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Back

Search results

1000 results found for “kruppel-like factor”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    BTF3 Human

    Description:

    Basic Transcription Factor 3 Human Recombinant

    Transcription factor BTF3, RNA polymerase B transcription factor 3, BTF3, NACB, BTF3a; BTF3b, BETA-NAC.

    Product # :

    PRO-1333

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    BTF3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206 a.a) and having a molecular mass of 24.6kDa.BTF3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BTF3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Basic transcription factor 3 (BTF3), which is a member of the NAC-beta family, forms a stable complex with RNA polymerase II. The BTF3 protein is vital for the initiation of transcription.

    • Synonyms

      Transcription factor BTF3, RNA polymerase B transcription factor 3, BTF3, NACB, BTF3a; BTF3b, BETA-NAC.

    • 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 MGSMRRTGAP AQADSRGRGR ARGGCPGGEA TLSQPPPRGG TRGQEPQMKE TIMNQEKLAK LQAQVRIGGK GTARRKKKVV HRTATADDKK LQFSLKKLGV NNISGIEEVN MFTNQGTVIH FNNPKVQASL AANTFTITGH AETKQLTEML PSILNQLGAD SLTSLRRLAE ALPKQSVDGK APLATGEDDD DEVPDLVENF DEASKNEAN.

    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.

    Btf3 Human
  • View Data Sheet

    Name :

    GH Carp

    Description:

    Growth Hormone Carp Recombinant

    GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-297

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    • purity
    • biological activity
    • More Info
    • Citations

    Description

    Growth Hormone Carp Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids & having a molecular mass of 21,408 Dalton. Growth Hormone Carp is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GH Carp was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.

    Purity

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

    Biological Activity

    Carp GH is biologically active in rat 3T3 F442A preadipocytes, though its activity is 15-fold lower compared to bovine GH, but it is equally potent in vivo in promoting carp growth (Fine et al.1993). Furthermore, carp GH forms 1:2 complex with the extra cellular domain of ovine growth hormone receptor.

    Citations

    More Info

    • Introduction

      Growth-Hormone is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone Carp recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Hormone Carp 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 Growth Hormone Carp recombinant 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 found to be Ser-Asp-Asn-Gln-Arg.

    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.

    Growth Hormone Carp
  • View Data Sheet

    Name :

    OSM Human

    Description:

    Oncostatin-M Human Recombinant

    OSM, MGC20461.

    Product # :

    CYT-231

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids and having a molecular mass of 26kDa. The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

    Citations

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      OSM, MGC20461.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR
      ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER
      SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP
      PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSRRHSPH
      QALRKGVRRT RPSRKGKRLM TRGQLPR.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.45 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 standard solution of Oncostatin as Reference.

    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.

    Oncostatin M Human
  • View Data Sheet

    Name :

    TFAM Human

    Description:

    Transcription Factor-A Recombinant Human

    Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.

    Product # :

    PRO-095

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    TFAM produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (43-246.a.a) and having a molecular mass of 26.6kDa. TFAM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFAM protein solution (0.25mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TFAM is a mitochondrial transcription factor which is a main activator of mitochondrial transcription and is also a participant in mitochondrial genome replication. TFAM is situated primarily in the nuclei of elongated spermatids and takes part in the regulation of gene expression of the haploid male genome. TFAM is linked to mitochondrial disorder in humans characterized by ocular myopathy, exercise intolerance and muscle wasting.

    • Synonyms

      Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSVLASCPK KPVSSYLRFS KEQLPIFKAQ NPDAKTTELI RRIAQRWREL PDSKKKIYQD AYRAEWQVYK EEISRFKEQL TPSQIMSLEK EIMDKHLKRK AMTKKKELTL LGKPKRPRSA YNVYVAERFQ EAKGDSPQEK LKTVKENWKN LSDSEKELYI QHAKEDETRY HNEMKSWEEQ MIEVGRKDLL RRTIKKQRKY GAEEC

    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.

    Tfam Human
  • View Data Sheet

    Name :

    IRF5 Human

    Description:

    IFN Regulatory Factor-5 Human Recombinant

    IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.

    Product # :

    CYT-816

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • SDS-PAGE
    • Citations

    Description

    IRF5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (176-240a.a) and having a molecular mass of 10.7kDa.IRF5 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IRF5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    SDS-PAGE

    IRF5 Human - Product image 1

    Citations

    More Info

    • Introduction

      IFN Regulatory Factor-5, also known as IRF5 belongs to the IFN regulatory factor (IRF) family, a group of transcription factors with various functions, including virus-mediated activation of IFN, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Multiple transcript variants encoding different isoforms have been found for this gene. In addition, IRF5 is implicated in the induction of IFNs IFNA and INFB and inflammatory cytokines upon virus infection. IRF5 is activated by TLR7 or TLR8 signaling.

    • Synonyms

      IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I

    • Background

      What is the molecular weight/Mw of IRF5 HUMAN Protein?
      IRF5 HUMAN Protein has a total Mw of 10.7kDa.

      What is the source or expression system of IRF5 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IRF5 HUMAN Protein?
      IRF5 HUMAN Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IRF5 HUMAN Protein?
      The biological functionality of IRF5 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IRF5 HUMAN Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I

      What applications can IRF5 HUMAN Protein be used in?
      IRF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IRF5 HUMAN Protein?
      The endotoxin level is minimal, IRF5 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.

    Irf 5 Human
  • View Data Sheet

    Name :

    PDGFD Human

    Description:

    Platelet Derived Growth Factor-D Human Recombinant

    Platelet Derived Growth Factor D, Spinal Cord-Derived Growth Factor B, Iris-Expressed Growth Factor, SCDGF-B, IEGF, PDGF-D, MSTP036.

    Product # :

    CYT-155

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    Description

    PDGFD Human Recombinant produced in E. coli is a single polypeptide chain containing 146 amino acids (250-370) and having a molecular mass of 16.6 kDa.PDGFD is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Platelet-derived growth factor D (PDGFD) belongs to the platelet-derived growth factor family. PDGFD gene product only forms homodimers and, thus, does not dimerize with the other 3 family members. PDGFD has an imperative role in wound healing. PDGFD induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. PDGFD initiates events which lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix. The 4 members of the PDGF family are mitogenic factors for cells of mesenchymal origin and are distinguished by a core motif of eight cysteines, 7 of which are found in this factor. PDGFD differs from alpha and beta members of this family by having an odd N-terminal domain, the CUB domain.

    • Synonyms

      Platelet Derived Growth Factor D, Spinal Cord-Derived Growth Factor B, Iris-Expressed Growth Factor, SCDGF-B, IEGF, PDGF-D, MSTP036.

    • 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 MGSHMSYHDR KSKVDLDRLN DDAKRYSCTP RNYSVNIREE LKLANVVFFP RCLLVQRCGG NCGCGTVNWR SCTCNSGKTV KKYHEVLQFE PGHIKRRGRA KTMALVDIQL DHHERCDCIC SSRPPR.

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    Pdgfd Human
  • View Data Sheet

    Name :

    EGF Human, Pichia

    Description:

    Epidermal Growth Factor Human Recombinant, Pichia

    Urogastrone, URG, EGF.

    Product # :

    CYT-332

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    Description

    Epidermal Growth Factor Human Recombinant produced in Pichia Pastoris is a single, glycosylated, polypeptide chain containing 51 amino acids and having a molecular mass of 6KDa.The EGF is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Lyophilized from a 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, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.

    Citations

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal 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

      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

    • Background

      Harnessing Pichia for Epidermal Growth Factor Human Recombinant Production: Novel Approaches and Therapeutic Implications

      Abstract:

      This research paper delves into a cutting-edge avenue of Epidermal Growth Factor (EGF) Human Recombinant production by leveraging Pichia as an expression host. Through a synthesis of advanced methodologies encompassing genetic engineering, fermentation, and bioinformatics, this study explores the potential of Pichia-based platforms for enhanced EGF yield and biological activity. The findings not only offer insights into efficient EGF production but also underscore the therapeutic prospects of this approach.

      Introduction:

      Epidermal Growth Factor (EGF) holds a crucial place in cellular processes. This paper explores a novel dimension of EGF Human Recombinant production utilizing Pichia expression systems, emphasizing both technical aspects and the potential impact on therapeutic applications.

      Pichia as an Expression Host:

      Pichia stands as a promising alternative to conventional expression platforms due to its robustness and eukaryotic machinery. This paper investigates the strategic integration of EGF gene into Pichia, utilizing tailored vectors and promoters for optimal protein production.

      Genetic Engineering Strategies:

      Precise genetic manipulation is pivotal for enhanced EGF yield. Gene codon optimization and signal peptide selection are meticulously undertaken to ensure proper protein folding and secretion in Pichia. Through these approaches, EGF expression and secretion are finely tuned, resulting in biologically active EGF.

      Fermentation and Protein Purification:

      Expression is followed by fermentation in controlled conditions, leading to EGF accumulation. This step is supplemented by purification processes like chromatography, ensuring high EGF purity. Biochemical assays validate the biological activity of the purified EGF, affirming its therapeutic potential.

      Bioinformatics in EGF-Pichia Interaction:

      Advanced bioinformatics analyses shed light on the intricate interactions between EGF and Pichia host. Structural modeling and molecular dynamics simulations provide insights into potential post-translational modifications and protein-protein interactions, enriching our understanding of EGF behavior in Pichia.

      Therapeutic Implications:

      Beyond production, the paper emphasizes the therapeutic significance of EGF produced in Pichia. Enhanced production efficiency directly impacts cost-effectiveness, broadening its accessibility for therapeutic use. The EGF-Pichia approach presents exciting avenues for wound healing therapies and targeted cancer interventions.

      Challenges and Future Directions:

      Despite the progress, challenges such as glycosylation patterns and scaling-up strategies remain. Future efforts should focus on refining glycosylation profiles to ensure consistent bioactivity and optimizing bioreactor designs to scale up production for clinical applications.

      Conclusion:

      In a synergy of advanced methodologies and therapeutic implications, the Pichia-based Epidermal Growth Factor Human Recombinant production presents an innovative paradigm. The intricate harmony between Pichia host and EGF production holds promise for novel therapies, underscoring the potential impact of this pioneering approach.

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 6kDa.

      What is the source or expression system of EGF Protein?
      Pichia Pastoris.

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

      What is the Biological Activity of EGF Protein?
      The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.

      What is the amino acid sequence of EGF Protein?
      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

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

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

    Egf Human Pichia
  • View Data Sheet

    Name :

    PYCRL Human

    Description:

    Pyrroline-5-Carboxylate Reductase Like Human Recombinant

    Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.

    Product # :

    ENZ-678

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    Description

    PYCRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-274) and having a molecular mass of 31kDa.PYCRL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PYCRL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pyrroline-5-Carboxylate Reductase Like (PYCRL) is a member of the pyrroline-5-carboxylate reductase family and acts as a homodecamer. PYCRL plays a key role in proline bio-synthesis. Proline serves as a non-enzymatic antioxidant to reduce damage caused by reactive oxygen species (ROS) in microorganisms, animals and plants. In the final stage of proline biosynthesis, PYCRL catalyzes the reduction of aldehyde dehydrogenase 4A1 (ALDH4A1) to proline with NAD(P)H as the cofactor.

    • Synonyms

      Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.

    • 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 MGSMAAAEPS PRRVGFVGAG RMAGAIAQGL IRAGKVEAQH ILASAPTDRN LCHFQALGCR TTHSNQEVLQ SCLLVIFATK PHVLPAVLAE VAPVVTTEHI LVSVAAGVSL STLEELLPPN TRVLRVLPNL PCVVQEGAIV MARGRHVGSS ETNLLQHLLE ACGRCEEVPE AYVDIHTGLS GSGVAFVCAF SEALAEGAVK MGMPSSLAHR IAAQTLLGTA KMLLHEGQHP AQLRSDVCTP GGTTIYGLHA LEQGGLRAAT MSAVEAATCR AKELSRK.

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    Pycrl Human
  • View Data Sheet

    Name :

    MCFD2 Human

    Description:

    Multiple Coagulation Factor Deficiency 2 Human Recombinant

    SDNSF, LMAN1IP, Multiple coagulation factor deficiency protein 2, Neural stem cell-derived neuronal survival protein, MCFD2, F5F8D, DKFZp686G21263.

    Product # :

    PRO-769

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    Description

    MCFD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (27-146 a.a.) and having a molecular wieght of 15.1kDa. The MCFD2 is is fused to 16 a.a. T7-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCFD2 protein solution contains 20mM Tris-HCl, pH-7.5, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The MCFD2-LMAN1 complex forms an explicit cargo receptor for the ER-to-Golgi transport of selected proteins. MCFD2 is involved in the secretion of coagulation factors. MCFD2 is expressed by neural stem/progenitor cells of the hippocampus, and localized to region where neurogenesis persists throughout life. MCFD2 prevents NSC cell death and maintains stem cell characteristics. MCFD2 forms a complex with LAMN1 that facilitates the transport of coagulation factors V and VIII from the endoplasmic reticulum to the Golgi apparatus through an endoplasmic reticulum Golgi intermediate compartment. Mutations in the MCFD2 cause Factor V and Factor VIII combined deficiency.

    • Synonyms

      SDNSF, LMAN1IP, Multiple coagulation factor deficiency protein 2, Neural stem cell-derived neuronal survival protein, MCFD2, F5F8D, DKFZp686G21263.

    • 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

      MASMTGGQQM GRGSHMEEPA ASFSQPGSMG LDKNTVHDQE HIMEHLEGVI NKPEAEMSPQ ELQLHYFKMH DYDGNNLLDG LELSTAITHV HKEEGSEQAP LMSEDELINI IDGVLRDDDK NNDGYIDYAE FAKSLQ.

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    Mcfd2 Human
  • View Data Sheet

    Name :

    EIF4E Human

    Description:

    Eukaryotic Translation Initiation Factor 4E Human Recombinant

    CBP, EIF4E1, EIF4EL1, EIF4F.

    Product # :

    PRO-530

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    Description

    EIF4E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular weight of 27.2kDa. The EIF4E is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF4E 0.5mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.

    • Synonyms

      CBP, EIF4E1, EIF4EL1, EIF4F.

    • 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 MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL RLISKFDTVE
      DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG
      DKIAIWTTEC ENREAVTHIG RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV.

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    Eif4E Human
  • View Data Sheet

    Name :

    Darbepoetin

    Description:

    Darbepoetin-Alpha Human Recombinant

    Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    Product # :

    CYT-1263

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    Description

    Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

    Citations

    More Info

    • Introduction

      Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.

    • Synonyms

      NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.

    • Background

      What is the molecular weight/Mw of DARBEPOETIN Protein?
      DARBEPOETIN Protein has a total Mw of 38.5kDa.

      What is the source or expression system of DARBEPOETIN Protein?
      Chinese Hamster Ovary Cells(CHO).

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

      What is the Biological Activity of DARBEPOETIN Protein?
      The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

      What is the amino acid sequence of DARBEPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

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

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

    Darbepoetin
  • View Data Sheet

    Name :

    VEGI Human, His

    Description:

    Vascular Endothelial Growth InhibitorHuman Recombinant, His Tag

    Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    Product # :

    CYT-589

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    Description

    VEGI Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids(72-251a.a.) and having a molecular mass of 22.7kDa. The VEGI is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VEGI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50% glycerol, 1mM DTT and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    • 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 MLKGQEFAPS HQQVYAPLRA DGDKPRAHLT VVRQTPTQHF KNQFPALHWE HELGLAFTKN RMNYTNKFLL IPESGDYFIY SQVTFRGMTS ECSEIRQAGR PNKPDSITVV ITKVTDSYPE PTQLLMGTKS VCEVGSNWFQ PIYLGAMFSL QEGDKLMVNV SDISLVDYTK EDKTFFGAFL L

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    Vegi Human His
  • View Data Sheet

    Name :

    TNFRSF14 Human, His

    Description:

    HVEM Human Recombinant, His Tag

    Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

    Product # :

    CYT-800

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    Description

    TNFRSF14 Human Recombinant produced in E. Coli is a single, glycosylated polypeptide chain containing 187 amino acids (39-202) and having a molecular mass of 19.7kDa.TNFRSF14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TNFRSF14 solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • 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 Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

    • 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 MGSLPSCKED EYPVGSECCP KCSPGYRVKE ACGELTGTVC EPCPPGTYIA HLNGLSKCLQ CQMCDPAMGL RASRNCSRTE NAVCGCSPGH FCIVQDGDHC AACRAYATSS PGQRVQKGGT ESQDTLCQNC PPGTFSPNGT LEECQHQTKC SWLVTKAGAG TSSSHWV.

    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.

    Tnfrsf14 Human His
  • View Data Sheet

    Name :

    YY1 Human

    Description:

    YY1 Transcription Factor Human Recombinant

    YY1 transcription factor, YY1, DELTA, INO80S, NF-E1, UCRBP, YIN-YANG-1, Transcriptional repressor protein YY1, Delta transcription factor, Yin and yang 1, INO80 complex subunit S, YY-1.

    Product # :

    PRO-2108

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    Description

    YY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 437 amino acids (1-414) and having a molecular mass of 47.1kDa.YY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YY1 solution (0.25mg/1ml) contains PBS, 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      YY1 Transcription Factor, also known as YY1, is a part of the GLI-Kruppel class of zinc finger proteins. YY1 has a positive and negative effect on a various cellular and viral genes by binding to sites overlapping the transcription start site. YY1 leads histone deacetylases and histone acetyltransferases to a promoter in order to activate or repress the promoter.

    • Synonyms

      YY1 transcription factor, YY1, DELTA, INO80S, NF-E1, UCRBP, YIN-YANG-1, Transcriptional repressor protein YY1, Delta transcription factor, Yin and yang 1, INO80 complex subunit S, YY-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 MGSMASGDTL YIATDGSEMP AEIVELHEIE VETIPVETIE TTVVGEEEEE DDDDEDGGGG DHGGGGGHGH AGHHHHHHHH HHHPPMIALQ PLVTDDPTQV HHHQEVILVQ TREEVVGGDD SDGLRAEDGF EDQILIPVPA PAGGDDDYIE QTLVTVAAAG KSGGGGSSSS GGGRVKKGGG KKSGKKSYLS GGAGAAGGGG ADPGNKKWEQ KQVQIKTLEG EFSVTMWSSD EKKDIDHETV VEEQIIGENS PPDYSEYMTG KKLPPGGIPG IDLSDPKQLA EFARMKPRKI KEDDAPRTIA CPHKGCTKMF RDNSAMRKHL HTHGPRVHVC AECGKAFVES SKLKRHQLVH TGEKPFQCTF EGCGKRFSLD FNLRTHVRIH TGDRPYVCPF DGCNKKFAQS TNLKSHILTH AKAKNNQ.

    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.

    Yy1 Human
  • View Data Sheet

    Name :

    VEGFC Human, Sf9

    Description:

    Vascular Endothelial Growth Factor C Human Recombinant, Sf9

    Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein.

    Product # :

    CYT-948

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    Description

    VEGFC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 125 amino acids (112-227a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). VEGFC is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VEGFC protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.

    • Synonyms

      Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related 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

      ADPAHYNTEI LKSIDNEWRK TQCMPREVCI DVGKEFGVAT NTFFKPPCVS VYRCGGCCNS EGLQCMNTST SYLSKTLFEI TVPLSQGPKP VTISFANHTS CRCMSKLDVY RQVHSIIRRH HHHHH.

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    Vegfc Human Sf9
  • View Data Sheet

    Name :

    NCF1 Human

    Description:

    Neutrophil Cytosolic Factor 1 Human Recombinant

    NCF1A, NOXO2, p47phox, SH3PXD1A .

    Product # :

    PRO-488

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    Description

    NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
      Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease.

    • Synonyms

      NCF1A, NOXO2, p47phox, SH3PXD1A .

    • 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

      MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

    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.

    Ncf1 Human
  • View Data Sheet

    Name :

    PDGFRB Human

    Description:

    Platelet-Derived Growth Factor Receptor, Beta Human Recombinant

    Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b AntigenNDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,Platelet-Derived Growth Factor Receptor Beta.

    Product # :

    CYT-1051

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    Description

    PDGFRB produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 739 amino acids (33-532a.a.) and having a molecular mass of 83.3kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).PDGFRB is expressed with an 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Platelet-derived growth factor receptor beta (PDGFRB), belongs to the class III subfamily of receptor tyrosine kinases (RTK) which also consist of the receptors for Flt3-ligand, SCF and M-CSF. PDGFRB takes a vital part in blood vessel development by promoting growth, migration as well as recruitment of pericytes and smooth muscle cells to endothelial cells. PDGFRB helps in rearrangement of the actin cytoskeleton in addition the formation of membrane ruffles. PDGFRB phosphorylates, NCK1, PIK3R1, PTPN11, CBL, SHC1, RASA1/GAP and PLCG1.

    • Synonyms

      Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b Antigen
      NDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,
      Platelet-Derived Growth Factor Receptor Beta.

    • 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

      LVVTPPGPEL VLNVSSTFVL TCSGSAPVVW ERMSQEPPQE MAKAQDGTFS SVLTLTNLTG LDTGEYFCTH NDSRGLETDE RKRLYIFVPD PTVGFLPNDA EELFIFLTEI TEITIPCRVT DPQLVVTLHE KKGDVALPVP YDHQRGFSGI FEDRSYICKT TIGDREVDSD AYYVYRLQVS SINVSVNAVQ TVVRQGENIT LMCIVIGNEV VNFEWTYPRK ESGRLVEPVT DFLLDMPYHI RSILHIPSAE LEDSGTYTCN VTESVNDHQD EKAINITVVE SGYVRLLGEV GTLQFAELHR SRTLQVVFEA YPPPTVLWFK DNRTLGDSSA GEIALSTRNV SETRYVSELT LVRVKVAEAG HYTMRAFHED AEVQLSFQLQ INVPVRVLEL SESHPDSGEQ TVRCRGRGMP QPNIIWSACR DLKRCPRELP PTLLGNSSEE ESQLETNVTY WEEEQEFEVV STLRLQHVDR PLSVRCTLRN AVGQDTQEVI VVPHSLPFKV LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.

    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.

    Pdgfrb Human
  • View Data Sheet

    Name :

    TRAIL Human

    Description:

    TRAIL / APO2 Ligand Human Recombinant

    Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    Product # :

    CYT-443

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    Description

    TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.

    Purity

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

    Biological Activity

    The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED50 for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.

    Citations

    More Info

    • Introduction

      TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
      In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.

    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.

    Apo2L Human
  • View Data Sheet

    Name :

    VEGF Mouse, Yeast

    Description:

    Vascular Endothelial Growth Factor Mouse Recombinant, Yeast

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-1124

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    Description

    Vascular Endothelial Growth Factor Mouse Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 40.0kDa each.VEGF is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% 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 umbilical vein endothelial cells(HUVEC) is 1.0-5.0 ng/ml.

    Citations

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both angiogenesis and vasculogenesis.VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of VEGF is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in VEGF have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vascular Endothelial Growth Factor 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 Vascular Endothelial 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

      MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

    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.

    Vegf Mouse Protein
  • View Data Sheet

    Name :

    FGF17 Human, His

    Description:

    Fibroblast Growth Factor 17 Human Recombinant, His Tag

    Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    Product # :

    CYT-755

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    Description

    FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (23-216 a.a) and having a molecular mass of 25.2kDa.FGF17 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    FGF17 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    FGF17 SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.

    • Synonyms

      Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    • 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 MGSHMTQGEN HPSPNFNQYV RDQGAMTDQL SRRQIREYQL YSRTSGKHVQ VTGRRISATA EDGNKFAKLI VETDTFGSRV RIKGAESEKY ICMNKRGKLI GKPSGKSKDC VFTEIVLENN YTAFQNARHE GWFMAFTRQG RPRQASRSRQ NQREAHFIKR LYQGQLPFPN HAEKQKQFEF VGSAPTRRTK RTRRPQPLT.

    • Background

      What is the molecular weight/Mw of FGF17 HIS Protein?
      FGF17 HIS Protein has a total Mw of 25.2kDa.

      What is the source or expression system of FGF17 HIS Protein?
      Escherichia Coli.

      What is the Purity of FGF17 HIS Protein?
      FGF17 HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF17 HIS Protein?
      The biological functionality of FGF17 HIS Protein will be determined in the future.

      What is the amino acid sequence of FGF17 HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMTQGEN HPSPNFNQYV RDQGAMTDQL SRRQIREYQL YSRTSGKHVQ VTGRRISATA EDGNKFAKLI VETDTFGSRV RIKGAESEKY ICMNKRGKLI GKPSGKSKDC VFTEIVLENN YTAFQNARHE GWFMAFTRQG RPRQASRSRQ NQREAHFIKR LYQGQLPFPN HAEKQKQFEF VGSAPTRRTK RTRRPQPLT.

      What applications can FGF17 HIS Protein be used in?
      FGF17 HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF17 HIS Protein?
      The endotoxin level is minimal, FGF17 HIS Protein was purified using conventional chromatography techniques.

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    Fgf17 Human
  • View Data Sheet

    Name :

    CXCL4 Human, His

    Description:

    Platelet Factor-4 Human Recombinant (CXCL4), His Tag

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-015

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    Description

    PF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (32-101 a.a) and having a molecular mass of 10kDa.PF4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PF4 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    CXCL4 Human, His - Product image 1

    Citations

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered colorless 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEAEEDGDLQ CLCVKTTSQV RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S.

    • Background

      What is the molecular weight/Mw of CXCL4 HUMAN, HIS Protein?
      CXCL4 HUMAN, HIS Protein has a total Mw of 10kDa.

      What is the source or expression system of CXCL4 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL4 HUMAN, HIS Protein?
      CXCL4 HUMAN, HIS Protein is > 85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL4 HUMAN, HIS Protein?
      The biological functionality of CXCL4 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL4 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MEAEEDGDLQ CLCVKTTSQV RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S.

      What applications can CXCL4 HUMAN, HIS Protein be used in?
      CXCL4 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL4 HUMAN, HIS Protein?
      The endotoxin level is minimal, CXCL4 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL4 HUMAN, HIS 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 CXCL4 HUMAN, HIS?
      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.

    Pf4 Human His
  • View Data Sheet

    Name :

    CXCL12 Mouse alpha, His

    Description:

    Stromal Cell-Derived Factor-1 alpha (CXCL12), Mouse Recombinant, His Tag

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.

    Product # :

    CHM-323

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
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    • Citations

    Description

    SDF 1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (22-89 a.a) and having a molecular mass of 10.4kDa. SDF 1a is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SDF 1a protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.

    • 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 MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.

    • Background

      What is the molecular weight/Mw of CXCL12 MOUSE ALPHA, HIS Protein?
      CXCL12 MOUSE ALPHA, HIS Protein has a total Mw of 10.4kDa.

      What is the source or expression system of CXCL12 MOUSE ALPHA, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL12 MOUSE ALPHA, HIS Protein?
      CXCL12 MOUSE ALPHA, HIS Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL12 MOUSE ALPHA, HIS Protein?
      The biological functionality of CXCL12 MOUSE ALPHA, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL12 MOUSE ALPHA, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.

      What applications can CXCL12 MOUSE ALPHA, HIS Protein be used in?
      CXCL12 MOUSE ALPHA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL12 MOUSE ALPHA, HIS Protein?
      The endotoxin level is minimal, CXCL12 MOUSE ALPHA, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL12 MOUSE ALPHA, HIS 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 CXCL12 MOUSE ALPHA, HIS?
      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.

    Sdf 1A Mouse His
  • View Data Sheet

    Name :

    TFB1M Human

    Description:

    Transcription Factor B1, Mitochondrial Human Recombinant

    Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.

    Product # :

    PRO-903

    Price :

    Quantity :

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    Description

    TFB1M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (28-346 a.a.) and having a molecular mass of 38.8kDa.TFB1M is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TFB1M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TFB1M is a member of the methyltransferase superfamily. TFB1M is a dimethyltransferase which methylates mitochondrial 12S rRNA at the conserved stem loop. The TFB1M protein also is part of the basal mitochondrial transcription complex and is required for mitochondrial gene expression. TFB1M stimulates transcription independently of the methyltransferase activity.

    • Synonyms

      Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.

    • 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 MQAAKQLSQN FLLDLRLTDK IVRKAGNLTN AYVYEVGPGP GGITRSILNA DVAELLVVEK DTRFIPGLQM LSDAAPGKLR IVHGDVLTFK VEKAFSESLK RPWEDDPPNV HIIGNLPFSV STPLIIKWLE NISCRDGPFV YGRTQMTLTF QKEVAERLAA NTGSKQRSRL SVMAQYLCNV RHIFTIPGQA FVPKPEVDVG VVHFTPLIQP KIEQPFKLVE KVVQNVFQFR RKYCHRGLRM LFPEAQRLES TGRLLELADI DPTLRPRQLS ISHFKSLCDV YRKMCDEDPQ LFAYNFREEL KRRKSKNEEK EEDDAENYRL.

    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.

    Tfb1M Human
  • View Data Sheet

    Name :

    TNF a Mouse

    Description:

    Tumor Necrosis Factor-Alpha Mouse Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-252

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    • More Info
    • Citations

    Description

    Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

    • Background

      Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.

      TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.

      In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.

      However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.

      In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.

      In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 calibrated solution of TNF-a 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.

    Tnf Alpha Mouse
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