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1000 results found for “Albumin”
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Name :
HCV NS4 (1916-1947 a.a.)Description:
Hepatitis C Virus NS4 (1916-1947 a.a.) Recombinant
Product # :
HCV-202Price :
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Description
E.coli derived 30 kDa recombinant protein. Artificial mosaic polypeptide composite constructed from diagnostically relevant antigenic regions derived from the NS4 region.
Formulation
1.5M urea, 25mM Tris-HCl pH-8, 0.2% Triton-X & 50% Glycerol.
Purity
HCV NS4 protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to IFN-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to IFN-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS4 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HCV NS4 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
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Specificity
Immunoreactive with sera of HCV-infected individuals.
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Purification Method
HCV NS4 protein was purified by proprietary chromatographic technique.
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 :
Protein GDescription:
Protein G Recombinant
Product # :
PRO-402Price :
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Description
The Protein G is a single, non-glycosylated protein contains 200 amino acids having a molecular mass of 21.8kDa. The Protein-G migrates on SDS-PAGE around 32kDa.
Source
Escherichia Coli.
Formulation
Lyophilized white powder containing no additives.
Purity
>96% as determined by SDS-PAGE and RP-HPLC.
sds-page
Citations
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Recombinant Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G 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
Reconstitution with deionized water or PBS.
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Amino Acid Sequence
LPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.
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 :
COMP HumanDescription:
Cartilage Oligomeric Matrix Protein Human Recombinant
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5
Product # :
PRO-2727Price :
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Description
COMP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 749 amino acids (21-757a.a) and having a molecular mass of 82.4kDa.COMP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The COMP solution (0. 5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. COMP is a calcium-binding protein of high molecular weight (>500kDa) found in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but is common in other tissues, such as synovium and tendon. Intact COMP is pentameric, with 5 equal subunits and the carboxy-terminal globular domain of native COMP binds to collagens I, II, and IX. COMP molecules are vital for conserving the properties and integrity of collagen network. Moreover, COMP has a storage and delivery function for hydrophobic cellsignaling molecules such as vitamin D. Mutations of the COMP gene cause Pseudoachondroplasia and some forms of multiple epiphyseal dysplasia which implicates that it is vital that COMP develops and functions normally.
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Synonyms
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5
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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
ADPDAHSLWY NFTIIHLPRH GQQWCEVQSQ VDQKNFLSYD CGSDKVLSMG HLEEQLYATD AWGKQLEMLR EVGQRLRLEL ADTELEDFTP SGPLTLQVRM SCECEADGYI RGSWQFSFDG RKFLLFDSNN RKWTVVHAGA RRMKEKWEKD SGLTTFFKMV SMRDCKSWLR DFLMHRKKRL EPTAPPTMAP GLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH
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 :
OmpA S.EnteritidisDescription:
Salmonella Enteritidis Outer Membrane Protein-A Recombinant
Outer Membrane Protein-A, OmpA.
Product # :
PRO-1918Price :
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Description
The Recombinant Salmonella Enteritidis Outer Membrane Protein A, E.Coli derived, 330 amino acids, contains the ompA immunodominant regions. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
PBS and 25MmM Arginine.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
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Synonyms
Outer Membrane Protein-A, OmpA.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
OmpA S.Enteritidis Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Immunoassay. Outer membrane protein A (ompA) of S. Enteritidis is a protein directly exposing to outsides of this organism, In hens, the production of antibodies against outer membrane protein A (ompA) during the infection has been demonstrated by inoculating both the complete bacterium and expressed protein produced from ompA DNA vaccine. Vaccination by ompA protein to hens is a poteintail tool to control S. enteritidis contaminated eggs into market, and prevent human foodborne disease from eggs.
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 :
Epoetin HumanDescription:
Erythropoietin-Alpha Human Recombinant
Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.
Product # :
CYT-201Price :
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Shipped at Room temp
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Description
Erythropoietin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a single, polypeptide chain containing 166 amino acids and having a predicted molecular mass of 21,000 Dalton and apparent glycosylated molecular mass of 36-40kDa. EPO-a is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells(CHO).
Formulation
Each mg of lyophilized powder contains 0.59 mg sodium citrate, 0.58 mg sodium chloride and 0.006 mg citric acid.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity was measured by Normocyth -aemic mice and was found to be 150,000 IU/mg.Citations
More Info
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Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
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Synonyms
Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha 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 EPO-alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR.
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Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 38kDa.
What is the source or expression system of EPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
The Specific Activity was measured by Normocyth -aemic mice and was found to be 150,000 IU/mg.
What is the amino acid sequence of EPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN 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 :
CST3 Human, PichiaDescription:
Cystatin C Human Recombinant, Pichia
Product # :
PRO-2743Price :
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Description
Recombinant Human Cystatin C is having a molecular mass of approximately 13kDa.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from 20mM NH4HCO3.
Purity
Greater than 96.0%.
Citations
More Info
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Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and subsequently, the atherosclerosis and abdominal aortic aneurysm.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Human CST3 although stable at 4°C for 1 week, should be stored at -20°C.
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Solubility
It is recommended to reconstitute the lyophilized CST3 Human in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TerlipressinDescription:
Terlipressin
Product # :
HOR-287Price :
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Description
Terlipressin contains 12 amino acids Gly-Gly-Gly-c[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2 and having a molecular weight of 1227.37 Dalton.
Formulation
The protein (1 mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Terlipressin is similar to a naturally occurring hormone present in the body, known as antidiuretic hormone (ADH) or vasopressin. ADH has two main effects in the body. Firstly, it causes narrowing of blood vessels (vasoconstriction), thereby limiting blood flow to a particular area of the body. It also acts on receptors in the kidney to retain water in the body, which helps to prevent excessive loss of water in the urine. Terlipressin is commonly used to stop bleeding of varices in the food pipe (oesophagus). Varices are fragile distended veins that can occur in various parts of the body such as the oesophagus. This is caused by an increase in blood pressure in certain diseases such as severe liver disease. These fragile varices can rupture and lead to life threatening bleeding. Terlipressin is therefore given to narrow blood vessels, and so restricting blood flow to the varices and stopping the bleeding.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Terlipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Terlipressin 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 Terlipressin18MΩ-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 :
Noggin Human, HEKDescription:
Noggin Human Recombinant, HEK
Noggin, Symphalangism 1 (Proximal), Synostoses (Multiple) Syndrome 1, SYNS1A, SYNS1, SYM1.
Product # :
CYT-977Price :
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Description
Noggin produced in HEK293 cells is a polypeptide chain containing 211 amino acids (28-232a.a.) and having a molecular mass of 23.8kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).Noggin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
Recombinant Human Noggin hek293 derived protein is provided as a solution (0.25mg/ml) containing 50mM MES (pH 6.5) and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
Noggin, Symphalangism 1 (Proximal), Synostoses (Multiple) Syndrome 1, SYNS1A, SYNS1, SYM1.
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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
QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSCHHHHH 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 :
ITGB3BP HumanDescription:
Integrin Beta 3 Binding Protein Human Recombinant
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
Product # :
PRO-1435Price :
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Description
ITGB3BP Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.1kDa. ITGB3BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ITGB3BP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.
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Synonyms
CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.
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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 MGSMPFAPVA QARVQWHDFR SLQHLLPAFK RFSCLSLGSS WDYSVKRSLK LDGLLEENSF DPSKITRKKS VITYSPTTGT CQMSLFASPT SSEEQKHRNG LSNEKRKKLN HPSLTESKES TTKDNDEFMM LLSKVEKLSE EIMEIMQNLS SIQALEGSRE LENLIGISCA SHFLKREMQK TKELMTKVNK QKLFEKSTGL PHKASRHLDS YEFLKAILN.
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 :
AMH (452-560) HumanDescription:
Anti-Mullerian Hormone (452-560) Human Recombinant
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Product # :
PRO-2843Price :
Quantity :
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Description
Anti-Mullerian Hormone Human Recombinant produced in CHO is a Homodimer, glycosylated, polypeptide chain containing 109 amino acids (Ser452-Arg560) and having a total molecular mass of 23.4Da.
Anti-Mullerian Hormone is purified by proprietary chromatographic techniques.
Source
CHO Cells.
Formulation
AMH Lyophilized from a 0.2µm filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.
Purity
Greater than 97% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Immobilized Recombinant Human AMH at 3 µg/mL (100 µL/well) will bind Recombinant Human MIS RII Fc Chimera with a linear range of 2.0-100 ng/mL. The activity was measured by its binding ability in a functional ELISA.Citations
More Info
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Introduction
Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.
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Synonyms
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
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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 reconstitute in sterile 4mM HCl to a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SAGATAADGP CALRELSVDL RAERSVLIPE TYQANNCQGV CGWPQSDRNP RYGNHVVLLL KMQVRGAALA RPPCCVPTAY AGKLLISLSE ERISAHHVPN MVATECGCR.
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 :
MoeXDescription:
Mycobacterium Tuberculosis MoeX Recombinant
Product # :
PRO-1919Price :
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Description
Recombinant Mycobacterium Tuberculosis MoeX produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 38 kDa. The MoeX is fused to a His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MoeX protein solution 0.75mg/ml contains 1xPBS, 25mM arginine and 0.02% NaN3.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
Citations
More Info
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Physical Appearance
Sterile Filtered clear solution.
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Stability
MoeX Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
F8 HumanDescription:
Coagulation Factor-VIII Human
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Product # :
PRO-317Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Factor VIII produced from Human Plasma contains 2332 amino acids and having a molecular mass of 330kDa. Factor-VIII is effective in the correction and prevention of severe bleeding episodes attributed to Factor VIII deficiency. The Factor-VIII is purified by proprietary chromatographic techniques.
Source
Human Plasma.
Formulation
The lyophilized protein 200IU/ml was lyophilized from a sterile solution containing 1.5% Glycine, 160mM Calcium chloride and 25mM NaCitrate and 25mM NaCl.
Biological Activity
The potency was found to be 10 Units/mg.
Citations
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 1 week, should be stored desiccated between 2-8°C. Upon reconstitution Factor-VIII should be stored at 4°C.
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Solubility
It is recommended to reconstitute the lyophilized Factor-VIII in sterile 18MΩ-cm H2O at a concentration of 200IU/ml, which can then be further diluted to other aqueous solutions.
Make sure that the vial has reached room temperature prior to its reconstitution, otherwise it might precipitate.
-
Human Virus Test
The plasma is collected from donors with Hepatitis B vaccinated. Each unit of plasma has been tested for HBsAg, Anti-HIV-1/2 plus O and Anti-HCV by using the imported kits which are approved by Federal Drug Administration (FDA).
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 :
Omentin HumanDescription:
Omentin Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-301Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.
Source
E.Coli.
Formulation
Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
-
Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Intelectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Omentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.
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 32A HumanDescription:
Interleukin-32 alpha Human Recombinant
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Product # :
CYT-584Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids and having a molecular mass of 14.9 kDa.
Source
Escherichia Coli.
Formulation
IL-32 was lyophilized from a concentrated (1mg/ml) solution in water containing 50mM sodium Phosphate buffer pH=7.5.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Human IL-32 alpha activity is measured via the dose-dependent induction of TNF-alpha in the human THP-1 monocytic cell line.Citations
More Info
-
Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of IFNgamma.
IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases. -
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL32 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL32 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 IL-32 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MCFPKVLSDD MKKLKARMHQ AIERFYDKMQ NAESGRGQVM SSLAELEDDF KEGYLETVAA YYEEQHPELT PLLEKERDGL RCRGNRSPVP DVEDPATEEP GESFCDKSYG APRGDKEELT PQKCSEPQSS K.
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 :
TRIM21 Human BiotinDescription:
Tripartite Motif Containing 21 (RO52) Human Recombinant, Biotinylated
52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.
Product # :
PRO-2559Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa. TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
TRIM21 solution is supplied in 20mM HEPES pH-7.6, 0.01mM EDTA and 0.02% SDS.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.
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Synonyms
52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.
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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 IgG type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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 RatDescription:
Activin-A Rat Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-147Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/mlCitations
More Info
-
Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
-
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
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/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?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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 :
HIF1A Human, HisDescription:
Hypoxia-Inducible Factor-1 Alpha Human Recombinant, His Tag
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
Product # :
PRO-415Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (576-785 a.a.) and having a molecular mass of 25.1 kDa. The HIF1A is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HIF1A Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
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Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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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 MSFDQLSPLE SSSASPESAS PQSTVTVFQQ TQIQEPTANA TTTTATTDEL KTVTKDRMED IKILIASPSP THIHKETTSA TSSPYRDTQS RTASPNRAGK GVIEQTEKSH PRSPNVLSVA LSQRTTVPEE ELNPKILALQ NAQRKRKMEH DGSLFQAVGI GTLLQQPDDH AATTSLSWKR VKGCKSSEQN GMEQKTIILI PSDLACRLLG Q.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
DCUN1D4 HumanDescription:
DCN1 Defective in Cullin Neddylation 1 Domain Containing 4 Human Recombinant
DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.
Product # :
PRO-1715Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCUN1D4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 36.5kDa.DCUN1D4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DCUN1D4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
DCUN1D4 holds 1 DCUN1 domain.
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Synonyms
DCN1 Defective In Cullin Neddylation 1 Domain Containing 4, Defective In Cullin Neddylation Protein 1-Like Protein 4, DCUN1 Domain-Containing Protein 4, KIAA0276, DCN1-Like Protein 4.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMHSDAAA VNFQLNSHLS TLANIHKIYH TLNKLNLTED IGQDDHQTGS LRSCSSSDCF NKVMPPRKKR RPASGDDLSA KKSRHDSMYR KYDSTRIKTE EEAFSSKRCL EWFYEYAGTD DVVGPEGMEK FCEDIGVEPE NVVMLVLAWK LDAQNMGYFT LQEWLKGMTS LQCDTTEKLR NTLDYLRSFL NDSTNFKLIY RYAFDFAREK DQRSLDINTA KCMLGLLLGK IWPLFPVFHQ FLEQSKYKVI NKDQWCNVLE FSRTINLDLS NYDEDGAWPV LLDEFVEWYK DKQMS
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 :
EFNB1 Human, Sf9Description:
Ephrin-B1 Human Recombinant, Sf9
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
Product # :
PRO-2543Price :
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Description
EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.
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Synonyms
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
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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
ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
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 :
FABP7 Human, HisDescription:
Fatty Acid Binding Protein-7 Human Recombinant, His Tag
MRG, BLBP, FABPB, B-FABP, DKFZp547J2313, Fatty acid-binding protein brain, Fatty acid-binding protein 7, Brain lipid-binding protein, Mammary-derived growth inhibitor related, FABP7.
Product # :
PRO-661Price :
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Description
FABP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 19.39kDa. FABP7 is fused to His-Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The FABP7 protein solution contains 20mM Tris-HCl pH-8 and 50% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
FABP7 is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs are are inovlved in fatty acid uptake, transport, and metabolism. FABP7 is expressed in radial glia by the activation of Notch receptors and binds DHA with the highest affinity among all of FABPs. FABP7 plays an important role in transport of hydrophobic ligand with potential morphogenic activity during cns development. FABP7 is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (by similarity).
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Synonyms
MRG, BLBP, FABPB, B-FABP, DKFZp547J2313, Fatty acid-binding protein brain, Fatty acid-binding protein 7, Brain lipid-binding protein, Mammary-derived growth inhibitor related, FABP7.
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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. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FAM3A HumanDescription:
Family with Sequence Similarity 3, Member A Human Recombinant
Protein FAM3A, Cytokine-like protein 2-19, FAM3A, 2-19, 2.19, DLD, XAP-7, DXS560S.
Product # :
PRO-1584Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FAM3A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 23.1kDa (calculated).
Source
Escherichia Coli.
Formulation
FAM3A filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM TRIS and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Family with Sequence Similarity 3, Member A (FAM3A) is a member of the FAM3 family along with FAM3B (Pander) protein which induces apoptosis of pancreatic alpha and beta cells. FAM3A is a cytokine-like protein, which is expressed in almost all tissues such as the testis, pancreas, adrenal, placenta, brain, fetal brain, liver, kidney, skeletal muscle and the heart. FAM3A gene expression may be regulated by peroxisome proliferator-activated receptor gamma, and the FAM3A protein might be involved in the regulation of glucose and lipid metabolism. Although the function of the FAM3A protein has been unclear until now, it may act as a defensin against invading fungal microorganisms.
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Synonyms
Protein FAM3A, Cytokine-like protein 2-19, FAM3A, 2-19, 2.19, DLD, XAP-7, DXS560S.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
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. FAM3A 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
MKHHHHHHASFPRIQQLFTS PESSVTAAPR ARKYKCGLPQ PCPEEHLAFR VVSGAANVIG PKICLEDKML MSSVKDNVGR GLNIALVNGV SGELIEARAF DMWAGDVNDL LKFIRPLHEG TLVFVASYDD PATKMNEETR KLFSELGSRN AKELAFRDSW VFVGAKGVQN KSPFEQHVKN SKHSNKYEGW PEALEMEGCI PRRSTAS.
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 :
FAS Human, Sf9Description:
sFas Receptor Human Recombinant, Sf9
Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.
Product # :
CYT-1153Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FAS Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 156 amino acids (26-173 aa) and having a molecular mass of 17.7KDa.FAS is fused to a 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FAS protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FAS or tumor necrosis factor receptor superfamily member 6 or TNFRSF6, is part of the death receptor family, which is part of the TNF receptor protein family. TNFRSF6 has a crucial part in regulating viral infections. FAS protein can be found in almost all cell types, when its cognate ligand (FasL) can be found in activated T cells, NK cells & dendritic cells. The regulating protein of FasL & TRAIL on HCMV-infected dendritic enhances direct destruction of activated T lymphocytes. furthermore, subvertneutrophil function in HCMV retinitis can occur when FasL is activated in HCMV infected retinal pigment epithelial cells.
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Synonyms
Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.
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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
QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRSNLE HHHHHH
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Background
What is the molecular weight/Mw of FAS Protein?
FAS Protein has a total Mw of 17.7kDa.
What is the source or expression system of FAS Protein?
Sf9, Baculovirus cells
What is the Purity of FAS Protein?
FAS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FAS Protein?
The biological functionality of FAS Protein will be determined in the future.
What is the amino acid sequence of FAS Protein?
QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRSNLE HHHHHH
What applications can FAS Protein be used in?
FAS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FAS Protein?
The endotoxin level is minimal, FAS 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 :
TRIM33 HumanDescription:
Tripartite Motif Containing 33 Human Recombinant
E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.
Product # :
PRO-1506Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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- Citations
Description
TRIM33 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 124,041 Dalton. TRIM33 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
TRIM33 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Tripartite Motif Containing 33 (TRIM33) belongs to the tripartite motif family. This motif includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM33 is assumed to be a transcriptional corepressor. TRIM33 functions as an E3 ubiquitin-protein ligase. TRIM33 also promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. In addition, TRIM33 inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Furthermore, TRIM33 has a role in the control of cell proliferation.
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Synonyms
E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.
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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. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LIF Human, GSTDescription:
Leukemia Inhibitory Factor, GST tag Human Recombinant
D factor, MLPLI, HILDA, Emfilermin, Leukemia Inhibitory factor, Differentiation-stimulating factor, Melanoma-derived LPL inhibitor.
Product # :
CYT-001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- formulation
- purity
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Description
LIF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (23-202a.a.) and having a molecular mass of 47.2kDa.LIF is fused to a 236 amino acid His-GST tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LIF GST protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leukemia inhibitory factor, is a pleiotropic cytokine which is expressed by numerous cells including activated T lymphocytes, monocytes, mast cells and neuronal cells. LIF takes part in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and is a key player in immune tolerance at the maternal-fetal interface.
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Synonyms
D factor, MLPLI, HILDA, Emfilermin, Leukemia Inhibitory factor, Differentiation-stimulating factor, Melanoma-derived LPL inhibitor.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MHHHHHHMSP ILGYWKIKGL VQPTRLLLEY LEEKYEEHLY ERDEGDKWRN KKFELGLEFP NLPYYIDGDV KLTQSMAIIR YIADKHNMLG GCPKERAEIS MLEGAVLDIR YGVSRIAYSK DFETLKVDFL SKLPEMLKMF EDRLCHKTYL NGDHVTHPDF MLYDALDVVL YMDPMCLDAF PKLVCFKKRI EAIPQIDKYL KSSKYIAWPL QGWQATFGGG DHPPKSDLVP RGSHMSPLPI TPVNATCAIR HPCHNNLMNQ IRSQLAQLNG SANALFILYY TAQGEPFPNN LDKLCGPNVT DFPPFHANGT EKAKLVELYR IVVYLGTSLG NITRDQKILN PSALSLHSKL NATADILRGL LSNVLCRLCS KYHVGHVDVT YGPDTSGKDV FQKKKLGCQL LGKYKQIIAV LAQAF
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.