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  • View Data Sheet

    Description:

    COP9 Constitutive Photomorphogenic 8 Human Recombinant

    COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.

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    PRO-983

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    Description

    COPS8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-209) and having a molecular mass of 25.3kDa.COPS8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The COPS8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COP9 signalosome complex subunit 8 isoform 1 (COPS8) is one of the 8 subunits of COP9 signalosome, which is a much conserved protein complex that functions as an imperative regulator in multiple signaling pathways. The structure and function of COP9 signalosome is analogous to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome interacts with SCF-type E3 ubiquitin ligases and acts as a positive regulator of E3 ubiquitin ligases.

    • Synonyms

      COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.

    • 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

      MGSSHHHHHH SSGLVPRGSH MPVAVMAESA FSFKKLLDQC ENQELEAPGG IATPPVYGQL LALYLLHNDM NNARYLWKRI PPAIKSANSE LGGIWSVGQR IWQRDFPGIY TTINAHQWSE TVQPIMEALR DATRRRAFAL VSQAYTSIIA DDFAAFVGLP VEEAVKGILE QGWQADSTTR
      MVLPRKPVAG ALDVSFNKFI PLSEPAPVPP IPNEQQLARL TDYVAFLEN.

    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.

    Cops8 Human
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    Description:

    Rantes Rhesus Macaque Recombinant (CCL5)

    C-C motif chemokine 5, Small-inducible cytokine A5, T-cell-specific protein RANTES, CCL5.

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    CHM-033

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    Description

    Rantes Rhesus Macaque Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7.8kDa.The CCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Rantes protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB pH 6.0 and 500mM NaCl.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 1.0-10 ng/ml.

    More Info

    • Introduction

      Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

    • Synonyms

      C-C motif chemokine 5, Small-inducible cytokine A5, T-cell-specific protein RANTES, CCL5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rantes although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL5 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 Rantes in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPHASDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS.

    • Background

      What is the molecular weight/Mw of CCL5 RHESUS MACAQUE Protein?
      CCL5 RHESUS MACAQUE Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL5 RHESUS MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of CCL5 RHESUS MACAQUE Protein?
      CCL5 RHESUS MACAQUE Protein is > 98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL5 RHESUS MACAQUE Protein?
      The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 1.0-10 ng/ml.

      What is the amino acid sequence of CCL5 RHESUS MACAQUE Protein?
      SPHASDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS.

      What applications can CCL5 RHESUS MACAQUE Protein be used in?
      CCL5 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL5 RHESUS MACAQUE Protein?
      The endotoxin level is minimal, CCL5 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL5 RHESUS MACAQUE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL5 RHESUS MACAQUE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Rantes Rhesus Macaque
  • View Data Sheet

    Description:

    Cleavage And Polyadenylation Specific Factor 4 Human Recombinant

    CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1.

    Product # :

    PRO-1406

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    Description

    CPSF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 29.9kDa.CPSF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CPSF4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cleavage And Polyadenylation Specific Factor 4 (CPSF4) is a member of the CPSF4/YTH1 family. CPSF4 complex plays a vital role in pre-mRNA 3'-end formation, distinguishing the AAUAAA signal sequence and interacting with poly(A) polymerase and further factors to bring about cleavage and poly(A) additive. CPSF4 binds RNA polymers with a preference for poly(U).

    • Synonyms

      CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1.

    • 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 MGSMQEIIAS VDHIKFDLEI AVEQQLGAQP LPFPGMDKSG AAVCEFFLKA ACGKGGMCPF RHISGEKTVV CKHWLRGLCK KGDQCEFLHE YDMTKMPECY FYSKFGECSN KECPFLHIDP ESKIKDCPWY DRGFCKHGPL CRHRHTRRVI CVNYLVGFCP EGPSCKFMHP RFELPMGTTE QPPLPQQTQP PAKQRTPQVI GVMQSQNSSA GNRGPRPLEQ VTCYKCGEKG HYANRCTKGH LAFLSGQ.

    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.

    Cpsf4 Human
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    Description:

    Corticotropin Releasing Hormone Binding Protein (22-322 a.a.) Human Recombinant

    Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

    Product # :

    HOR-025

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    Description

    CRHBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (22-322 a.a) and having a molecular mass of 36.1kDa.CRHBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRHBP protein (1mg/ml) contains 10% glycerol, 0.4M urea and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Corticotropin Releasing Hormone Binding Protein or CRHBP is a hormone that stimulates the preopiomelanocortin-derived peptides secretion & synthesis. In general, the levels of CRHBP in the human plasma are relatively low. There are times when we can find high levels of the hormone, mainly in pregnancy, after parturition the levels drop back, the high levels are thought to be derived from the placenta. CRH-binding protein can be found in the plasma, this protein inactivates CRH, in order to avoid inappropriate pituitary-adrenal stimulation during gestation.

    • Synonyms

      Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSESRYLEL REAADYDPFL LFSANLKREL AGEQPYRRAL RCLDMLSLQG QFTFTADRPQ LHCAAFFISE PEEFITIHYD QVSIDCQGGD FLKVFDGWIL KGEKFPSSQD HPLPSAERYI DFCESGLSRR SIRSSQNVAM IFFRVHEPGN GFTLTIKTDP NLFPCNVISQ TPNGKFTLVV PHQHRNCSFS IIYPVVIKIS DLTLGHVNGL QLKKSSAGCE GIGDFVELLG GTGLDPSKMT PLADLCYPFH GPAQMKVGCD NTVVRMVSSG KHVNRVTFEY RQLEPYELEN PNGNSIGEFC LSGL

    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.

    Crhbp Protein
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9

    CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    Product # :

    CYT-416

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    Description

    GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids (18-144) and having a molecular mass of 14.6kDa. GM-CSF is fused to a C-terminal His -tag (6x His) and purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    The protein was lyophilized with PBS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

    • Background

      Recombinant Granulocyte-Macrophage Colony-Stimulating Factor (GMCSF) is a protein that plays a crucial role in the production and differentiation of white blood cells, including granulocytes and macrophages. It is a potent stimulator of hematopoietic stem cells, which are responsible for the production of all blood cells in the body. Recombinant GMCSF is a synthetic version of the protein that is produced using recombinant DNA technology.

      Recombinant GMCSF has been extensively studied for its potential therapeutic applications in a variety of medical conditions, including cancer, autoimmune diseases, and infectious diseases. In cancer, GMCSF is used as an immunostimulatory agent to enhance the immune response against cancer cells. By stimulating the production and differentiation of white blood cells, GM-CSF can increase the number of immune cells that can recognize and attack cancer cells. This approach has been successfully used in the treatment of several types of cancer, including melanoma and leukemia.

      In autoimmune diseases, recombinant GMCSF has been investigated as a potential treatment for conditions such as rheumatoid arthritis and multiple sclerosis. These diseases are characterized by an overactive immune response that attacks healthy tissues in the body. By modulating the immune response, GMCSF may be able to reduce inflammation and prevent further damage to affected tissues.

      In infectious diseases, recombinant GMCSF has been studied as a potential treatment for conditions such as sepsis and HIV/AIDS. In sepsis, a severe bacterial infection, GMCSF may be able to stimulate the production of white blood cells and improve the immune response against the infection. In HIV/AIDS, GMCSF may be able to enhance the immune response against the virus and reduce the risk of opportunistic infections.

      Recombinant GMCSF is typically administered by injection, either directly into the affected tissue or into the bloodstream. It is generally well-tolerated, although some patients may experience side effects such as fever, fatigue, and muscle pain.

      In conclusion, recombinant GMCSF is a promising therapeutic agent with potential applications in a variety of medical conditions. Its ability to stimulate the production and differentiation of white blood cells makes it a valuable tool in the treatment of cancer, autoimmune diseases, and infectious diseases. Ongoing research is likely to uncover new uses for this protein and further refine its therapeutic potential.

      What is the molecular weight/Mw of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of GM- CSF HUMAN, SF9 Protein?
      Insect Cells.
      What is the Purity of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM- CSF HUMAN, SF9 Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of GM- CSF HUMAN, SF9 Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

      What applications can GM- CSF HUMAN, SF9 Protein be used in?
      GM- CSF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GM- CSF HUMAN, SF9 Protein?
      The endotoxin level is minimal, GM- CSF HUMAN, SF9 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.

    Gm Csf Human Sf9
  • View Data Sheet

    Description:

    Neurotrophin-1 Human Recombinant

    Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.

    Product # :

    CYT-869

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    Description

    Neurotrophin-1 Human Recombinant (28-225) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 199 amino acids and having a molecular mass of 22kDa.The NNT-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NNT-1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

    More Info

    • Introduction

      Cardiotrophin-like cytokine (CLC/ NNT-1) belongs to the IL-6 family of cytokines. All family members share the receptor subunit gp130, which belongs to the type I cytokine receptor superfamily. NNT1 is a trophic factor for motor neurons, a stimulator of ACTH release from corticotrophs, and an inducer of IgE synthesis and B cell proliferation. Cells expressing NNT-1 include embryonic muscle, lung epithelium, and mesenchyme. NNT1 binds to and activates the ILST/gp130 receptor.

    • Synonyms

      Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Neurotrophin-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NNT1 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 NNT1 in sterile 18M-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

    • Background

      What is the molecular weight/Mw of CLCF Protein?
      CLCF Protein has a total Mw of 22kDa.

      What is the source or expression system of CLCF Protein?
      Escherichia Coli.

      What is the Purity of CLCF Protein?
      CLCF Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CLCF Protein?
      The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

      What is the amino acid sequence of CLCF Protein?
      MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

      What applications can CLCF Protein be used in?
      CLCF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CLCF Protein?
      The endotoxin level is minimal, CLCF 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.

    Nnt1 Human
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    Description:

    Chimeric Chagas Multiantigen Recombinant

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    CCH-001

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    Description

    Recombinant Chimeric Chagas Multiantigen (MACH) (Trypanosoma cruzi) produced in E.Coli, is a polypeptide chain of 87 a.a. with epitopes PEP-2, TcD, TcE and SAPA. The protein is fused to a 6-His tag and having an Mw of 9.9kDa.

    Formulation

    Chimeric Chagas Multiantigen was lyophilized from 20mM Tris pH-8.5, 100mM Sodium chloride, 20% trehalose and 0.1% Sodium azide as preservative.

    Purity

    Protein is >90% pure as determined by metal affinity chromatography.

    More Info

    • Introduction

      Trypanosoma cruzi, better known as T. cruzi, is a deadly parasite that causes Chagas’ disease. This disease is a chronic infection, which primarily affects the heart and nervous system, causing severe neurological disorders, as well as swelling or denervation of nervous tissue in the heart, colon and esophagus. Chagas’ disease often goes undiagnosed due to close association of symptoms to heart disease and a variety of other disorders. The organism can circulate in the blood of infected patients for many years after infection, and can lead to transfusion-acquired infections in blood recipients from these infected donors. Contaminated blood transfusions are suspected to be the primary way in which the parasite has been transmitted to industrialized countries.

    • Stability

      Store lyophilized Chagas Multiantigen at 2-8°C. After reconstitution, store at -20°C. Prevent freeze/thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Chimeric Chagas Multiantigen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Applications

      Suitable for use in ELISA and Lateral flow. Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.

    • 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.

    Chimeric Chagas
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    Description:

    Carbohydrate Sulfotransferase 10 Human Recombinant

    Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.

    Product # :

    ENZ-894

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    Description

    CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHST10 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.

    • Synonyms

      Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.

    • 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

      MGSSHHHHHH SSGLVPRGSH MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.

    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.

    Chst10 Human
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    Description:

    Heme Oxygenase 1 Human Recombinant

    HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.

    Product # :

    ENZ-392

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    Description

    HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-266) and having a molecular mass of 31.4 kDa. HO-1 is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HMOX1 1 mg/ml solution containing 20mM Tris-HCl pH-8, 50mM NaCl, 0.1mM PMSF and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function and its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, and TNF-alpha in murine and human macrophages.

    • Synonyms

      HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.

    • 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

      MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH.

    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.

    Hmox1 Human
  • View Data Sheet

    Description:

    Eotaxin Rhesus Macaque Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    Product # :

    CHM-022

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    Description

    Recombinant Eotaxin Rhesus Macaque produced in E.coli cells is a non-glycosylated, homodimeric protein containing 74 amino acid chain and having a molecular mass of 8.4kDa. The Eotaxin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Eotaxin was lyophilized from a 0.2µm filtered concentrated solution in 2×PBS, pH 7.0.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood eosinophils is in a concentration range of 0.1-10.0 ng/ml corresponding to a specific activity of 1.0 × 105 - 1.0 × 107 IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Eotaxin 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 Eotaxin Recombinant in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPDSVATTCC FTLTNKKIPL QRLESYRRII SGKCPQKAVI FKTKLAKDIC ADPKKKWVQD SMKYLDRKSP TPKP

    • Background

      What is the molecular weight/Mw of EOTAXIN RHESUS MACAQUE Protein?
      EOTAXIN RHESUS MACAQUE Protein has a total Mw of 8.4kDa.

      What is the source or expression system of EOTAXIN RHESUS MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of EOTAXIN RHESUS MACAQUE Protein?
      EOTAXIN RHESUS MACAQUE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of EOTAXIN RHESUS MACAQUE Protein?
      Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood eosinophils is in a concentration range of 0.1-10.0 ng/ml corresponding to a specific activity of 1.0 × 105 - 1.0 × 107 IU/mg.

      What is the amino acid sequence of EOTAXIN RHESUS MACAQUE Protein?
      GPDSVATTCC FTLTNKKIPL QRLESYRRII SGKCPQKAVI FKTKLAKDIC ADPKKKWVQD SMKYLDRKSP TPKP

      What applications can EOTAXIN RHESUS MACAQUE Protein be used in?
      EOTAXIN RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EOTAXIN RHESUS MACAQUE Protein?
      The endotoxin level is minimal, EOTAXIN RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant EOTAXIN RHESUS MACAQUE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of EOTAXIN RHESUS MACAQUE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Eotaxin Rhesus Macaque
  • View Data Sheet

    Description:

    Macrophage-Colony Stimulating Factor Human Recombinant

    Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-308

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    Description

    Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 159 amino acids and having a total molecular mass of 37.1 KD. MCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCSF protein was lyophilized with 10mM sodium Phosphate, pH-8.0 & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependent stimulation of the proliferation of murine M-NFS-60 indicator cells was found to be 1.15ng/ml corresponding to a specific activity of 8.7x105 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. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCSF 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 MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ GHERQSEGS.

    • Background

      M-CSF (Macrophage-Colony Stimulating Factor) Human Recombinant: Unraveling Its Role in Macrophage Biology and Beyond

      Abstract:

      M-CSF (Macrophage-Colony Stimulating Factor), also known as Lanimostim, MCSF, or MGC31930, is a crucial growth factor that regulates the development, proliferation, and function of macrophages.

      This research paper aims to provide a comprehensive analysis of the molecular characteristics, signaling pathways, and diverse physiological functions of M-CSF. Additionally, it explores the therapeutic implications of M-CSF in various diseases and disorders.

      Synonyms such as Lanimostim, MCSF, and MGC31930 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a growth factor that plays a critical role in the regulation of macrophage biology. This section introduces M-CSF and its synonyms, highlighting their significance and relevance in scientific research.

      Molecular Characteristics of M-CSF:

      1. This section explores the molecular characteristics of M-CSF, including its primary amino acid sequence, protein structure, and post-translational modifications. The importance of these factors in determining M-CSF's biological activity and receptor binding is discussed.

      Signaling Pathways Activated by M-CSF:

      1. M-CSF activates specific signaling pathways upon binding to its receptor, leading to diverse cellular responses. This section focuses on the activation of the MAPK/ERK and PI3K/Akt pathways. The downstream effectors and transcriptional regulators involved in mediating M-CSF's cellular responses are also discussed.

      Physiological Functions of M-CSF:

      1. M-CSF plays critical roles in various physiological processes, particularly in macrophage development, survival, polarization, and immune regulation. This section provides an in-depth analysis of M-CSF's contributions to these processes, emphasizing its role in hematopoiesis, tissue homeostasis, wound healing, and host defense.

      Therapeutic Implications of M-CSF:

      1. The unique properties of M-CSF make it a promising therapeutic candidate for various diseases and disorders. This section discusses the potential applications of M-CSF in immunotherapy, tissue regeneration, cancer treatment, and autoimmune diseases. The challenges and future directions in utilizing M-CSF as a therapeutic agent are also explored.

      M-CSF in Disease Pathogenesis:

      1. M-CSF dysregulation is implicated in the pathogenesis of several diseases, including cancer, inflammation, and bone disorders. This section examines the role of M-CSF in promoting tumor progression, macrophage-mediated inflammation, osteoclast differentiation, and metabolic diseases. The therapeutic implications and targeting of M-CSF in disease management are also discussed.

      Conclusion:

      1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a critical growth factor involved in macrophage biology and disease pathogenesis. Understanding the molecular characteristics, signaling pathways, and physiological functions of M-CSF contributes to the exploration of its therapeutic potential in various disorders.

    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.

    M Csf Human
  • View Data Sheet

    Description:

    Hepatocyte Growth Factor Human Recombinant, CHO

    Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

    Product # :

    CYT-251

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    Description

    Hepatocyte Growth Factor Human Recombinant produced in CHO is a heterodimer, non-glycosylated, polypeptide chain consisting an a-chain of 463 amino acids and b-chain of 234 having a total molecular mass of approximately 75kDa. The HGF is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovarian Cells.

    Formulation

    The protein was lyophilized from a concentrated (1.4mg/ml) solution containing Phosphate-Buffered Saline with 0.02% Tween 80, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

    More Info

    • Introduction

      Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

    • Synonyms

      Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Hepatocyte Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Agrees with the sequence of native human HGF.

    • Background

      What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein has a total Mw of 75kDa.

      What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      Chinese Hamster Ovarian Cells.

      What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

      What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      Agrees with the sequence of native human HGF.

      What applications can HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein be used in?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN, CHO 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.

    Hgf Human Cho
  • View Data Sheet

    Description:

    Beta-Nerve Growth Factor Human Recombinant, CHO

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-246

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    Description

    Nerve Growth Factor-beta Human Recombinant produced in CHO is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.The NGF-b is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells.

    Formulation

    The protein was lyophilized from a 0.2µm filtered solution in 20mM PB and 250mM NaCl, pH 7.0.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Nerve Growth Factor b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Nerve Growth Factor-beta 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 NGF-b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Was analyzed by Mass spectrometry.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 26.5kDa.

      What is the source or expression system of B NGF Protein?
      Chinese Hamster Ovary Cells.

      What is the Purity of B NGF Protein?
      B NGF Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of B NGF Protein?
      The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.

      What is the amino acid sequence of B NGF Protein?
      B NGF Protein is composed from 118 amino acids.

      What applications can B NGF Protein be used in?
      B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for B NGF Protein?
      The endotoxin level is minimal, B NGF 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.

    Beta Ngf Human Cho
  • View Data Sheet

    Description:

    Uteroglobin Mouse Recombinant

    Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    Product # :

    CYT-746

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    Description

    Uteroglobin Mouse Recombinant produced in E.coli is a non-glycosylated disulfide-linked homodimeric protein containing 2x75 amino acids chains and having a molecular mass of 16.7kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.

    More Info

    • Introduction

      Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

    • Synonyms

      Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DICPGFLQVL EALLMESESG YVASLKPFNP GSDLQNAGTQ LKRLVDTLPQ ETRINIMKLT EKILTSPLCK QDLRF.

    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.

    Scgb1A1 Mouse
  • View Data Sheet

    Description:

    Nanog Homeobox Pseudogene 8 Human Recombinant

    Nanog Homeobox Pseudogene 8, NANOG, NANOGP1, PN8.

    Product # :

    PRO-1553

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    Description

    NANOGP8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (1-305) and having a molecular mass of 34.6kDa.NANOGP8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NANOGP8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      NANOGP8 belongs to the homeobox family of DNA binding transcription factors which is known to conserve pluripotency of embryonic stem cells. One change only separate NANOGP8 from NANOG – instead of 'Gln-253' in the inferred amino acid sequence in NANOG there is a ‘His-253’ in NANOGP8.

    • Synonyms

      Nanog Homeobox Pseudogene 8, NANOG, NANOGP1, PN8.

    • 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

      MSVDPACPQS LPCFEASDCK ESSPMPVICG PEENYPSLQM SSAEMPHTET VSPLPSSMDL LIQDSPDSST SPKGKQPTSA ENSVAKKEDK VPVKKQKTRT VFSSTQLCVL NDRFQRQKYL SLQQMQELSN ILNLSYKQVK TWFQNQRMKS KRWQKNNWPK NSNGVTQKAS APTYPSLYSS YHQGCLVNPT GNLPMWSNQT WNNSTWSNQT QNIQSWSNHS WNTQTWCTQS WNNQAWNSPF YNCGEESLQS CMHFQPNSPA SDLEAALEAA GEGLNVIQQT TRYFSTPQTM DLFLNYSMNM QPEDV

    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.

    Nanogp8 Human
  • View Data Sheet

    Description:

    Bleomycin Hydrolase Mouse Recombinant

    BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

    Product # :

    ENZ-1109

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    Description

    BLMH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 478 amino acids (1-455 aa) and having a molecular mass of 54.9 kDa.BLMH is fused to a 23 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BLMH solution (0.25 mg/ml) contains 1mM DTT, 30% Glycerol, 20mM Tris-HCl(pH8.0) and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,500 pmole/min/ug. Measured by hydrolysis of 1pmole of Met-AMC to Methionine and AMC per minute at pH7.5 at 37C˚.

    More Info

    • Introduction

      BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. BLMH shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

    • Synonyms

      BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMNNAGLN SEKVSALIQK LNSDPQFVLA QNVGTTHDLL
      DICLRRATVQ GAQHVFQHVV PQEGKPVTNQ KSSGRCWIFS CLNVMRLPFM KKFNIEEFEF
      SQSYLFFWDK VERCYFFLNA FVDTAQKKEP EDGRLVQYLL MNPTNDGGQW DMLVNIVEKY
      GVVPKKCFPE SHTTEATRRM NDILNHKMRE FCIRLRNLVH SGATKGEISS TQDAMMEEIF
      RVVCICLGNP PETFTWEYRD KDKNYHKIGP ITPLQFYKEH VKPLFNMEDK ICFVNDPRPQ
      HKYNKLYTVD YLSNMVGGRK TLYNNQPIDF LKKMVAASIK DGEAVWFGCD VGKHFNGKLG
      LSDMNVYDHE LVFGVSLKNM NKAERLAFGE SLMTHAMTFT AVSEKDNQEG TFVKWRVENS
      WGEDHGHKGY LCMTDEWFSE YVYEVVVDKK HVPEEVLAVL EQEPIVLPAW DPMGALAE

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    Blmh Mouse
  • View Data Sheet

    Description:

    Carboxylesterase 1D Mouse Recombinant

    Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    Product # :

    ENZ-1007

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    Description

    CES1D Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 555 amino acids (19-565 a.a) and having a molecular mass of 60.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1D is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1D protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 80,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to pnitrophenol per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.

    • Synonyms

      Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    • 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

      YPSSPPVVNT VKGKVLGKYV NLEGFTQPVA VFLGVPFAKP PLGSLRFAPP QPAEPWSFVK NTTSYPPMCS QDAVGGQVLS ELFTNRKENI PLQFSEDCLY LNIYTPADLT KNSRLPVMVW IHGGGLVVGG ASTYDGLALS AHENVVVVTI QYRLGIWGFF STGDEHSRGN WGHLDQVAALRWVQDNIANF GGNPGSVTIF GESAGGFSVS VLVLSPLAKN LFHRAISESG VSLTAALITT DVKPIAGLVA TLSGCKTTTS AVMVHCLRQK TEDELLETSL KLNLFKLDLL GNPKESYPFL PTVIDGVVLP KAPEEILAEK SFSTVPYIVG INKQEFGWII PTLMGYPLAE GKLDQKTANSLLWKSYPTLK ISENMIPVVA EKYLGGTDDL TKKKDLFQDL MADVVFGVPS VIVSRSHRDA GASTYMYEFE YRPSFVSAMR PKAVIGDHGD EIFSVFGSPF LKDGASEEET NLSKMVMKFW ANFARNGNPN GGGLPHWPEY DQKEGYLKIG ASTQAAQRLK DKEVSFWAEL RAKESAQRPSHREHVELLEH HHHHH.

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    Ces1D Mouse
  • View Data Sheet

    Description:

    Creatine Kinase MB Isoenzyme Type-II Human Recombinant

    Creatine Kinase MB Isoenzyme Type-II, CKMBITII, CKMBI, CKMB.

    Product # :

    CKI-270

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    Description

    CKMBITII Human Recombinant produced in Pichia Pastoris reacts with polyclonal antibodies to MB Isoenzyme in ELISA.

    Source

    Pichia Pastoris.

    Formulation

    Each mg of protein contains 10mM Tris-HCl, pH-6.8, 0.5mM EDTA and 0.5mM DTT, 50% (v/v) glycerol.

    Biological Activity

    The enzyme activity measured by kinetic assay at 340nm was 650 IU/mg at 37 degrees.

    More Info

    • Introduction

      CK-MB Type II possesses the naturally occurring carboxy-terminal amino acid lysine.
      This occurs during a myocardial infarct (MI or heart attack) when CK-MB Type II is released from damaged heart muscle, and the C-terminal lysine is cleaved in the blood stream, thus creating CK-MB Type I. This difference can be exploited in diagnosis of an MI.

    • Synonyms

      Creatine Kinase MB Isoenzyme Type-II, CKMBITII, CKMBI, CKMB.

    • Physical Appearance

      Sterile Filtered colourless liquid formulation.

    • Stability

      CKMBITII although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.

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    Ckmbitii Human
  • View Data Sheet

    Description:

    D-Dopachrome Tautomerase Mouse Recombinant

    D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

    Product # :

    ENZ-1073

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    Description

    DDT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-118 a.a) and having a molecular mass of 15.5kDa. DDT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DDT protein solution (1mg/ml) contains 20mM Tris-Hcl buffer (pH8.0) & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.

    • Synonyms

      D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

    • 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 MGSMPFVELE TNLPASRIPA GLENRLCAAT ATILDKPEDR VSVTIRPGMT LLMNKSTEPC AHLLVSSIGV VGTAEQNRTH SASFFKFLTE ELSLDQDRIV IRFFPLEAWQ IGKKGTVMTF L

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    Ddt Mouse
  • View Data Sheet

    Description:

    Cardiotrophin-1 Human Recombinant

    CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

    Product # :

    CYT-944

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    Description

    Cardiotrophin-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 21.2kDa.The CTF1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTF-1 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.

    More Info

    • Introduction

      Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
      CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
      Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
      Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.

    • Synonyms

      CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF-1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

    • Background

      Title: Cardiotrophin-1 Human Recombinant: A Potential Therapeutic Target for Cardiovascular Diseases

      Abstract:


      Cardiotrophin-1 (CT-1) is a cytokine that plays a crucial role in cardiac development and homeostasis. This research paper provides a comprehensive analysis of human recombinant CT-1, focusing on its production, characterization, and potential therapeutic implications in cardiovascular diseases. The paper discusses the significance of CT-1 in cardiac cell survival, hypertrophy, and regeneration. Furthermore, it elucidates the ongoing research and clinical trials exploring the therapeutic potential of recombinant CT-1 in cardiovascular disorders. The information presented in this paper aims to enhance the understanding of human recombinant CT-1 and its utility as a research tool and a potential therapeutic agent for cardiovascular diseases.

      Introduction:


      Cardiotrophin-1 (CT-1) is a member of the interleukin-6 cytokine family, primarily produced by cardiac cells. It exerts its effects by binding to the CT-1 receptor complex, leading to the activation of various signaling pathways. Human recombinant CT-1, produced through genetic engineering techniques, provides researchers with a valuable tool to explore its biological functions and therapeutic potential.

      Production and Characterization:


      Recombinant CT-1 is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CT-1.

      Role in Cardiovascular Physiology:


      CT-1 plays a critical role in cardiac cell survival, hypertrophy, and regeneration. It promotes cardiomyocyte growth and survival, contributing to the adaptation of the heart to stress and injury. CT-1 also exhibits angiogenic properties, stimulating the formation of new blood vessels in the heart. These functions make recombinant CT-1 an important tool for studying cardiac physiology and exploring potential therapeutic interventions.

      Therapeutic Implications:


      The dysregulation of CT-1 signaling has been implicated in various cardiovascular diseases, including heart failure, myocardial infarction, and cardiac hypertrophy. Recombinant CT-1 holds promise as a potential therapeutic agent for these conditions. Clinical trials are underway to evaluate the safety and efficacy of CT-1-based therapies, including recombinant CT-1 administration and gene therapy approaches.

      Conclusion:


      Human recombinant CT-1 is a valuable research tool and a potential therapeutic target for cardiovascular diseases. Its production, characterization, and applications in cardiac cell signaling contribute to our understanding of cardiovascular physiology and the development of novel treatments. Continued research and clinical trials exploring the therapeutic potential of recombinant CT-1 hold promise for improving outcomes in patients with cardiovascular disorders.

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 21.2kDa.

      What is the source or expression system of CTF1 Protein?
      Escherichia Coli.

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.

      What is the amino acid sequence of CTF1 Protein?
      MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

      What applications can CTF1 Protein be used in?
      CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF1 Protein?
      The endotoxin level is minimal, CTF1 Protein was purified using conventional chromatography techniques.

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    Ctf1 Human
  • View Data Sheet

    Description:

    Chromosome 20 Open Reading Frame 20 Human Recombinant

    MRG-binding protein, MRGBP, C20orf20.

    Product # :

    PRO-1000

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    Description

    C20ORF20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (1-204 a.a.) and having a molecular mass of 24.5kDa (Molecular weight on SDS-PAGE will appear higher).C20ORF20 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    C20ORF20 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.2M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      MRG-binding protein (MRGBP or C20ORF20) is a 204 amino acid protein which is a part of the NuA4 histone acetyltransferase (HAT) complex that functions to acetylate histone H2A and H4. The HAT complex may be essential for the activation of transcriptional programs linked with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. C20ORF20 also has a potential to interact with MORF4L1/MRG15 and MORF4L2/MRGX.

    • Synonyms

      MRG-binding protein, MRGBP, C20orf20.

    • Physical Appearance

      Sterile Filtered clear 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

      MGSSHHHHHH SSGLVPRGSH MGEAEVGGGG AAGDKGPGEA ATSPAEETVV WSPEVEVCLF HAMLGHKPVG VNRHFHMICI RDKFSQNIGR QVPSKVIWDH LSTMYDMQAL HESEILPFPN PERNFVLPEE IIQEVREGKV MIEEEMKEEM KEDVDPHNGA DDVFSSSGSL GKASEKSSKD KEKNSSDLGC KEGADKRKRS RVTDKVLTAN SNPSSPSAAK RRRT.

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    C20Orf20 Human
  • View Data Sheet

    Description:

    Macrophage Colony Stimulating Factor Rat Recombinant HEK

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-046

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    Description

    MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.

    Source

    HEK293

    Formulation

    The recombinant MCSF was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.

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    • 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, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCSF 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.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 MCSF in sterile PBS 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.

    M Csf Rat
  • View Data Sheet

    Description:

    Canopy FGF Signaling Regulator 1 Human Recombinant

    Protein canopy homolog 1, CNPY1.

    Product # :

    PRO-1872

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    Description

    CNPY1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-92 a.a) and having a molecular mass of 13.3kDa. CNPY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNPY1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Canopy FGF Signaling Regulator 1, also known as CNPY1, is expressed in the midbrain-hindbrain (MHB) boundary in zebrafish. CNPY1, which binds FGFR1, also takes part in FGF signaling.

    • Synonyms

      Protein canopy homolog 1, CNPY1.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMNDYKLE EDPVTKERTF KRFAPRKGDK IYQEFKKLYF YSDAYRPLKF ACETIIEEYE DEISSLIAQE THYLADKLCS EKSDLCETSA NHTEL.

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    Cnpy1 Human
  • View Data Sheet

    Description:

    Collapsin Response Mediator Protein-1 Human Recombinant

    Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, CRMP1, DPYSL1, DRP1.

    Product # :

    PRO-493

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    Description

    CRMP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa (Will appear as multiple bands on SDS-PAGE).CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRMP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol, 1mM DTT and 0.2mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.

    • Synonyms

      Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, CRMP1, DPYSL1, DRP1.

    • 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 MGSEFMSYQG KKSIPHITSD RLLIKGGRII NDDQSLYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTA ADDFFQGTRA ALVGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDVYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAITIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KLKTITAKSH KSAVEYNIFE GMECHGSPLV VISQGKIVFE DGNINVNKGM GRFIPRKAFP EHLYQRVKIR NKVFGLQGVS RGMYDGPVYE VPATPKYATP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.

    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.

    CRMP1 Human