponectin (108-244) HumanDescription:
Adiponectin (108-244 a.a.) Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-073Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
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Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% 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? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..
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 :
Flt3 Ligand MouseDescription:
Flt3 Ligand Mouse Recombinant
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Product # :
CYT-340Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Flt3-Ligand Mouse Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 163 amino acids and having a molecular mass of 18.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FLT3L Mouse protein was lyophilized from sterile filtered solution containing 10mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.
More Info
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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt-3 Ligand 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 Flt3l Mouse recombinant 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
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.
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Background
What is the molecular weight/Mw of FLT3 LIGAND MOUSE Protein?
FLT3 LIGAND MOUSE Protein has a total Mw of 18.6kDa.
What is the source or expression system of FLT3 LIGAND MOUSE Protein?
Escherichia Coli.
What is the Purity of FLT3 LIGAND MOUSE Protein?
FLT3 LIGAND MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND MOUSE Protein?
The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.
What is the amino acid sequence of FLT3 LIGAND MOUSE Protein?
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.
What applications can FLT3 LIGAND MOUSE Protein be used in?
FLT3 LIGAND MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND MOUSE Protein?
The endotoxin level is minimal, FLT3 LIGAND MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
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.
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Name :
Ganirelix peptideDescription:
Ganirelix
Product # :
HOR-276Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Ganirelix acetate is a synthetic decapeptide with high antagonistic activity against naturally occurring gonadotropin-releasing hormone (GnRH). Ganirelix acetate is derived from native GnRH with substitutions of amino acids at positions 1, 2, 3, 6, 8, and 10 to form the following molecular formula of the peptide: N-acetyl-3-(2-napthyl)-D-alanyl-4-chloro-D-phenylalanyl-3-(3-pyridyl)-D-alanyl-L-seryl-L-tyrosyl-N 9 ,N 10 -diethyl- D-homoarginyl-L-leucyl-N 9 ,N 10 -diethyl-L-homoarginyl-L-prolyl-D-alanylamide acetate. The molecular weight for Ganirelix acetate is 1570.4 Dalton as an anhydrous free base.
Formulation
The Ganirelix hormone (0.5mg/ml) contains 0.1mg acetic acid and 23.5mg mannitol pH-5.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Ganirelix should be stored between 2°C- 8°C at all time. DO NOT FREEZE.
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Background
What is the molecular weight/Mw of GANIRELIX PEPTIDE Protein?
GANIRELIX PEPTIDE Protein has a total Mw of 1.57kDa.
What is the Purity of GANIRELIX PEPTIDE Protein?
GANIRELIX PEPTIDE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GANIRELIX PEPTIDE Protein?
The biological functionality of GANIRELIX PEPTIDE Protein will be determined in the future.
What applications can GANIRELIX PEPTIDE Protein be used in?
GANIRELIX PEPTIDE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GANIRELIX PEPTIDE Protein?
The endotoxin level is minimal, GANIRELIX PEPTIDE 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 :
Insulin Human, HisDescription:
Insulin Human Recombinant, His Tag
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Product # :
CYT-1076Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Insulin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (25-110 a.a) and having a molecular mass of 11.8kDa. Insulin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Insulin protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using MCF7 human breast cancer cell. The ED50 for this effect is less or equal to 4 ug/ml.
More Info
-
Introduction
Insulin decreases blood glucose concentration. it increases cell permeability to monosaccharides, amino acids and fatty acids. it accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
-
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFVNQHLC GSHLVEALYL VCGERGFFYT PKTRREAEDL QVGQVELGGG PGAGSLQPLA LEGSLQKRGI VEQCCTSICS LYQLENYCN
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 :
Holo Transferrin HumanDescription:
Holo Transferrin Human Recombinant
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-2844Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page, activity
Description
Human Holo Transferrin Recombinant produced in HEK Cells is a glycosylated polypeptide containing 679 amino acids and having a Mw of of 76 kDa.
Source
HEK Cells
Formulation
The protein was lyophilized from 1x PBS pH-7.4.
Purity
Protein is >98% pure as determined by 10% PAGE (coomassie staining).
Biological Activity
The activity of Recombinant Holo Transferrin was determined by the proliferation assay using MDCK cells stimulated with recombinant human Holo Transferrin. The protein was found biologically activesds-page, activity
More Info
-
Introduction
Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.
-
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
-
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
-
Stability
Store the lyophilized Holo Transferrin recombinant between 2-8°C, do not freeze.
Upon reconstitution Holo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Holo Transferrin recombinant in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VPDKTVRWCA VSEHEATKCQ SFRDHMKSVI PSDGPSVACV KKASYLDCIR AIAANEADAV TLDAGLVYDA YLAPNNLKPV VAEFYGSKED PQTFYYAVAV VKKDSGFQMN QLRGKKSCHT GLGRSAGWNI PIGLLYCDLP EPRKPLEKAV ANFFSGSCAP CADGTDFPQL CQLCPGCGCS TLNQYFGYSG AFKCLKDGAG DVAFVKHSTI FENLANKADR DQYELLCLDN TRKPVDEYKD CHLAQVPSHT VVARSMGGKE DLIWELLNQA QEHFGKDKSK EFQLFSSPHG KDLLFKDSAH GFLKVPPRMD AKMYLGYEYV TAIRNLREGT CPEAPTDECK PVKWCALSHH ERLKCDEWSV NSVGKIECVS AETTEDCIAK IMNGEADAMS LDGGFVYIAG KCGLVPVLAE NYNKSDNCED TPEAGYFAVA VVKKSASDLT WDNLKGKKSC HTAVGRTAGW NIPMGLLYNK INHCRFDEFF SEGCAPGSKK DSSLCKLCMG SGLNLCEPNN KEGYYGYTGA FRCLVEKGDV AFVKHQTVPQ NTGGKNPDPW AKNLNEKDYE LLCLDGTRKP VEEYANCHLA RAPNHAVVTR KDKEACVHKI LRQQQHLFGS NVTDCSGNFC LFRSETKDLL FRDDTVCLAK LHDRNTYEKY LGEEYVKAVG NLRKCSTSSL LEACTFRRP.
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 :
ENTPD3 Human, sf9 BioactiveDescription:
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
Product # :
ENZ-1020Price :
Quantity :
Shipping Method :
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Description
ENTPD3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 451 amino acids (44-485a.a.) and having a molecular mass of 50.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ENTPD3 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.
Biological Activity
Specific activity is > 250,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze ATP per minute at pH 7.5 at 37C.More Info
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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
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Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.
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 :
EPHB1 HumanDescription:
EPH Receptor B1 Human Recombinant
EPHB-1, Ephrin type-B receptor 1, Eph Receptor B1, ELK, EPH tyrosine kinase 2, EPH-like kinase 6, EK6, hEK6, HEK6, Neuronally-expressed EPH-related tyrosine kinase, NET, NETHek6, Tyrosine-protein kinase receptor EPH-2, EPHT2, soluble EPHB1 variant 1
Product # :
PRO-2728Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EPHB1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 529 amino acids (18-540 a.a) and having a molecular mass of 59.2 kDa.EPHB1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The EPHB1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human EFNB1 (cat# pro-2543).
More Info
-
Introduction
EPH Receptor B1 (EPHB1) is a member of the ephrin receptor subfamily of the proteintyrosine kinase family which 16 receptors are known. EPHB1 binds ephrin-B2, ephrin-B1,ephrin‑A3,ephrin-A1,ephrin-B3 and ephrin-A4. EPHB1 binds tyrosine kinase and phosphorylates syndecan-2 and thisphosphorylation is necessary for syndecan-2 clustering and spine formation. Ephrin receptors and theirligands (the ephrins) mediate several developmental processes, mainly in the nervous system.
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Synonyms
EPHB-1, Ephrin type-B receptor 1, Eph Receptor B1, ELK, EPH tyrosine kinase 2, EPH-like kinase 6, EK6, hEK6, HEK6, Neuronally-expressed EPH-related tyrosine kinase, NET, NETHek6, Tyrosine-protein kinase receptor EPH-2, EPHT2, soluble EPHB1 variant 1
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MEETLMDTRT ATAELGWTAN PASGWEEVSG YDENLNTIRT YQVCNVFEPN QNNWLLTTFI NRRGAHRIYT EMRFTVRDCS SLPNVPGSCK ETFNLYYYET DSVIATKKSA FWSEAPYLKV DTIAADESFS QVDFGGRLMK VNTEVRSFGP LTRNGFYLAF QDYGACMSLL SVRVFFKKCP SIVQNFAVFP ETMTGAESTS LVIARGTCIP NAEEVDVPIK LYCNGDGEWM VPIGRCTCKP GYEPENSVAC KACPAGTFKA SQEAEGCSHC PSNSRSPAEA SPICTCRTGY YRADFDPPEV ACTSVPSGPR NVISIVNETS IILEWHPPRE TGGRDDVTYN IICKKCRADR RSCSRCDDNV EFVPRQLGLT ECRVSISSLW AHTPYTFDIQ AINGVSSKSP FPPQHVSVNI TTNQAAPSTV PIMHQVSATM RSITLSWPQP EQPNGIILDY EIRYYEKEHN EFNSSMARSQ TNTARIDGLR PGMVYVVQVR ARTVAGYGKF SGKMCFQTLT DDDYKSELRE QLPHHHHHH
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 :
GlycininDescription:
Allergen Ara h 3.0101 Recombinant
Glycinin, Arah3.
Product # :
ALR-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.
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Synonyms
Glycinin, Arah3.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
F8 ProteinDescription:
Coagulation Factor-VIII Human Recombinant
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Product # :
PRO-318Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Antihemophilic Facor Human Recombinant produced in CHO is a glycosylated polypeptide chain having 2332 amino acids. The Factor-VIII is purified by proprietary chromatographic techniques.
Source
CHO cells (Chinese Hamster Ovarian Cells).
Formulation
Each 250IU vial was lyophilized from a solution containing 8mg Tween-80, 112mM NaCl, 40mg Mannitol, 10mg Trehalose, 1ng VWF and 4.2mM CaCl2.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 7,058 IU/mg.More Info
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Introduction
Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
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Synonyms
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Factor-VIII although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIII 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 250IU lyophilized Factor-VIII in 5ml sterile 18M-cm H2O, 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 :
MG HumanDescription:
Menopausal Gonadotropin Human
Product # :
HOR-251Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Menopausal Gonadotropin Human is produced from a sterile preparation of placental glucoprotein urine of post-menopausal women.The MG is purified by proprietary chromatographic techniques.
Source
Urine of post-menopausal women.
Formulation
The Human MG was lyophilized from a concentrated (1mg/ml) solution with no additives.
Biological Activity
100 IU/mg of FSH and 100 IU/mg LH.More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Menopausal Gonadotropin Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MG 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 MG 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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Contaminants
Free of: HbsAg, Hepatitis B surface antigen and antibodies to HIV, Hepatitis C and HIV.
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 :
Ferritin Human, FTLDescription:
Ferritin Human Recombinant, Light Chain
Ferritin, FTL, MGC71996, Ferritin light chain.
Product # :
PRO-650Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Ferritin Human Recombinant Light Chain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20 kDa.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ferritin is a fairly large, iron-storage heteropolymeric protein composed of 2 subunit types, light Ferritin & heavy Ferritin polypeptides, which is expressed in most kinds of cells and co-assemble in different proportion in a tissue-specific manner. Ferritin is composed of 24 self-assembled polypeptide subunits of the heavy and light ferritin chains and is characterized by the capacity to remove Fe from solution in the presence of oxygen.
Ferritin light polypeptide protein is the main intracellular iron storage protein in prokaryotes and eukaryotes. Variation in ferritin subunit composition influence the rates of iron uptake and release in various tissues. A key function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyper ferrit anemia-cataract syndrome.
Ferritin stores iron in a soluble, nontoxic, readily accessible form. Ferritin is needed for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after it has been oxidized. -
Synonyms
Ferritin, FTL, MGC71996, Ferritin light chain.
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Physical Appearance
Sterile Filtered solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MSSQIRQNYS TDVEAAVNSL VNLYLQASYT YLSLGFYFDR DDVALEGVSH FFRELAEEKR EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA MALEKKLNQA LLDLHALGSA RTDPHLCDFL ETHFLDEEVK LIKKMGDHLT NLHRLGGPEA GLGEYLFERL TLKHD.
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 :
RetatrutideDescription:
Retatrutide
Product # :
HOR-058Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Retatrutide is a synthetic single, non-glycosylated polypeptide chain containing 39 amino acids, having a molecular mass of 4731 Dalton and a Molecular formula of C221H342N46O68.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Retatrutide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Retatrutide 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 Retatrutide 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-Tyr-Aib-Gln-Gly-Thr-Phe-Thr-SerAsp-Tyr-Ser-Ile-α-Me-Leu-Leu-Asp-Lys-{diacid-C20-gamma-Glu- (AEEA)-Lys}-Ala-Gln-Aib-Ala-Phe-Ile-Glu-Tyr-Leu-Leu-Glu-Gly-GlyPro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser-NH2.
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Background
Retatrutide is atriple agonist targeting the GIP, GLP-1, and glucagon receptors which offers a distinct metabolic profile that goes beyond previous dual agonists like Tirzepatide. Retatrutide takes a very important part in metabolic pharmacotherapy, achieving high weight loss of nearly 30% in Phase 3 trials. Retatrutide’s triple-receptor agonism—mainly the inclusion of the glucagon receptor—provides a superior metabolic advantage in clearing liver fat and increasing thermogenesis compared to dual agonists.
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 HumanDescription:
Leptin Antagonist Quadruple Mutant Human Recombinant
Product # :
CYT-353Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was 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 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Quadruple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NEFL HumanDescription:
Neurofilament Light Human Recombinant
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Product # :
PRO-2584Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- More Info
Description
NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).
Source
Escherichia Coli.
Formulation
NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.
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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
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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 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.
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 :
PON1 Human, HEKDescription:
Paraoxonase-1 Human Recombinant, HEK
Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5
Product # :
ENZ-1154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
PON1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (16-355 a.a) containing a total of 346 amino acids, having a molecular mass of 39.0kDa. PON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PON1 solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500 pmol/min/ug. Defined by the amount of enzyme that hydrolyzes 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37˚C.
More Info
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Introduction
Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.
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Synonyms
Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5
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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
LFRNHQSSYQ TRLNALREVQ PVELPNCNLV KGIETGSEDL EILPNGLAFI SSGLKYPGIK SFNPNSPGKI LLMDLNEEDP TVLELGITGS KFDVSSFNPH GISTFTDEDN AMYLLVVNHP DAKSTVELFK FQEEEKSLLH LKTIRHKLLP NLNDIVAVGP EHFYGTNDHY FLDPYLQSWE MYLGLAWSYV VYYSPSEVRV VAEGFDFANG INISPDGKYV YIAELLAHKI HVYEKHANWT LTPLKSLDFN TLVDNISVDP ETGDLWVGCH PNGMKIFFYD SENPPASEVL RIQNILTEEP KVTQVYAENG TVLQGSTVAS VYKGKLLIGT VFHKALYCEL 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.
- View Data Sheet
Name :
GHBP HumanDescription:
GHBP Human Recombinant
Product # :
CYT-238Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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- formulation
- purity
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Description
GHBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids and having a molecular mass of 28107.01 Dalton. GHR 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) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
GHBP is fully biologically active as evidenced by its ability of forming 2:1 complex with G.H.
More Info
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Introduction
GHBP is a transmembrane receptor for GH. Binding of GH 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 GH 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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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GHBP 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 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
AFSGSEATAAILSRAPWSLQSVNPGLKTNS SKEPKFTKCRSPERETFSCHWTDEVHHGTK
NLGPIQLFYTRRNTQEWTQEWKECPDYVSA GENSCYFNSSFTSIWIPYCIKLTSNGGTVD
EKCFSVDEIVQPDPPIALNWTLLNVSLTGI HADIQVRWEAPRNADIQKGWMVLEYELQYK
EVNETKWKMMDPILTTSVPVYSLKVDKEYE VRVRSKQRNSGNYGEFSEVLYVTLPQMSQF
TCEEDFYF. -
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GHBP as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MX2 HumanDescription:
Myxovirus Resistance 2 Human Recombinant
Myxovirus (Influenza Virus) Resistance 2 (Homolog Of Mouse), Myxovirus Resistance Protein 2, P78-Related Protein.
Product # :
PRO-1837Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MX2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (626-715) and having a molecular mass of 14.9 kDa. MX2 is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The MX2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MX2 is a member of 2 protein families: the dynamin family and the large GTPases family. MX2 has a cytoplasmic and nuclear structure which is found in a granular pattern in the heterochromatin region under the nuclear envelope. The nuclear form has a NLS (nuclear localization signal) at the amino terminal end however it is missing in the cytoplasmic form as a result of the use of a different translation start codon. MX2 is upregulated by IFN-a, but unlike myxovirus resistance protein 1 has no antiviral activity.
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Synonyms
Myxovirus (Influenza Virus) Resistance 2 (Homolog Of Mouse), Myxovirus Resistance Protein 2, P78-Related Protein.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSIGIH LNAYFLETSK RLANQIPFII QYFMLRENGD SLQKAMMQIL QEKNRYSWLL QEQSETATKR RILKERIYRL TQARHALCQF SSKEIH
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 :
BDNF HumanDescription:
Brain-Derived Neurotrophic Factor Human Recombinant
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-207Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
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- Activity
Description
BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.
Purity
BDNF is greater than 950% as determined SDS-PAGE.
Biological Activity
The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mLActivity
More Info
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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF 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
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
Escherichia Coli.
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.
What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.