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1000 results found for “Sclerostin”
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Name :
HCST HumanDescription:
Hematopoietic Cell Signal Transducer Human Recombinant
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
Product # :
PRO-2522Price :
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Shipped with Ice Packs
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Description
HCST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 271 amino acids (20-48 a.a.) and having a molecular mass of 30.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).HCST is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HCST protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HCST (Hematopoietic Cell Signal Transducer) is part of the DAP10 family. HCST is capable of being a part of an immunoreceptor complex. HCST takes a vital part in inducing cytotoxicity against MHC class I chain-associated MICA & target cells expressing cell surface ligands such as UL16-binding protein (ULBP) & MICB. HCST complex participates in proliferation as well as cell survival by activating T & NK cell responses.
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Synonyms
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc 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
ADPTTPGERS SLPAFYPGTS GSCSGCGSLS LPLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Activin B HumanDescription:
Activin-B Human Recombinant
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Product # :
CYT-058Price :
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Description
Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
Synonyms
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B 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
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG
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Background
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.
What is the source or expression system of Activin B Protein?
Nicotinia
What is the Purity of Activin B Protein?
Activin B Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin B Protein?
The biological functionality of Activin-B Protein will be determined in the future.
What is the endotoxin level for Activin B Protein?
The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG
What applications can ACTIVIN B Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
SCGB1A1 Human, HisDescription:
Uteroglobin Human Recombinant, His Tag
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Product # :
CYT-752Price :
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Shipped at Room temp
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Description
Uteroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 9.2kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
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Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
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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. SCGB1A1 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
MKHHHHHHASEICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.
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 :
TSLPR Human, Sf9Description:
Thymic Stromal Lymphopoietin Receptor Human Recombinant, Sf9
Cytokine receptor-like factor 2, CRLF2, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, Thymic stromal lymphopoietin protein receptor, TSLP receptor, CRL2, ILXR, TSLPR, Cytokine receptor-like factor 2 isoform 1, CRLF2Y.
Product # :
CYT-995Price :
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Shipped with Ice Packs
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Description
TSLPR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 218 amino acids (23-231) and having a molecular mass of 25.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).TSLPR is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TSLPR protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.
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Synonyms
Cytokine receptor-like factor 2, CRLF2, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, Thymic stromal lymphopoietin protein receptor, TSLP receptor, CRL2, ILXR, TSLPR, Cytokine receptor-like factor 2 isoform 1, CRLF2Y.
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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
ADPQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SKHHHHHH.
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 :
LGALS8 MouseDescription:
Galectin-8 Mouse Recombinant
Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.
Product # :
CYT-185Price :
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Shipped with Ice Packs
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Description
LGALS8 mouse Recombinant produced E. coli is a single polypeptide chain containing 339 amino acids (1-316) and having a molecular mass of 38kDa.LGALS8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is ≤ 2ug/ml. Measured by its ability to agglutinate human red blood cells.
SDS-PAGE
More Info
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Introduction
LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.
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Synonyms
Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.
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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 MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW. -
Background
What is the molecular weight/Mw of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein has a total Mw of 38kDa.
What is the source or expression system of LGALS8 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS8 MOUSE Protein?
The biological functionality of LGALS8 MOUSE Protein will be determined in the future.
What is the amino acid sequence of LGALS8 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW.
What applications can LGALS8 MOUSE Protein be used in?
LGALS8 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS8 MOUSE Protein?
The endotoxin level is minimal, LGALS8 MOUSE Protein was purified using conventional chromatography techniques.
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Assay Conditions
1. Mix equal volumes of human blood and Alsever’s solution (pH 7.0). (Alsever’s solution: NaCl 0.42g, Sodium citric acid 0.8g, Citric acid 0.055g, D-glucose 2.05g in DW100 ml).2. Centrifuge at 15000rpm for 10 minutes and wash 4 times with PBS.3. Dilute packed cells in a 0.5mg/ml trypsin-EDTA solution to give 4% red cell suspension.4. Incubate for 1 hour at 37°C and wash 4 times with PBS.5. Dilute packed cells in PBS to give a 4% red cell suspension.6. Load 50µl of 0.5%BSA-in-0.15M-NaCl solution and 25µl of 4%-Red-Cell-in-PBS in U shaped wells.7. Add 25µl of serial diluted galectin protein in PBS to each well plate (Round bottom 96 well plate).8. Incubate for 30 minutes at room temperature to observe visible agglutination.
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 :
CHST5 HumanDescription:
Carbohydrate Sulfotransferase 5 Human Recombinant
Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.
Product # :
ENZ-1165Price :
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Description
CHST5 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (27-395 a.a.) and having a molecular mass of 42.9kDa.CHST5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CHST5 protein solution (0.25mg/ml) containing 20% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 10,000 pmol/min/ug, and is defined as the amount of enzyme that sulfate from PAPS to Nacetyl-D-glucosamine per minute at pH 7.5, at 37˚C.
More Info
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Introduction
Carbohydrate Sulfotransferase 5 (CHST5) is a Golgi-embedded enzyme that is found in B cells, T cells and intestinal epithelium and is also mediates sulfation of keratan in cornea. CHST5 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine residues of keratan. CHST5 works on the non-reducing terminal GlcNAc of short andlong carbohydrate substrates that have poly-N-acetyllactosamine structures.
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Synonyms
Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.
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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
ADPEFSRQVP SSPAGLGERV HVLVLSSWRS GSSFVGQLFS QHPDVFYLME PAWHVWDTLS QGSAPALHMA VRDLIRSVFL CDMDVFDAYL PWRRNISDLF QWAVSRALCS PPVCEAFARG NISSEEVCKP LCATRPFGLA QEACSSYSHV VLKEVRFFNL QVLYPLLSDP ALNLRIVHLV RDPRAVLRSR EQTAKALARD NGIVLGTNGT WVEADPRLRV VNEVCRSHVR IAEAALHKPP PFLQDRYRLV RYEDLARDPL TVIRELYAFT GLGLTPQLQT WIHNITHGSG PGARREAFKT TSRDALSVSQ AWRHTLPFAK IRRVQELCGG ALQLLGYRSV HSELEQRDLS LDLLLPRGMD SFKWASSTEK QPESHHHHHH
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 :
Clusterin CanineDescription:
Clusterin Canine Recombinant
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J.
Product # :
CYT-549Price :
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Shipped at Room temp
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- sds-page
Description
Apolipoprotein-J canine Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain (Asn227~Glu445) and having a molecular mass of 30 kDa.
The protein is fused to His tag at N-Terminus.
The Apolipoprotein-J canine is purified by proprietary chromatographic techniques.Source
Escherichia Coli.
Formulation
Canine Clusterin was lyophilized from 20mM Tris, 150mM NaCl, pH8.0, 0.01% skl and 5%Trehalose.
Purity
Greater than 90% as determined by SDS PAGE.
sds-page
More Info
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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Reconstitute in 20mM Tris and 150mM NaCl (pH8.0) to a concentration of 0.1-1.0 mg/mL and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
NIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE.
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 30kDa.
What is the source or expression system of CLUSTERIN Protein?
Escherichia Coli.
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
NIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE.
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN 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 :
VEGF D HumanDescription:
Vascular Endothelial Growth Factor D Human Recombinant
c-fos induced growth factor (vascular endothelial growth factor D), FIGF, VEGFD.
Product # :
CYT-045Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
VEGFD Human Recombinant produced in HEK-293 cells is a secreted protein (amino acids Phe93-Ser201) fused to a polyhistidine tag at the C-terminus.
Source
HEK293.
Formulation
The recombinant VEGF-D was lyophilized after extensive dialysis against PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of human microvascular endothelial cells (HMVECs).More Info
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Introduction
VEGF-D belongs to the VEGF/PDGF family of proteins. VEGF-D promotes lymphangiogesis, endothelial cell growth, and regulates vascular permeability. In addition, VEGF-D has an important part in the creation of the venous and lymphatic vascular systems and in the growth and maintenance of differentiated lymphatic endothelium Mature VEGF-D forms a noncovalently linked homodimer, and binds to and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4).
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Synonyms
c-fos induced growth factor (vascular endothelial growth factor D), FIGF, VEGFD.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGF-D although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-D 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 Vascular Endothelial Growth Factor D in sterile 18M-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.
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Name :
RELT HumanDescription:
RELT Human Recombinant
RELT, TNF Receptor, Receptor Expressed In Lymphoid Tissues, Tumor Necrosis Factor Receptor Superfamily Member 19L, RELT Tumor Necrosis Factor Receptor, TNFRSF19L, Tumor Necrosis Factor Receptor Superfamily, Member 19-Like, TRLT.
Product # :
CYT-1101Price :
Quantity :
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Shipped with Ice Packs
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Description
RELT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 376 amino acids (26-162a.a.) and having a molecular mass of 41.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).RELT is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RELT protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
RELTis expressed in hematopoietic tissues and peripheral blood leukocytesand is a part of thetumor necrosis factor receptor superfamily. RELT mediates activation of NF-kappa-B and takes part in T-cell activation.overexpression of RELT in HEK-293 cells induces p38 and JNK signalling and leads to apoptosis. it can also costimulate T-cell proliferation in the presence of CD3 signalling.
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Synonyms
RELT, TNF Receptor, Receptor Expressed In Lymphoid Tissues, Tumor Necrosis Factor Receptor Superfamily Member 19L, RELT Tumor Necrosis Factor Receptor, TNFRSF19L, Tumor Necrosis Factor Receptor Superfamily, Member 19-Like, TRLT.
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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
STTLWQCPPG EEPDLDPGQG TLCRPCPPGT FSAAWGSSPC QPHARCSLWR RLEAQVGMAT
RDTLCGDCWP GWFGPWGVPR VPCQPCSWAPLGTHGCDEWG RRARRGVEVA AGASSGGETR QPGNGTRAGG PEETAAQVEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 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 :
Leptin Human, HisDescription:
Leptin Human Recombinant, His Tag
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.
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Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin tA HumanDescription:
Leptin Antagonist Triple Mutant Human Recombinant
Product # :
CYT-352Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant 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 triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected 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.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, 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 0.88 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 :
IGF1 Human Des1-3Description:
Insulin-Like Growth Factor 1 Des (1-3) Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
Product # :
CYT-518Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IGF-I Des(1-3) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids (aa 4-70) and having a molecular mass of 7368.5 Dalton. IGF-1 Des1-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) was lyophilized was lyophilized from a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.
Purity
Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×105 units/mg.More Info
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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF-I des(1-3) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 des-1-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the IGF-I des(1-3) 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
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.
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Background
What is the molecular weight/Mw of IGF1 HUMAN DES1-3 Protein?
IGF1 HUMAN DES1-3 Protein has a total Mw of 7.3kDa.
What is the source or expression system of IGF1 HUMAN DES1-3 Protein?
Escherichia Coli.
What is the Purity of IGF1 HUMAN DES1-3 Protein?
IGF1 HUMAN DES1-3 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 HUMAN DES1-3 Protein?
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×105 units/mg.
What is the amino acid sequence of IGF1 HUMAN DES1-3 Protein?
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.
What applications can IGF1 HUMAN DES1-3 Protein be used in?
IGF1 HUMAN DES1-3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 HUMAN DES1-3 Protein?
The endotoxin level is minimal, IGF1 HUMAN DES1-3 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 :
Prolactin Ovine AntagonistDescription:
Prolactin Ovine Antagonsit Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-311Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prolactin Ovine Antagonist Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 23kDa. Ovine Prolactin Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Ovine Prolactin was lyophilized from a concentrated (1mg/ml) solution with 0.02%-0.03% NaHCO3.
Purity
Greater than 99.0% as determined by SDS-PAGE.
Biological Activity
Ovine Prolactin Antagonist is devoid of agonistic activity and capable of inhibiting biological activity of Ovine Prolactin or other lactogenic hormones as evidenced by proliferation assay of Nb2 or other cells.More Info
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Introduction
Prolactin is a lactogenic hormone secreted by the adenohypophysis .Besides its major action on lactation, in some species prolactin exerts effects on reproduction, maternal behavior, fat metabolism, immunomodulation and osmoregulation.Prolactin has been shown also to have cytokine-like activities and to have important immunoregulatory activities. It contributes to the development of lymphoid tissues and the maintenance of physiological immune function and also modulates a variety of T-cell immune responses. Prolactin has been reported to activate cellular proliferation in nonreproductive tissue, such as liver, spleen, and thymus. It induces significant proliferation in aortic smooth muscle cells and also enhances proliferation of these cells induced by PDGF . Prolactin also appears to be directly mitogenic for pancreatic beta cells. Prolactin is also mitogenic for cultured astrocytes.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Ovine Prolactin Antagonist although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Ovine Prolactin Antagonist 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 Ovine Prolactin Antagonist 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-Thr-Pro-Val-Cys-Pro.
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 :
GlucagonDescription:
Glucagon Human
GLP1, GLP2, GRPP.
Product # :
HOR-286Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Glucagon Human Synthetic is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton and the molecular formula is: C153H225N43O49S.The Glucagon is purified by proprietary chromatographic techniques.
Formulation
Glucagon peptide was formulated with no additives.
Purity
Greater than 96.0% as determined by RP-HPLC.
More Info
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Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (?-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract. -
Synonyms
GLP1, GLP2, GRPP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Glucagon although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Glucagon 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 Glucagon in a sterile 1% HCl solution at a concentration of 0.1-1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-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.
- View Data Sheet
Name :
Colloidal GoldDescription:
Colloidal Gold 40nM 2OD
Product # :
PRO-2830Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Gold nanoparticles have one-of-a-kind properties turn them to ideal for detecting even the smallest amounts of biological molecules. These particles can be loaded with drugs or other therapeutic agents and then targeted to specific cells/tissues. Further to their diagnostic applications, gold nanoparticles may also take part in drug delivery and cancer therapy. Colloidal Gold is purified by proprietary chromatographic techniques.
Formulation
Colloidal Gold solution (6.7mg/ml) contains 50mM sodium citrate.
More Info
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Physical Appearance
Sterile Filtered red solution.
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Stability
Colloidal Gold should be stored at 4°C, DO NOT FREEZE.
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Background
Colloidal gold is liquid form colloid nanoparticles of gold in a water. The colloidal gold color is dependent of the particle size, below 100 nm gives a is deep purple red color due to the spherical nanoparticles. Colloid gold is crucial for research due to its unique properties such as electronic charge, Mw and optical properties. Colloid gold is used in biomedical devices, electron microscopy and nanotechnology.
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 :
NRG1 A HumanDescription:
Neuregulin-1/Heregulin Alpha (EGF Domain) Human Recombinant
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
Product # :
CYT-736Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 65 amino acids and having a total molecular mass of 7.4kDa. NRG1-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 6.0 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 40 ng/ml, corresponding to a specific activity of > 2.5×104 units/mg.More Info
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Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms act to induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.
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Synonyms
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NRG1-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-A 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 NRG1-A 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
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK.
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 :
IL 1RA RatDescription:
Interleukin-1 Receptor Antagonist Rat Recombinant
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Product # :
CYT-152Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.5kDa.The IL 1RA Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.More Info
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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
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Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL 1RA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1RA 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 IL 1RA 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
HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ
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 :
Betacellulin MouseDescription:
Betacellulin Mouse Recombinant
Betacellulin, Probetacellulin.
Product # :
CYT-131Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
BTC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids and having a molecular mass of 9.0kDa. The BTC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.
More Info
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Introduction
BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Synonyms
Betacellulin, Probetacellulin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BTC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC 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 BTC Mouse Recombinant 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
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY
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Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9kDa.
What is the source or expression system of BETACELLULIN Protein?
Escherichia Coli.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.
What is the amino acid sequence of BETACELLULIN Protein?
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LAIR2 HumanDescription:
Leukocyte-Associated Ig-Like Receptor 2 Human Recombinant
Leukocyte-associated immunoglobulin-like receptor 2, LAIR-2, CD306, LAIR2.
Product # :
PRO-1081Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- More Info
Description
LAIR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (22-135 a.a) and having a molecular mass of 15.2kDa.LAIR2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAIR2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Leukocyte-associated immunoglobulin-like receptor 2 (LAIR2) is a secreted, 131 amino acids protein which contains one IglikeC2 type domain, rendering it a member of the Ig superfamily. Even though one is secreted and one is membrane bound, the 2 LAIR proteins are assumed to have evolved from a common gene ancestor and seem to share similar adhesion profiles, suggesting that LAIR2 may compete with LAIR1 for ligand binding. LAIR2 was discovered by its similarity to LAIR1, which is an inhibitory receptor present on mononuclear leukocytes. The LAIR2 gene maps to a region of 19q13.4, dubbed the leukocyte receptor cluster, which contains 29 genes in the immunoglobulin superfamily, including LAIR1. The function of the LAIR2 protein is unknown, though it is assumed to be secreted and may help modulate mucosal tolerance.
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Synonyms
Leukocyte-associated immunoglobulin-like receptor 2, LAIR-2, CD306, LAIR2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQEGAL PRPSISAEPG TVISPGSHVT FMCRGPVGVQ TFRLEREDRA KYKDSYNVFR LGPSESEARF HIDSVSEGNA GLYRCLYYKP PGWSEHSDFL ELLVKGTVPG TEASGFDAP.
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 :
GM- CSF HumanDescription:
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Product # :
CYT-221Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14477 Dalton. GM-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GM-CSF was lyophilized after extensive dialysis against 2mM sodium phosphate buffer pH= 7.4±0.1.
Purity
Greater than 98.0% as determined by:
1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.More Info
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Introduction
Granulocyte Macrophage Colony Stimulating Factor (GM-CSF) was first characterized as a growth factor that supports the in-vitro colony formation of granulocytes-macrophages progenitor cells. It is a pleiotropic cytokine and a member of a family of endogenous cytokines of the hematopoietic system. GM-CSF is produced as a response to immune or inflammatory stimuli by activated cells of the hematopoietic system such as T cells, B cells, macrophages, mast cells and also fibroblasts and alveolar epithelial cells. It plays an important role in regulating the proliferation, differentiation, survival and activation of hematopoietic cells such as granulocytes and monocytes ,neutrophiles, basophiles and eosonophoiles, erythroid cells, megakaryocytes and T cells.
Human and mouse GM-CSF have about 56% homology and are species specific. Human GM-CSF is not active on mouse cells and vice versa. It is active on canine and feline cells.
GMCSF is 144 amino acids, 22kDa glycoprotein. It is composed of four bundles alpha helices. Its receptor is heterodimers with a ligand-specific alpha subunit and a betac subunit that is shared with the interleukin IL-3 and IL-5 receptors. This unusual form of receptor assembly likely applies also to IL-3 and IL-5 receptors. Cross-linking the two receptor subunits is required for receptor activation and signaling .
GMCSF has been shown to be involved in maturation, mobilization and antigen presentation of myeloid dentritic cells (DCs) in-vivo or ex-vivo. This function promotes Th1 immune responses, cytotoxcity, anti-angiogenesis as well as allergic inflammation, and the development of autoimmunity. Therefore GMCSF can be used in immunotherapy for the treatment of immune suppressed and immune-compromised patients as well as in veterinary medicine for the same purpose. GM-CSF is also important in regulation of embryo development and pregnancy and specifically in embryo implantation and subsequent development . -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
N-terminal methionine has been completely removed enzymatically. -
Background
What is the molecular weight/Mw of GM CSF HUMAN Protein?
GM CSF HUMAN Protein has a total Mw of 14.47kDa.
What is the source or expression system of GM CSF HUMAN Protein?
Escherichia Coli.
What is the Purity of GM CSF HUMAN Protein?
GM CSF HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GM CSF HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.
What is the amino acid sequence of GM CSF HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
N-terminal methionine has been completely removed enzymatically.
What applications can GM CSF HUMAN Protein be used in?
GM CSF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM CSF HUMAN Protein?
The endotoxin level is minimal, GM CSF HUMAN Protein was purified using conventional chromatography techniques.
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Protein content
GM-CSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.963 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GEN computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GM-CSF 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 :
VEGF (121 a.a.) MouseDescription:
Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-574Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor-121 Mouse Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28.4 kDa.Recombinant Mouse VEGF-121 is a truncated version of Murine VEGF-165.The VEGF-121 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
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
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGF-121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 VEGF-121 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
MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKRPR R.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL9 BovineDescription:
MIG (CXCL9) Bovine Recombinant
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
Product # :
CHM-041Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
MIG (CXCL9) BovineRecombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 104 amino acids and having a molecular mass of approximately 18.0kDa.MIG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.
More Info
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Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belongs to the CXC chemokine family that is also known as Monokine induced by gamma INF (MIG). CXCL9 is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
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Synonyms
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIG (CXCL9) 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 MIG (CXCL9) 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
VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.
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Background
What is the molecular weight/Mw of CXCL9 BOVINE Protein?
CXCL9 BOVINE Protein has a total Mw of 18kDa.
What is the source or expression system of CXCL9 BOVINE Protein?
Escherichia Coli.
What is the Purity of CXCL9 BOVINE Protein?
CXCL9 BOVINE Protein is > 96% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL9 BOVINE Protein?
The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.
What is the amino acid sequence of CXCL9 BOVINE Protein?
VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.
What applications can CXCL9 BOVINE Protein be used in?
CXCL9 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL9 BOVINE Protein?
The endotoxin level is minimal, CXCL9 BOVINE 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 :
Activin-A, CHO HumanDescription:
Activin-A Human Recombinant, CHO
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-1258Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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Description
Activin-A Human Recombinant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 26.0kDa. The Active form Activin-A is purified by standard chromatographic techniques.
Source
CHO cells.
Formulation
Human Activin-A was lyophilized from a concentrated filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.
More Info
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Human INHBA protein should be reconstituted in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26 kDa.
What is the source or expression system of Activin A Protein?
CHO Cells.
What is the Purity of Activin A Protein?
Activin A Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
SHH RatDescription:
Sonic HedgeHog Rat Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-1099Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog 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 SHH 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
MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.
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.