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Search results

971 results found for “Natural Coagulation Factors”

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  • View Data Sheet

    Name :

    BDNF Human, CHO

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, CHO

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-1262

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    Description

    Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    CHO Cells

    Formulation

    The protein was lyophilized with 5% trehalose and 1x PBS

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

    sds-page

    bdnf human cho sds-page - Product image 1

    Citations

    More Info

    • Introduction

      BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
      BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

      What is the source or expression system of BDNF Protein?
      CHO Cells

      What is the Purity of BDNF Protein?
      BDNF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BDNF Protein?
      BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

      What is the amino acid sequence of BDNF Protein?
      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • References

      Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
      Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
      Link:BDNF prospec publication

    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.

    Bdnf Human Cho
  • View Data Sheet

    Name :

    GM-CSF Human, His

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, His Tag

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    Product # :

    CYT-477

    Price :

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    Description

    GMCSF Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids fragment (18-144) and having a molecular mass of 18.98kDa with an amino-terminal hexahistidine tag. GM-CSF Human Recombinant His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Granulocyte Macrophage Colony Stimulating Factor-His is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.

    Purity

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

    Citations

    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. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    • 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 GM-CSF HUMAN, HIS Protein?
      GM-CSF HUMAN, HIS Protein has a total Mw of 18.98kDa.

      What is the source or expression system of GM-CSF HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GM-CSF HUMAN, HIS Protein?
      GM-CSF HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF HUMAN, HIS Protein?
      The biological functionality of GM-CSF HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of GM-CSF HUMAN, HIS Protein?
      GM-CSF HUMAN, HIS Protein is composed from 127 amino acids.

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

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

    Gm Csf Human His
  • View Data Sheet

    Name :

    IGF1 Human, V44M

    Description:

    Insulin Like Growth Factor-1, Mutant V44M Human Recombinant

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    Product # :

    CYT-1088

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
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    • Citations

    Description

    IGF1 V44M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa. The IGF1 V44M is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IGF1 V44M Lyophilized from a 0.2 µm filtered concentrated solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      It is recommended to reconstitute the lyophilized IGF1 V44M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIMDECCFR SCDLRRLEMY
      CAPLKPAKSA

    • Background

      What is the molecular weight/Mw of IGF1 HUMAN, V44M Protein?
      IGF1 HUMAN, V44M Protein has a total Mw of 7.7kDa.

      What is the source or expression system of IGF1 HUMAN, V44M Protein?
      Escherichia Coli.

      What is the Purity of IGF1 HUMAN, V44M Protein?
      IGF1 HUMAN, V44M Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 HUMAN, V44M Protein?
      The biological functionality of IGF1 HUMAN, V44M Protein will be determined in the future.

      What is the amino acid sequence of IGF1 HUMAN, V44M Protein?
      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIMDECCFR SCDLRRLEMY.

      What applications can IGF1 HUMAN, V44M Protein be used in?
      IGF1 HUMAN, V44M Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 HUMAN, V44M Protein?
      The endotoxin level is minimal, IGF1 HUMAN, V44M 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.

    Igf1 V44M
  • View Data Sheet

    Name :

    CTGF Human, His

    Description:

    Connective Tissue Growth Factor Human Recombinant, His Tag

    CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    Product # :

    CYT-438

    Price :

    Quantity :

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    • description
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    • sds-page
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    Description

    CTGF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (27-349) and having a molecular mass of 37.7kDa.The CTGF is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTGF protein (1mg/ml) is supplied in 20mM Tris-HCl, pH-8 and 10% Glycerol.

    Purity

    Greater than 85.0% as determined by Analysis by SDS-PAGE.

    sds-page

    CTGF-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
      Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
      Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
      Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
      Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells. CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

    • Synonyms

      CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    • 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 MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.

    • Background

      What is the molecular weight/Mw of CTGF Protein?
      CTGF Protein has a total Mw of 37.7kDa.

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

      What is the Purity of CTGF Protein?
      CTGF Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTGF Protein?
      The biological functionality of CTGF Protein will be determined in the future.

      What is the amino acid sequence of CTGF Protein?
      MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.

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

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

    Ctgf Human His
  • View Data Sheet

    Name :

    TNFSF14 Mouse

    Description:

    LIGHT Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

    Product # :

    CYT-826

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    Description

    TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.

    Source

    Escherichia Coli.

    Formulation

    TNFSF14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.

    Purity

    Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cytotoxicity assay using human HT-29 cells is less than 2µg/ml, corresponding to a specific activity of > 500 IU/mg in the presence of murine anti-polyHistidine monoclonal antibody and rHuIFN-g.

    Citations

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    • Introduction

      TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFSF14 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 TNFSF14 in sterile 100mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DGGKGSWEKL IQDQRSHQAN PAAHLTGANA SLIGIGGPLL WETRLGLAFL RGLTYHDGAL VTMEPGYYYV YSKVQLSGVG CPQGLANGLP ITHGLYKRTS RYPKELELLV SRRSPCGRAN SSRVWWDSSF LGGVVHLEAG EEVVVRVPGN RLVRPRDGTR SYFGAFMV.

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    Tnfsf14 Mouse
  • View Data Sheet

    Name :

    PLGF3 Human, sf9

    Description:

    Placental Growth Factor-3 Human Recombinant, sf9

    Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

    Product # :

    CYT-961

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    Description

    PLGF3 Human Recombinant produced in Spodoptera frugiperda is a glycosylated homodimer containing 2 chains of 203 amino acids (Leu19-Arg221) and having a molecular mass of 58kDa.The PLGF-3 is purified by proprietary chromatographic techniques.

    Source

    Spodoptera frugiperda.

    Formulation

    PLGF-3 protein was lyophilized from a 0.2µm filtered solution in HCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its binding ability to rHuVEGF R1 in a functional ELISA, is less than 3ng/ml.

    Citations

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    • Introduction

      PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.

    • Synonyms

      Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PLGF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF-3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized PLGF3 in sterile 4mM HCl 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.

    Plgf3 Human
  • View Data Sheet

    Name :

    IGF1 E3R Human

    Description:

    Insulin Like Growth Factor-1, Mutant E3R Human Recombinant

    Insulin-Like Growth Factor-1.

    Product # :

    CYT-1217

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    Description

    IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Insulin-Like Growth Factor-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

    • Background

      Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.

      The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.

      The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.

      The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.

      By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related diseases.

      What is the molecular weight/Mw of IGF1 E3R HUMAN Protein?
      IGF1 E3R HUMAN Protein has a total Mw of 8.6kDa.

      What is the source or expression system of IGF1 E3R HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IGF1 E3R HUMAN Protein?
      IGF1 E3R HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 E3R HUMAN Protein?
      The biological functionality of IGF1 E3R HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IGF1 E3R HUMAN Protein?
      MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

      What applications can IGF1 E3R HUMAN Protein be used in?
      IGF1 E3R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 E3R HUMAN Protein?
      The endotoxin level is minimal, IGF1 E3R HUMAN 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.

    Igf1 Mutant
  • View Data Sheet

    Name :

    NXT1 Human

    Description:

    NTF2-like Export Factor 1 Human Recombinant

    NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.

    Product # :

    PRO-218

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    Description

    NXT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140a.a.) and having a molecular mass of 18.0kDa. The NXT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NXT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NXT1 operates as a nuclear export factor in both RAN and CRM1 dependent pathways. NXT1 is known to stimulate the export of U1 snRNA in RAN (Ras-related nuclear protein) and CRM1 (chromosome region maintenance) dependent pathways and the export of tRNA and mRNA in a CRM1-independent pathway. This protein heterodimerizes with Tap protein and regulates the ability of Tap protein to intermediate nuclear mRNA export.

    • Synonyms

      NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.

    • 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 MASVDFKTYV DQACRAAEEF VNVYYTTMDK RRRLLSRLYM GTATLVWNGN AVSGQESLSE FFEMLPSSEF QISVVDCQPV HDEATPSQTT VLVVICGSVK FEGNKQRDFN QNFILTAQAS PSNTVWKIAS DCFRFQDWAS.

    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.

    Nxt1 Human
  • View Data Sheet

    Name :

    EFNA1 Human, HEK

    Description:

    Ephrin A1 Human Recombinant, HEK

    Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    Product # :

    PRO-2477

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    Description

    EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

    • Synonyms

      Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. EFNA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS HHHHHH.

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    Efna1 Protein
  • View Data Sheet

    Name :

    Leptin qA Mouse, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Mouse Recombinant

    Product # :

    CYT-1244

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    Description

    Leptin Antagonist Quadruple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin Quadruple anatagonist Pegylated runs as a 55 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Mouse Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.  Pegylated recombinant mouse leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super mouse leptin antagonist but in vivo it has profound weight gain effect, resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

    Citations

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Quadruple Mutant Mouse 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 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin produced mainly by adipocytes. Leptin mostly regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization 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 at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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    Leptin Mouse Ta Peg
  • View Data Sheet

    Name :

    HHEX Human

    Description:

    Hematopoietically Expressed Homeobox Human Recombinant

    Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    Product # :

    PRO-1624

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    Description

    HHEX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-270) and having a molecular mass of 32.4kDa. HHEX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HHEX solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

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    • Introduction

      The homeobox protein family of transcription factors has many members that take part in developmental processes such as HHEX. HHEX is known to interact with Promyelocytic leukemia protein and expression in specific hematopoietic lines indicates that this protein is involved in hematopoietic differentiation.

    • Synonyms

      Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    • 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 MGSMQYPHPG PAAGAVGVPL YAPTPLLQPA HPTPFYIEDI LGRGPAAPTP APTLPSPNSS FTSLVSPYRT PVYEPTPIHP AFSHHSAAAL AAAYGPGGFG GPLYPFPRTV NDYTHALLRH DPLGKPLLWS PFLQRPLHKR KGGQVRFSND QTIELEKKFE TQKYLSPPER KRLAKMLQLS ERQVKTWFQN RRAKWRRLKQ ENPQSNKKEE LESLDSSCDQ RQDLPSEQNK GASLDSSQCS PSPASQEDLE SEISEDSDQE VDIEGDKSYF NAG

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    Hhex Human
  • View Data Sheet

    Name :

    HGFR Mouse

    Description:

    Hepatocyte Growth Factor Receptor Mouse Recombinant

    hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.

    Product # :

    CYT-1139

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    Description

    HGF Receptor Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 1146 amino acids (25-931aa) and having a molecular mass of 127.8kDa. HGF is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    HGF Receptor protein (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    HGFR Mouse - Product image 1

    Citations

    More Info

    • Introduction

      HGF, also known as scatter factor (SF) and Hepatocyte growth factor, is secreted from mesenchymal cells, targets and acts mainly on epithelial and endothelial cells. The protein is a paracrine cellular growth, motility and morphogenic factor. HGF can also be part of haemopoietic progenitor cells and T cells. HGF has a crucial role in embryonic organ development, mainly in myogenesis. In adults HGF takes part in organ regeneration and wound healing.

    • Synonyms

      hepatocyte growth factor receptor, HGF R/c-MET, Met, AI838057, c-Met, HGF, HGFR, Par4, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met.

    • 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

      ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

    • Background

      What is the molecular weight/Mw of HGFR MOUSE Protein?
      HGFR MOUSE Protein has a total Mw of 127.8kDa.

      What is the source or expression system of HGFR MOUSE Protein?
      Sf9, Baculovirus cells.

      What is the Purity of HGFR MOUSE Protein?
      HGFR MOUSE Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of HGFR MOUSE Protein?
      The biological functionality of HGFR MOUSE Protein will be determined in the future.

      What is the amino acid sequence of HGFR MOUSE Protein?
      ECKEALVKSE MNVNMKYQLP NFTAETPIQN VVLHGHHIYL GATNYIYVLN DKDLQKVSEF KTGPVLEHPD CLPCRDCSSK ANSSGGVWKD NINMALLVDT YYDDQLISCG SVNRGTCQRH VLPPDNSADI QSEVHCMFSP EEESGQCPDC VVSALGAKVL LSEKDRFINF FVGNTINSSY PPGYSLHSIS VRRLKETQDG FKFLTDQSYI DVLPEFQDSY PIKYIHAFES NHFIYFLTVQ KETLDAQTFH TRIIRFCSVD SGLHSYMEMP LECILTEKRR KRSTREEVFN ILQAAYVSKP GANLAKQIGA SPSDDILFGV FAQSKPDSAE PVNRSAVCAF PIKYVNDFFN KIVNKNNVRC LQHFYGPNHE HCFNRTLLRN SSGCEARSDE YRTEFTTALQ RVDLFMGRLN QVLLTSISTF IKGDLTIANL GTSEGRFMQV VLSRTAHLTP HVNFLLDSHP VSPEVIVEHP SNQNGYTLVV TGKKITKIPL NGLGCGHFQS CSQCLSAPYF IQCGWCHNQC VRFDECPSGT WTQEICLPAV YKVFPTSAPL EGGTVLTICG WDFGFRKNNK FDLRKTKVLL GNESCTLTLS ESTTNTLKCT VGPAMSEHFN VSVIISNSRE TTQYSAFSYV DPVITSISPR YGPQAGGTLL TLTGKYLNSG NSRHISIGGK TCTLKSVSDS ILECYTPAQT TSDEFPVKLK IDLANRETSS FSYREDPVVY EIHPTKSFIS GGSTITGIGK TLNSVSLPKL VIDVHEVGVN YTVACQHRSN SEIICCTTPS LKQLGLQLPL KTKAFFLLDG ILSKHFDLTY VHNPVFEPFE KPVMISIGNE NVVEIKGNNI DPEAVKGEVL KVGNQSCESL HWHSGAVLCT VPSDLLKLNS ELNIEWKQAV SSTVLGKVIV QPDQNFALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
      What applications can HGFR MOUSE Protein be used in?
      HGFR MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hgf Mouse
  • View Data Sheet

    Name :

    PDGF BB Rat

    Description:

    Platelet-Derived Growth Factor BB Rat Recombinant

    Platelet-derived growth factor subunit B, PDGF subunit B, PDGF-2, Platelet-derived growth factor B chain, Platelet-derived growth factor beta polypeptide, Pdgfb, SIS, c-sis.

    Product # :

    CYT-740

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    Description

    PDGF-BB Rat Recombinant produced in E.coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide of two B chains containing 2x109 amino acids (218 amino acids in total) and having a molecular mass of 24.4 kDa.The PDGF-BB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PDGF-BB was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.0.

    Purity

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

    Biological Activity

    The ED50as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

    Citations

    More Info

    • Introduction

      PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.

    • Synonyms

      Platelet-derived growth factor subunit B, PDGF subunit B, PDGF-2, Platelet-derived growth factor B chain, Platelet-derived growth factor beta polypeptide, Pdgfb, SIS, c-sis.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SLGSLAAAEP AVIAECKTRT EVFQISRNLI DRTNANFLVW PPCVEVQRCS GCCNNRNVQC RASQVQMRPV QVRKIEIVRK KPVFKKATVT LEDHLACKCE TVVTPRPVT.

    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.

    Pdgf Bb Rat
  • View Data Sheet

    Name :

    TNFRSF21 Human

    Description:

    TNF Ligand Receptor Superfamily Member 21 Human Recombinant

    Tumor necrosis factor receptor superfamily member 21, BM-018, CD358, DR6, Death receptor 6.

    Product # :

    CYT-1073

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    Description

    TNFRSF21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 547 amino acids (42-349a.a.) and having a molecular mass of 60.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).TNFRSF21 is expressed with a 239 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF21 protein solution (1mg/ml) contains phosphate buffered saline (pH7.4),10% glycerol and 0.1 mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor receptor superfamily member 21 or TNFRSF21, is a protein that located in the cell membrane from the TNF receptor superfamily. By activating the NF-kappaB pathway, TNFRSF21 promotes cell apoptosis. The degeneration of cells caused by activating caspase 3 and caspase 6, the TNFRSF21 binds to the N-terminal APP in neuronal cell bodies and axons which leads to apoptosis. TNFRSF21 takes part in signaling cascades activated by stimulation of T-cell receptor.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 21, BM-018, CD358, DR6, Death receptor 6.

    • 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

      QPEQKASNLI GTYRHVDRAT GQVLTCDKCP AGTYVSEHCT NTSLRVCSSC PVGTFTRHEN GIEKCHDCSQ PCPWPMIEKL PCAALTDREC TCPPGMFQSN ATCAPHTVCP VGWGVRKKGT ETEDVRCKQC ARGTFSDVPS SVMKCKAYTD CLSQNLVVIK PGTKETDNVC GTLPSFSSST SPSPGTAIFP RPEHMETHEV PSSTYVPKGM NSTESNSSAS VRPKVLSSIQ EGTVPDNTSS ARGKEDVNKT LPNLQVVNHQ QGPHHRHILK LLPSMEATGG EKSSTPIKGP KRGHPRQNLH KHFDINEHLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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    Tnfrsf21 Human
  • View Data Sheet

    Name :

    Adipsin Human, Sf9

    Description:

    Complement Factor D Human Recombinant, Sf9

    Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    Product # :

    PRO-2213

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    Description

    Adipsin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 241 amino acids (21-253a.a.) and having a molecular mass of 26.01kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). Adipsin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Adipsin protein solution (1mg/ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.

    • Synonyms

      Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    • 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

      PPRGRILGGR EAEAHARPYM ASVQLNGAHL CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS VLAVEHHHHH H.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Adipsin Human Sf9
  • View Data Sheet

    Name :

    TAF10 Human

    Description:

    TAF10 RNA Polymerase II Human Recombinant

    TAF10 RNA Polymerase II TATA Box Binding Protein (TBP)-Associated Factor 30kDa, Transcription Initiation Factor TFIID 30 KDa Subunit, STAF28, TAF2A, TAF2H.

    Product # :

    ENZ-750

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    Description

    TAF10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (84-218) and having a molecular mass of 16.9kDa.TAF10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAF10 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TAF10 is a small subunit of TFIID which is related to a subdivision of TFIID complexes. Studies with human and mammalian cells verified that this subunit is mandatory for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and is essential for several cellular differentiation programs.

    • Synonyms

      TAF10 RNA Polymerase II TATA Box Binding Protein (TBP)-Associated Factor 30kDa, Transcription Initiation Factor TFIID 30 KDa Subunit, STAF28, TAF2A, TAF2H.

    • 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 MGSGAAPPEG AISNGVYVLP SAANGDVKPV VSSTPLVDFL MQLEDYTPTI PDAVTGYYLN RAGFEASDPR IIRLISLAAQ KFISDIANDA LQHCKMKGTA SGSSRSKSKD RKYTLTMEDL TPALSEYGIN VKKPHYFT

    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.

    Taf10 Human
  • View Data Sheet

    Name :

    PGF1 Mouse

    Description:

    Placental Growth Factor-1 Mouse Recombinant

    Placenta growth factor, PlGF, PGF1.

    Product # :

    CYT-907

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    Description

    PGF1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 138 amino acids (27-158a.a.) and having a molecular mass of 15.9kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). PGF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PGF1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 0.1mM PMSF and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Placental Growth Factor, also known as PGF is rich in trophoblastic giant cells which are linked with the parietal yolk sac at early stages of embryogenesis. Furthermore, the secretion of PGF by trophoblastic giant cells is the signal which initiates as well as co-ordinates vascularization in the deciduum and placenta during early embryogenesis.

    • Synonyms

      Placenta growth factor, PlGF, PGF1.

    • 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

      AGNNSTEVEV VPFNEVWGRS YCRPMEKLVY ILDEYPDEVS HIFSPSCVLL SRCSGCCGDE GLHCVPIKTA NITMQILKIP PNRDPHFYVE MTFSQDVLCE CRPILETTKA ERRKTKGKRK RSRNSQTEEP HPHHHHHH.

    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.

    Pgf Mouse
  • View Data Sheet

    Name :

    GCSF Rat

    Description:

    Granulocyte-Colony Stimulating Factor Rat Recombinant

    Granulocyte colony stimulating factor, Protein Csf3, Csf3.

    Product # :

    CYT-940

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    Description

    GCSF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.5kDa.The G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 5mM Sodium Citrate, pH 4.0.

    Purity

    Greater than 97.0% as determined by:
    (a)Analysis by RP-HPLC.
    (b)Analysis by SDS-PAGE.

    Biological Activity

    The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

    Citations

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. 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. This csf induces granulocytes.

    • Synonyms

      Granulocyte colony stimulating factor, Protein Csf3, Csf3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

    • Background

      What is the molecular weight/Mw of G CSF RAT Protein?
      G CSF RAT Protein has a total Mw of 21.5kDa.

      What is the source or expression system of G CSF RAT Protein?
      Escherichia Coli.

      What is the Purity of G CSF RAT Protein?
      G CSF RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of G CSF RAT Protein?
      The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

      What is the amino acid sequence of G CSF RAT Protein?
      KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

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

      What is the endotoxin level for G CSF RAT Protein?
      The endotoxin level is minimal, G CSF RAT 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.

    Gcsf Rat
  • View Data Sheet

    Name :

    CSTF1 Human

    Description:

    Cleavage Stimulation Factor 1 Human Recombinant

    Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    Product # :

    PRO-1170

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    Description

    CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.

    • Synonyms

      Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    • 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

      MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.

    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.

    Cstf1 Human
  • View Data Sheet

    Name :

    SCF Mouse

    Description:

    Stem Cell Factor Mouse Recombinant

    Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.

    Product # :

    CYT-275

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    Description

    Stem Cell Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18309 Dalton. The SCF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of Human TF-1 cell line is < 10 ng/ml, corresponding to a Specific Activity of 1x105 IU/mg.

    Citations

    More Info

    • Introduction

      Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
      SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).

    • Synonyms

      Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MKEICGNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV IQLSLSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVLC MEENAPKNIK ESPKRPETRS FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.52 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Stem Cell Factor as a Reference Standard.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Scf Mouse
  • View Data Sheet

    Name :

    KLF7 (80-230) Human

    Description:

    Kruppel-Like Factor 7 (80-230) Human Recombinant

    UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.

    Product # :

    PRO-2824

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    Description

    The KLF7 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The KLF7 His-Tagged Fusion Protein, produced in E. coli, is a 22kDa protein containing 126 amino acid residues of the KLF7 Human, 80-230 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized KLF7 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Kruppel-Like Factor 7 (KLF7) which is a part of the KLF family, plays an important roles in many biological processes, including cellular proliferation, differentiation and apoptosis.

      KLF7 functions as a transcription factor, binding to specific DNA sequences to regulate gene expression.

      KLF7 takes part in the regulation of metabolic pathways, including glucose homeostasis. KLF7 modulates insulin sensitivity and plays a role in adipocyte differentiation.

      KLF7 contributes to the progression of type 2 diabetes by inhibiting hormone expression and secretion in pancreatic beta-cells and also by deregulating adipocytokine secretion in adipocytes.

      KLF7 is critical in the development and maturation of neurons. KLF7 promotes the differentiation of neural progenitor cells and influences axon growth and synaptic plasticity.

    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.

    Klf7 Protein
  • View Data Sheet

    Name :

    TNFRSF17 Human

    Description:

    B-Cell Maturation Antigen Human Recombinant

    BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

    Product # :

    CYT-598

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    Description

    TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.3 kDa. The TNFRSF17 is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1mg of TNFRSF17 Human contain 20mM sodium phosphate buffer, pH-7.4, and 130mM NaCl.

    Purity

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

    Citations

    More Info

    • Introduction

      TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.

    • Synonyms

      BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFRSF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFRSF17 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 TNFRSF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AGQCSQNEYF DSLLHACIPC QLRCSSNTPP LTCQRYCNAS VTNSVKGTNA.

    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.

    Tnfrsf17 Human
  • View Data Sheet

    Name :

    NUTF2 Human

    Description:

    Nuclear Transport Factor 2 Human Recombinant

    Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.

    Product # :

    PRO-844

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    Description

    NUTF2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 16.6 kDa. The NUTF2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUTF2 Human solution containing 20mM Tris HCL pH-8, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NUTF2 assists in protein transport into the nucleus and interacts with the nucleoporin p62 and with Ran. NUTF2 plays a role at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. NUTF2 is part of a multicomponent system of cytosolic factors that come together at the pore complex during nuclear import.

    • Synonyms

      Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.

    • 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 MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR LALHNFG.

    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.

    Nutf2 Human
  • View Data Sheet

    Name :

    BLyS Human, His

    Description:

    B cell Activating Factor Human Recombinant, His Tag

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-545

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    • sds-page
    • Citations

    Description

    BLyS Human Recombinant fused to His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (134-285 a.a.) and having a molecular mass of 21 kDa. BAFF is fused to a 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Recombinant His Tag BAFF contains PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    BLyS-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. a third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 21kDa.

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

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

      What is the Biological Activity of BLYS Protein?
      The biological functionality of BLYS Protein will be determined in the future.

      What is the amino acid sequence of BLYS Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL

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

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

    Blys Human His
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