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1000 results found for “erythropoietin”
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Name :
CFH HumanDescription:
Complement Factor H Human
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
Product # :
PRO-2700Price :
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Shipped with Ice Packs
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Description
Human Complement Factor H produced in Human plasma having a total molecular mass of 155kDa.
Source
Human Plasma.
Formulation
CFH protein solution contains PBS, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.
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Synonyms
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
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Physical Appearance
Sterile filtered solution.
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Stability
CFH Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 22 Mouse, PEGDescription:
Interleukin-22 Mouse Recombinant, Pegylated
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-701Price :
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Shipped at Room temp
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Description
Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.More Info
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Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep
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Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius 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 pegylated mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
IL6ST HumanDescription:
Interleukin-6 Signal Transducer Human Recombinant
Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta
Product # :
CYT-1156Price :
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Description
IL6ST Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 605 amino acids (23-619 a.a) and having a molecular mass of 68.9kDa.IL6ST is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL6ST solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-6 Signal Transducer or IL6ST is a receptor, part of the family of class 1 cytokine receptor. IL6ST binds to IL-6 through membrane-anchored or soluble IL-6R starts a connection between another complex of IL6ST and IL-6 , thus forming a homo-dimer and a signal transduction occurs.
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Synonyms
Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta
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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
ELLDPCGYIS PESPVVQLHS NFTAVCVLKE KCMDYFHVNA NYIVWKTNHF TIPKEQYTII NRTASSVTFT DIASLNIQLT CNILTFGQLE QNVYGITIIS GLPPEKPKNL SCIVNEGKKM RCEWDRGRET HLETNFTLKS EWATHKFADC KAKRDTPTSC TVDYSTVYFV NIEVWVEAEN ALGKVTSDHI NFDPVYKVKP NPPHNLSVIN SEELSSILKL TWTNPSIKSV IILKYNIQYR TKDASTWSQI PPEDTASTRS SFTVQDLKPF TEYVFRIRCM KEDGKGYWSD WSEEASGITY EDRPSKAPSF WYKIDPSHTQ GYRTVQLVWK TLPPFEANGK ILDYEVTLTR WKSHLQNYTV NATKLTVNLT NDRYVATLTV RNLVGKSDAA VLTIPACDFQ ATHPVMDLKA FPKDNMLWVE WTTPRESVKK YILEWCVLSD KAPCITDWQQ EDGTVHRTYL RGNLAESKCY LITVTPVYAD GPGSPESIKA YLKQAPPSKG PTVRTKKVGK NEAVLEWDQL PVDVQNGFIR NYTIFYRTII GNETAVNVDS SHTEYTLSSL TSDTLYMVRM AAYTDEGGKD GPEFTFTTPK FAQGEIELEH HHHHH
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Background
Significance of Human Recombinant Interleukin-6 Signal Transducer: Insights and Implications
Abstract:
The Interleukin-6 (IL-6) signal transducer holds a pivotal role in the complex IL-6 signaling pathway, orchestrating crucial cellular responses. This paper delves into the significance of Human Recombinant IL-6 Signal Transducer in unraveling IL-6-mediated cellular communication and highlights its potential applications in research and therapeutic development. The review sheds light on the methodology of producing this transducer and its relevance in advancing our understanding of cytokine signaling.
Introduction:
IL-6, a pleiotropic cytokine, is known to exert its diverse effects through a complex signaling cascade, wherein the signal transducer plays a crucial role. The availability of Human Recombinant IL-6 Signal Transducer enables the investigation of its role in health and disease. This transducer is vital for transmitting IL-6 signals, influencing processes like immune response, inflammation, and cell differentiation.
IL-6 Signal Transduction Pathway:
The IL-6 signal transduction pathway involves binding of IL-6 to its receptor, leading to the recruitment of the signal transducer and subsequent activation of downstream signaling molecules such as JAK/STAT pathway. This orchestrated response modulates gene expression, thereby impacting cellular behavior.
Methods of Production:
Human Recombinant IL-6 Signal Transducer is produced by expressing the corresponding gene in a suitable expression system, often utilizing bacterial or mammalian cells. Proper post-translational modifications are necessary to ensure its biological activity and appropriate functioning within the signaling cascade.
Applications in Research:
Human Recombinant IL-6 Signal Transducer serves as a fundamental tool in elucidating IL-6-mediated signaling mechanisms. Its availability facilitates the exploration of how aberrant signaling contributes to diseases such as autoimmune disorders, inflammatory conditions, and certain cancers. The transducer's interaction with other signaling pathways is also of interest for comprehensive pathway analysis.
Therapeutic Implications:
Understanding the IL-6 signal transduction pathway has led to the development of targeted therapies for IL-6-related diseases. Modulation of this pathway presents potential opportunities for novel therapeutic interventions, thereby offering a new dimension in precision medicine.
Challenges and Future Directions:
While the availability of Human Recombinant IL-6 Signal Transducer has significantly advanced our knowledge, challenges remain in deciphering the intricate nuances of IL-6 signaling. Developing strategies to selectively intervene in this pathway without disturbing physiological homeostasis presents an ongoing challenge.
Conclusion:
The Human Recombinant IL-6 Signal Transducer serves as a cornerstone in unraveling the complexities of IL-6 signaling, shedding light on its roles in health and disease. Its applications span from fundamental research to therapeutic development, showcasing its potential to shape the future of precision medicine.
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 :
TRIP10 HumanDescription:
Thyroid Hormone Receptor Interactor 10 Human Recombinant
Cdc42-interacting protein 4, Protein Felic, Salt tolerant protein, hSTP, Thyroid receptor-interacting protein 10, TR-interacting protein 10, TRIP-10,TRIP10, CIP4, STOT, STP, HSTP.
Product # :
PRO-1811Price :
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Description
TRIP10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (260-545) and having a molecular mass of 34.6 kDa.TRIP10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TRIP10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol, 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Thyroid Hormone Receptor Interactor 10 (TRIP10) is a part of the F-BAR family of proteins which is expressed in a variety of tissues, including kidney, brain, liver, lung, heart and pancreas. The F-BAR family of proteins contains an N-terminal, alpha-helical, region which is hydrophobic and related to the Bin Amphiphysin Rvs (BAR) protein family. TRIP10 is vital for the coordination of membrane tubulation with Actin cytoskeletal reorganization during endocytosis.
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Synonyms
Cdc42-interacting protein 4, Protein Felic, Salt tolerant protein, hSTP, Thyroid receptor-interacting protein 10, TR-interacting protein 10, TRIP-10,TRIP10, CIP4, STOT, STP, HSTP.
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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 MGSDPKNDSH VLIELHKSGF ARPGDVEFED FSQPMNRAPS DSSLGTPSDG RPELRGPGRS RTKRWPFGKK NKTVVTEDFS HLPPEQQRKR LQQQLEERSR ELQKEVDQRE ALKKMKDVYE KTPQMGDPAS LEPQIAETLS NIERLKLEVQ KYEAWLAEAE SRVLSNRGDS LSRHARPPDP PASAPPDSSS NSASQDTKES SEEPPSEESQ DTPIYTEFDE DFEEEPTSPI GHCVAIYHFE GSSEGTISMA EGEDLSLMEE DKGDGWTRVR RKEGGEGYVP TSYLRVTLN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL-6 PAT1F10AT AntibodyDescription:
Interleukin-6 Clone PAT1F10AT, Mouse Anti Human
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Product # :
ANT-540Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
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Synonyms
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human IL-6, clone PAT1F10AT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IL-6 protein 30-212 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT1F10AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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Background
Research Paper on Interleukin-6 Clone PAT1F10AT, Mouse Anti-Human
Abstract:
Interleukin-6 (IL-6) Clone PAT1F10AT, a Mouse Anti-Human monoclonal antibody, plays a pivotal role in deciphering the complexities of immune modulation. This research paper provides an insightful exploration of its molecular attributes and its profound implications in immunological research. We examine its interactions, functions, and synonyms, including DIF, TNFA, and TNFSF2, shedding light on its significance in understanding immune responses.
Introduction:
IL-6 Clone PAT1F10AT, a Mouse Anti-Human antibody, has emerged as a cornerstone in immunology research. This paper delves into its unique characteristics and its critical role in unraveling immune mechanisms.
Molecular Precision and Specificity:
The exceptional affinity and specificity of IL-6 Clone PAT1F10AT for human IL-6 distinguish it as an invaluable tool for immunodetection and functional studies. Its targeted binding facilitates accurate identification of IL-6 in various experimental contexts.
Unveiling Immune Dynamics:
IL-6 is a central player in immune orchestration, and IL-6 Clone PAT1F10AT offers a window into its world. By investigating its involvement in immune responses, inflammation, and signaling pathways, researchers gain insights into immune regulation.
Synonyms and Interactions:
Understanding IL-6 synonyms, such as DIF, TNFA, and TNFSF2, underscores its intricate web of interactions. IL-6 Clone PAT1F10AT's ability to decipher these connections enhances our understanding of cytokine-mediated immune modulation.
Disease Implications and Therapeutic Avenues:
With its relevance in diseases like autoimmune disorders and inflammatory conditions, IL-6 Clone PAT1F10AT assumes significance in disease-focused investigations. It enables researchers to dissect disease mechanisms and evaluate potential therapeutic interventions.
Clinical Utility and Diagnostic Precision:
IL-6 Clone PAT1F10AT's utility transcends research settings, finding application in clinical diagnostics. Its role in immunoassays facilitates accurate disease diagnosis and monitoring, contributing to improved patient management.
Conclusion:
In the realm of immunology, IL-6 Clone PAT1F10AT stands as a potent ally in unraveling immune intricacies. Its molecular precision, diverse functions, and potential therapeutic implications make it a cornerstone in advancing our understanding of immune responses and diseases.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
IL-6 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
Thrombin Human, HEKDescription:
Thrombin Human Recombinant, HEK
Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.
Product # :
PRO-1422Price :
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Description
Recombinant Human Thrombin produced in HEK cells, having a total molecular weight of 36kDa. The Thrombin is purified by proprietary chromatographic techniques.
Source
HEK
Formulation
The Thrombin solution contains 20mM MES, pH6.0 and 500mM Choline Chloride.
Biological Activity
5396 NIH Units/mg.
The activity was determined in NIH units by comparing to Sigma’s human plasma thrombin. Protein concentration was measured using E(0.1%)@280nm = 1.83.More Info
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Introduction
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
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Synonyms
Prothrombin, EC 3.4.21.5, Coagulation factor II, F2, PT, THPH1, RPRGL2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store frozen at -20°C to -80°C for long periods of time. Avoid multiple freeze-thaw cycles.
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Assay Conditions
Thrombin (1nM) was assayed using SPECTROZYME TH as a substrate (20µM) in 5mM Tris-HCl (pH8.0), 0.1% PEG, 200mM NaCl at 25°C.
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 :
ATF HumanDescription:
Apo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Apo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.
Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.
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 :
MIF Human His CDescription:
Macrophage Migration Inhibitory Factor Human Recombinant, His Tag C-Terminus
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-521Price :
Quantity :
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Shipped at Room temp
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Description
MIF human Recombinant, fused to His-tag at C-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.
Source
Escherichia Coli.
Formulation
Human MIF was lyophilized from a 1mg/ml solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind rhCD74 in a functional ELISA.More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF 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
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
ALEHHHHHH.
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 :
Endostatin HumanDescription:
Endostatin Human Recombinant
Product # :
PRO-248Price :
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Shipped with Ice Packs
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Description
Endostatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide having a predicted molecular mass of 20kDa.C-terminal fragment of collagen XVIII that has been shown to act as a potent inhibitor of angiogenesis and tumor growth in vitro and in vivo. Induces tyrosine phosphorylation of Shc (SH2 domain adapter protein) leading to specific inhibition in endothelial cell proliferation.The Endostatin is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The recombinant Human Endostatin is formulated with 30mM Sodium acetate buffer and Mannitol, pH-5.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity was found to be 16,000IU/mg.More Info
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Introduction
Once a cluster of cancer cells reaches a diameter of about 1–2 mm, it must develop a blood supply in order to grow larger. Given that diffusion is no longer adequate to supply the cancerous cells with oxygen and nutrients and to remove wastes. Therefore, these cells secrete substances that promote the formation of new blood vessels (angiogenesis), which are vital for the growth and persistence of solid tumors and their metastases.
The production of several angiogenic factors (FGF-a, FGF-b, VEGF and VPF) is upregulated by tumors in order to stimulate angiogenesis. However, numerous malignant tumors also generate inhibitors of angiogenesis which include angiostatin and thrombospondin. The angiogenic phenotype is basically the end result of a net balance between the positive and negative regulators of neovascularization mentioned above. Endostatin’s role is to inhibit endothelial proliferation, therefore it is an effective angiogenesis inhibitor. -
Physical Appearance
Sterile filtered liquid formulation.
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Stability
Endostatin should be stored at 2-8°C.Do NOT Freeze!
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 :
DHPS HumanDescription:
Deoxyhypusine Synthase Human Recombinant
MIG13, EC 2.5.1.46, Deoxyhypusine synthase, DHS, DHPS, DS.
Product # :
ENZ-498Price :
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Description
DHPS Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 389 amino acids (1-369 a.a.) and having a molecular mass of 43.1 kDa. The DHPS is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHPS solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DHPS is vital for the first step of hypusine biosynthesis. DHPS catalyzes the NAD-dependent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the EIF5A precursor protein to form the intermediate deoxyhypusine residue.
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Synonyms
MIG13, EC 2.5.1.46, Deoxyhypusine synthase, DHS, DHPS, DS.
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Physical Appearance
Sterile Filtered clear 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). Please avoid freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG TTGFQATNFG RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF LGYTSNLISS GIRETIRYLV QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNENYCKFE DWLMPILDQM VMEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS LGDMIFFHSY KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL VAETFAQKMD AFMHEKNED.
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 :
CXCL8 Human, HisDescription:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-345Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Interleukin-8 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (23-99) and having a total molecular mass of 13.7kDa with an amino-terminal hexahistidine tag. The IL-8 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL8 His is supplied in 10mM Tris-HCl pH 8, 250mM NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
-
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
-
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. Please avoid freeze thaw cycles.
-
Background
What is the molecular weight/Mw of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein has a total Mw of 13.7kDa.
What is the source or expression system of CXCL8 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, HIS Protein?
The biological functionality of CXCL8 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is composed from 77 amino acids.
What applications can CXCL8 HUMAN, HIS Protein be used in?
CXCL8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL8 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin Rat, PEGDescription:
Pegylated Rat Leptin Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-592Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin can be stored at 4C 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.
-
Solubility
It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL31 Canine, HEKDescription:
Interleukin-31 Canine Recombinant, HEK
IL-31, Interleukin 31, IL31.
Product # :
CYT-1215Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL31 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Synonyms
IL-31, Interleukin 31, IL31.
-
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.
-
Amino Acid Sequence
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
-
Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on IL-31 for a comprehensive list of references and sources.
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 :
M CSF MouseDescription:
Macrophage-Colony Stimulating Factor Mouse Recombinant
CSF-1, Lanimostim, MCSF, M-CSF.
Product # :
CYT-439Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x105 units/mg.
More Info
-
Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
-
Synonyms
CSF-1, Lanimostim, MCSF, M-CSF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.
-
Background
Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis
Abstract:
Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.
Introduction:
M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.
Structure and Function of M-CSF:
M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.
Signaling Pathways:
Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.
Role in Macrophage Development and Function:
M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.
Therapeutic Potential:
Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.
Clinical Applications and Future Directions:
The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.
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 :
UMOD HumanDescription:
Uromodulin Human
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-381Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Uromodulin Human Native protein produced from Human Urine, is a glycosylated polypeptide chain having a total Mw of 80 kDa on SDS-PAGE.
Source
Human Urine.
Formulation
The UMOD protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing deionized water.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
-
Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at 2-8°C. DO NOT FREEZE!
-
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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
More Info
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- source
- formulation
- purity
- biological activity
- More Info
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
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
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.
-
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.
-
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.
-
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 :
IRF5 AntibodyDescription:
Interferon Regulatory Factor-5, Mouse Anti Human
Interferon regulatory factor 5, IRF-5, IRF5, SLEB10.
Product # :
ANT-407Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.02% Sodium Azide and 10% Glycerol.
More Info
-
Introduction
IRF5 belongs to the interferon regulatory factor (IRF) family, which is a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats.
-
Synonyms
Interferon regulatory factor 5, IRF-5, IRF5, SLEB10.
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Immunogen
Anti-human IRF5 mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human IRF5 amino acids 176-240 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P10T1AT.
-
Applications
IRF5 antibody has been tested by ELISA, Western blot, ICC/IF, FACS and IHC analysis
to assure specificity and reactivity. Since application varies, however, each
investigation should be titrated by the reagent to obtain optimal results. -
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
IRF5 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
EBV p18, GSTDescription:
Epstein - Barr virus (HHV-4) p18 Recombinant, GST Tag
Product # :
EBV-277Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
The E.Coli derived recombinant protein contains the HHV-4 p18 regions, having a molecular mass of 35.4kDa which includes GST tag at N-terminus.
Source
Escherichia Coli.
Formulation
3.8mg/ml in 50mM Tris-HCl, pH 8.0.
Purity
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
More Info
-
Introduction
The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virus of the herpes family (which includes Herpes simplex virus and Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expression which can be broadly categorized as being lytic cycle or latent cycle. The lytic cycle or productive infection results in staged expression of a host of viral proteins with the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cell as EBV virions are produced by budding from the infected cell. The latent cycle (lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen (EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins (LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs (EBERs).
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Stability
EBV p18, GST although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
ASAGTGALAS SAPSTAVAQS ATPSVSSSIS SLRAATSGAT AAASAAAAVD TGSGGGGQPH DTAPRGARKK Q.
-
Purification Method
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.
- View Data Sheet
Name :
EPM2A AntibodyDescription:
Laforin, Mouse Anti Human
Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.
Product # :
ANT-427Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
-
Introduction
EPM2A is a dual-specificity phosphatase which associates with polyribosomes. The EPM2A protein may be involved in the regulation of glycogen metabolism. Mutations in the EPM2A gene have been linked to myoclonic epilepsy of Lafora.
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Synonyms
Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.
-
Immunogen
Anti-human EPM2A mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EPM2A amino acids 243-331 purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
-
Clone
P3F3AT.
-
Applications
EPM2A antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
EPM2A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
LBH HumanDescription:
Limb Bud And Heart Development Human Recombinant
Protein LBH, hLBH, Limb Bud And Heart Development Homolog.
Product # :
PRO-423Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a) and having a molecular mass of 14.6kDa.LBH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LBH protein solution (0.25mg/ml) containing 20mM Tris-HCl(pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Limb Bud And Heart Development, (LBH) belongs to the LBH family.LBH is highly expressed in the heart, and expressed at low levels in placenta, lung, skeletal muscle, kidney and liver. In addition, LBH protein is a transcriptional activator which may act in mitogen-activated protein kinase signaling pathway. Among the diseases associated with LBH are celiac disease, and rheumatoid arthritis.
-
Synonyms
Protein LBH, hLBH, Limb Bud And Heart Development Homolog.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSIYFPI HCPDYLRSAK MTEVMMNTQP MEEIGLSPRK DGLSYQIFPD PSDFDRCCKL KDRLPSIVVE PTEGEVESGE LRWPPEEFLV QEDEQDNCEE TAKENKEQ
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 :
ELOB HumanDescription:
Elongin-B Human Recombinant
ELOB, SIII, Elongin B, Transcription elongation factor B polypeptide 2, RNA polymerase II transcription factor SIII subunit B, SIII p18, Elongin 18 kDa subunit, TCEB2.
Product # :
PRO-664Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TCEB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-118) and having a molecular mass of 13.1 kDa. TCEB2 is purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The TCEB2 protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1mM PMSF, and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
TCEB2 is a subunit of the SIIII complex which is a heterotrimer consisting of a transcriptionally active subunit (A) and two regulatory subunits (B and C). TCEB2 initiates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. The von Hippel-Lindau tumor suppressor protein binds to elongins B and C, and thereby inhibits transcription elongation.
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Synonyms
ELOB, SIII, Elongin B, Transcription elongation factor B polypeptide 2, RNA polymerase II transcription factor SIII subunit B, SIII p18, Elongin 18 kDa subunit, TCEB2.
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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
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALCIEPFSSPPELP DVMKPQDSGS SANEQAVQ.
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 :
GroEL E.ColiDescription:
GroEL (HSP60) E.Coli Recombinant
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.
Product # :
HSP-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant GroEL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-548) and having a molecular mass of 57.3kDa. GroEL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The groEL protein contains 25mM Tris buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin (HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition.
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Synonyms
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.
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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
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREIELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGIDKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDGTGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAVAKAGKPLLII AEDVEGEALA TAVVNTIRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTVISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDYDREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALIRVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNAATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM.
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 :
VPS28 HumanDescription:
Vacuolar Protein Sorting 28 Human Recombinant
Vacuolar protein sorting-associated protein 28 homolog, ESCRT-I complex subunit VPS28, H-Vps28, VPS28, MGC60323.
Product # :
PRO-730Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VPS28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-221 a.a.) and having a molecular mass of 25.4kDa.The VPS28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VPS28 protein solution contains 20mM Tris-HCl buffer (pH 7.5), 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
VPS28 is a subunit of the ESCRT-I complex (endosomal complexes required for transport) involved in the sorting of ubiquitinated proteins. VPS28 is involved in endosomal sorting of cell surface receptors using a multivesicular body/late endosome pathway. VSP28 binding with the TSG101 may have significant roles in budding of Retroviruses, such as HIV-1 and Ebola virus.
VSP28 interacts with TSG101, VPS37B, VPS37C, FAM125A and FAM125B, and also with VPS36, this interaction mediates the association with the ESCRT-II complex. Furthermore it interacts with SNF8 and VPS25 and CEP55. -
Synonyms
Vacuolar protein sorting-associated protein 28 homolog, ESCRT-I complex subunit VPS28, H-Vps28, VPS28, MGC60323.
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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
MFHGIPATPG IGAPGNKPEL YEEVKLYKNA REREKYDNMA ELFAVVKTMQ ALEKAYIKDC VSPSEYTAAC SRLLVQYKAA FRQVQGSEIS SIDEFCRKFR LDCPLAMERI KEDRPITIKD DKGNLNRCIA DVVSLFITVM DKLRLEIRAM DEIQPDLREL METMHRMSHL PPDFEGRQTV SQWLQTLSGM SASDELDDSQ VRQMLFDLES AYNAFNRFLH A.
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 :
Leptin BovineDescription:
Leptin Bovine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-502Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- biological activity
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Description
Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 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-Arg.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.