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    Insulin-Like Growth Factor

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  • Aprotinin

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Search results

1000 results found for “Keratinocyte Growth Factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    BDNF Human, His

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, His Tag

    Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    Product # :

    CYT-881

    Price :

    Quantity :

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    • description
    • source
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    • More Info
    • sds-page

    Description

    BDNF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (129-247 a.a) and having a molecular mass of 15.8kDa. BDNF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BDNF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    BDNF-sds-page - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic 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

      MGSSHHHHHH SSGLVPRGSH MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 15.8kDa.

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

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

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

      What is the amino acid sequence of BDNF Protein?
      MGSSHHHHHH SSGLVPRGSH MHSDPARRGE 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.

    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 His
  • View Data Sheet

    Name :

    IL5 Mouse, Sf9

    Description:

    Interleukin-5 Mouse Recombinant, Sf9

    interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    Product # :

    CYT-1195

    Price :

    Quantity :

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    • description
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    • biological activity
    • More Info

    Description

    IL5 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (21-133 a.a) and having a molecular mass of 13.9kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL5 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

    • Synonyms

      interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    • 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

      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH

    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.

    Il 5 Mouse
  • View Data Sheet

    Name :

    LTF Apo Human

    Description:

    Lactoferrin Apo Human Recombinant

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-2771

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • purity
    • More Info

    Description

    Recombinant Human Apo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Apo Lactoferrin is purified by proprietary chromatographic techniques.

    Source

    Rice Flour.

    Formulation

    The Human Apo lactoferrin was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • Physical Appearance

      Pink lyophilized powder.

    • Stability

      Recombinant Apo Lactoferrin although stable at room temperature for 3 weeks, should be stored 2-8°C.

    • Solubility

      It is recommended to reconstitute the lyophilized LTF Apo Human in sterile water at 10mg/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.

    Lactoferrin Apo
  • View Data Sheet

    Name :

    CPSF4 Human

    Description:

    Cleavage And Polyadenylation Specific Factor 4 Human Recombinant

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

    Product # :

    PRO-1406

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

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

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

    Cpsf4 Human
  • View Data Sheet

    Name :

    Flt3 Ligand Porcine

    Description:

    Flt3 Ligand Porcine Recombinant

    Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    Product # :

    CYT-1041

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.

      What is the source or expression system of FLT3 LIGAND PORCINE Protein?
      Escherichia Coli.

      What is the Purity of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
      The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.

      What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

      What applications can FLT3 LIGAND PORCINE Protein be used in?
      FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
      The endotoxin level is minimal, FLT3 LIGAND PORCINE 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.

    Flt3 Ligand Porcine
  • View Data Sheet

    Name :

    GH Gilthead Seabream

    Description:

    Growth Hormone Gilthead Seabream Recombinant

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

    Product # :

    CYT-529

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    Description

    Somatotropin Gilthead Seabream Recombinant Sparus Aurata produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.4 kDa. The Gilthead Seabream Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Binding assays of the 125I-labeled gilthead seabream GH to dolphin fish liver microsomal fraction resulted in high specific binding characterized by a Ka of 1.93 nM and a Bmax of 540 fmol/mg microsomal fraction protein. Recombinant gilthead seabream Growth Hormone, like ovine placental lactogen, exhibited growth-stimulating activity when applied orally to Sparus aurata larvae or intraperitoneally to juvenile fish.

    More Info

    • Introduction

      GH 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 Gilthead Seabream although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Gilthead Seabream in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      AQPITDGQRLFSIAVSRVQHLHLLAQRLFSDFESSLQTEEQPQLNKIFLQ

      DFCNCDYIISPIDKHETQRSSVLKLLSISYRLVESWEFPSRSLSGGSAPR

      NQISPKLSELKTGIHLLIRANEDGAEIFPDRSALQLAPYGNYYQSLGTDE

      SLRRTYELLACFKKDMHKVETYLTVAKCRLSPEANCTL

    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 Seabream
  • View Data Sheet

    Name :

    FKBP3 Human

    Description:

    FK506 Binding Protein 3 Human Recombinant

    EC 5.2.1.8, FKBP-3, FKBP25, FKBP-25, Peptidyl-prolyl cis-trans isomerase FKBP3, PPIase FKBP3, FK506-binding protein 3, Rotamase, Immunophilin FKBP25, 25 kDa FK506-binding protein, 25 kDa FKBP, Rapamycin-selective 25 kDa immunophilin, FKBP3, PPIase.

    Product # :

    ENZ-495

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    Description

    FKBP3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (1-224 a.a.) and having a molecular mass of 25.1 kDa. FKBP3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FKBP3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >900 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 37C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      FKBP3 is part of a family of immunosuppressant receptors which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. FKBP3 accelerates the folding of proteins. FKBP3 is part of the immunophilin protein family, which participates in immunoregulation and fundamental cellular processes concerning protein folding and trafficking. FKBP3 is a cis-trans prolyl isomerase enzyme that binds the immunosuppressants FK506 and rapamycin, as well as histone deacetylases, the transcription factor YY1, casein kinase II, and nucleolin. It has a greater affinity for rapamycin than for FK506 and therefore is a significant protein for immunosuppression by rapamycin.

    • Synonyms

      EC 5.2.1.8, FKBP-3, FKBP25, FKBP-25, Peptidyl-prolyl cis-trans isomerase FKBP3, PPIase FKBP3, FK506-binding protein 3, Rotamase, Immunophilin FKBP25, 25 kDa FK506-binding protein, 25 kDa FKBP, Rapamycin-selective 25 kDa immunophilin, FKBP3, PPIase.

    • 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

      MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV AKTANKDHLV TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSAKKKKNAK PLSFKVGVGK VIRGWDEALL TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLTFEVEL VDID.

    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.

    Fkbp3 Human
  • View Data Sheet

    Name :

    PKIB Human

    Description:

    Protein Kinase Inhibitor Beta Human Recombinant

    cAMP-dependent protein kinase inhibitor beta, PKI-beta, PKIB, PRKACN2, FLJ23817.

    Product # :

    PKA-003

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    Description

    PKIB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids (1-78) and having a molecular mass of 10.6kDa (Molecular size on SDS-PAGE will appear higher). PKIB is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      cAMP-dependent protein kinase inhibitor beta (PKIB) belongs to the cAMP-dependent protein kinase inhibitor family. PKIB may interact with the catalytic subunit of cAMP-dependent protein kinase and function as a competitive inhibitor.

    • Synonyms

      cAMP-dependent protein kinase inhibitor beta, PKI-beta, PKIB, PRKACN2, FLJ23817.

    • 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 MRTDSSKMTD VESGVANFAS SARAGRRNAL PDIQSSAATD GTSDLPLKLE ALSVKEDAKE KDEKTTQDQL EKPQNEEK.

    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.

    Pkib Human
  • View Data Sheet

    Name :

    Placental Lactogen Caprine

    Description:

    Placental Lactogen Caprine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    Product # :

    CYT-510

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    Description

    Placental Lactogen Caprine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant Goat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Placental Lactogen Caprine is biologically active as evidenced by inducing proliferation of Nb2 cells.

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
      Placental Lactogen Goat is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized caprine recombinant placental lactogen although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of caprine recombinant placental lactogen at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization caprine recombinant placental lactogen can be stored at 4C for several weeks.

    • Solubility

      It is recommended to reconstitute the lyophilized caprine recombinant placental lactogen in sterile water or 0.4% NaHCO3 adjusted tp pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

    • Amino Acid Sequence

      The sequence of the first four N-terminal amino acids was determined and was found to be Ala-Glu-Asn-Tyr.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Placental Lactogen Caprine
  • View Data Sheet

    Name :

    NFATC2 Human

    Description:

    Nuclear Factor Of Activated T Cells 2 Human Recombinant

    Nuclear Factor Of Activated T Cells 2, Nuclear Factor Of Activated T-Cells, Cytoplasmic, Calcineurin-Dependent 2, Nuclear Factor Of Activated T-Cells 2, NFAT Pre-Existing Subunit, NF-ATc2, NFAT1, NFATP, Nuclear Factor Of Activated T-Cells, Preexisting Component , Nuclear Factor Of Activated T-Cells, Cytoplasmic 2, NFAT Transcription Complex, Preexisting Component, Preexisting Nuclear Factor Of Activated T-Cells 2, T Cell Transcription Factor NFAT1, T-Cell Transcription Factor NFAT1,  NF-ATp, NFATc2.       

    Product # :

    PRO-2535

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    Description

    NFATC2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 290 amino acids (396-678a.a.) and having a molecular mass of 33.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). NFATC2 is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NFATC2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) 40% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NFATC2, also known as nuclear factor of activated T-cells 2, belongs to the nuclear factor of activated T cells family. NFATC2 takes a significant part in the course of T helper cell differentiation, activation, and effector function. Even though KO of an individual NFAT isoform in T cells directs to rather minor effects, T cells lacking for NFATC1 and 2 totally fail to produce T helper cell effector cytokines, for instance the interleukins IL-4 and IL-2. Moreover, NFATC2 is highly phosphorylated and kept in the cytoplasm. Next T cell receptor stimulation, dephosphorylation via calcium-activated calcineurin induces a conformational modification of NFATC2 which reveals a few nuclear localization sequences.

    • Synonyms

      Nuclear Factor Of Activated T Cells 2, Nuclear Factor Of Activated T-Cells, Cytoplasmic, Calcineurin-Dependent 2, Nuclear Factor Of Activated T-Cells 2, NFAT Pre-Existing Subunit, NF-ATc2, NFAT1, NFATP, Nuclear Factor Of Activated T-Cells, Preexisting Component , Nuclear Factor Of Activated T-Cells, Cytoplasmic 2, NFAT Transcription Complex, Preexisting Component, Preexisting Nuclear Factor Of Activated T-Cells 2, T Cell Transcription Factor NFAT1, T-Cell Transcription Factor NFAT1, NF-ATp, NFATc2.

    • 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

      MPLEWPLSSQ SGSYELRIEV QPKPHHRAHY ETEGSRGAVK APTGGHPVVQ LHGYMENKPL GLQIFIGTAD ERILKPHAFY QVHRITGKTV TTTSYEKIVG NTKVLEIPLE PKNNMRATID CAGILKLRNA DIELRKGETD IGRKNTRVRL VFRVHIPESS GRIVSLQTAS NPIECSQRSA HELPMVERQD TDSCLVYGGQ QMILTGQNFT SESKVVFTEK TTDGQQIWEM EATVDKDKSQ PNMLFVEIPE YRNKHIRTPV KVNFYVINGK RKRSQPQHFT YHPVHHHHHH

    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.

    Nfatc2 Human
  • View Data Sheet

    Name :

    GFRA1 Rat

    Description:

    GDNF Family Receptor Alpha 1 Rat Recombinant

    GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    Product # :

    CYT-1012

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    Description

    GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

    • Synonyms

      GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    • 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

      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    • Background

      What is the molecular weight/Mw of GFRA1 RAT Protein?
      GFRA1 RAT Protein has a total Mw of 72.3kDa.

      What is the source or expression system of GFRA1 RAT Protein?
      Sf9, Baculovirus cells.

      What is the Purity of GFRA1 RAT Protein?
      GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA1 RAT Protein?
      The biological functionality of GFRA1 RAT Protein will be determined in the future.

      What is the amino acid sequence of GFRA1 RAT Protein?
      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

      What applications can GFRA1 RAT Protein be used in?
      GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA1 RAT Protein?
      The endotoxin level is minimal, GFRA1 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.

    Gfra1 Rat
  • View Data Sheet

    Name :

    EREG Human, His

    Description:

    Epiregulin Human Recombinant, His Tag

    Epiregulin, Proepiregulin, ER, ERP.

    Product # :

    CYT-859

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    • sds-page

    Description

    EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE

    sds-page

    EREG-sds-page - Product image 1

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      Epiregulin, Proepiregulin, ER, ERP.

    • 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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 7.7kDa.

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

      What is the Purity of EREG Protein?
      EREG Protein is >80% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of EREG Protein?
      MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

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

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

    Ereg Human His
  • View Data Sheet

    Name :

    GH Zebrafish

    Description:

    Growth Hormone Zebrafish Recombinant

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

    Product # :

    CYT-710

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    Description

    Somatotropin Zebrafish Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.18 kDa. The Zebrafish Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.05% NaHCO3 pH-8.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Zebrafish Growth-Hormone is biologically active in PDF-P1 3B9 cells stably transfected with rabbit GH receptors.

    More Info

    • Introduction

      GH 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 Zebrafish Growth-Hormone although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Zebrafish Growth-Hormone in 0.4% NaHCO3 or water adjusted to pH-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      AQRLFNNAVIRVQHLHQLAAKMINDFEEGLMPEERRQLSKIFPL

      SFCNSDSIETPTGKDETQKSSMLKLLRISFRLIESWEFPSQTLSS

      TISNSLTIGNPNLITEKLVDLKMGISVLIKGCLDGQPNMDDNDSL

      PLPFEDFYLTVGETSLRESFRLLACFKKDMHKVETYLRVANCRRSLDSNCTL

    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 Zebrafish
  • View Data Sheet

    Name :

    ASF1A Human

    Description:

    ASF1 Anti-Silencing Function 1 Homolog A Human Recombinant

    CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.

    Product # :

    PRO-682

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    Description

    ASF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-204 a.a.) and having a molecular mass of 27kDa.ASF1A is fused to a 36 amino acid His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ASF1A protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASF1A is part of the H3/H4 family of histone chaperone proteins corresponding to the anti-silencing function-1 gene in yeast. ASF1A is an important element of the histone donor complex that functions in nucleosome assembly. ASF1A interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. Deletion of ASF1A in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint.

    • Synonyms

      CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.

    • 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 KDRWGSMAKV QVNNVVVLDN PSPFYNPFQF EITFECIEDL SEDLEWKIIY VGSAESEEYD QVLDSVLVGP VPAGRHMFVF QADAPNPGLI PDADAVGVTV VLITCTYRGQ EFIRVGYYVN NEYTETELRE NPPVKPDFSK LQRNILASNPRVTRFHINWE DNTEKLEDAE SSNPNLQSLL STDALPSASK GWSTSENSLN VMLESHMDCM.

    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.

    Asf1A Human
  • View Data Sheet

    Name :

    PPIF Human

    Description:

    Cyclophilin-F Human Recombinant

    Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    Product # :

    ENZ-385

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    Description

    PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPIF solution containing 20mM Tris-HCl pH-7.5, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 250 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

    • Synonyms

      Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    • 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 CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.

    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.

    Ppif Human
  • View Data Sheet

    Name :

    Flt3 Ligand Human

    Description:

    Flt3 Ligand Human Recombinant

    Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.

    Product # :

    CYT-331

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    • sds-page

    Description

    Flt3-Ligand Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Biological Activity

    The ED50 as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×106 IU/mg.

    sds-page

    FLT3 Ligand human sds-page - Product image 1

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    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.

    • Background


      What is the molecular weight/Mw of FLT3 LIGAND HUMAN Protein?
      FLT3 LIGAND HUMAN Protein has a total Mw of 17.6kDa.

      What is the source or expression system of FLT3 LIGAND HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FLT3 LIGAND HUMAN Protein?
      FLT3 LIGAND HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND HUMAN Protein?
      The ED50 as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×106 IU/mg.

      What is the amino acid sequence of FLT3 LIGAND HUMAN Protein?
      TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.

      What applications can FLT3 LIGAND HUMAN Protein be used in?
      FLT3 LIGAND HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND HUMAN Protein?
      The endotoxin level is minimal, FLT3 LIGAND 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.

    Flt3 Human
  • View Data Sheet

    Name :

    ACVR2A Human

    Description:

    Actv Receptor Type 2A Human Recombinant

    ACVR2A, ACTRIIA, ACTR-IIA,

    Product # :

    CYT-976

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    Description

    ACVR2A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 124 amino acids (20-135a.a.) and having a molecular mass of 14.4kDa (Molecular size on SDS-PAGE will appear at approximately 28kDa.ACVR2A is fused to 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACVR2A protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    sds-page

    ACVR2A Human sds-page - Product image 1

    More Info

    • Introduction

      ACVR2A takes part in various biological processes including mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis, carcinogenesis, and inflammation. ACVR2A which is a receptor for Actv A, Actv B and inhibin A mediates induction of adipogenesis by GDF6.

    • Synonyms

      ACVR2A, ACTRIIA, ACTR-IIA,

    • 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

      AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

    • Background

      A Comprehensive Examination of the Activin Receptor Type 2A Human Recombinant: Biological Functions and Therapeutic Possibilities

      1. Abstract

      This paper delves into the complex world of Activin Receptor Type 2A Human Recombinant (ACVR2A), a crucial element of the Transforming Growth Factor-beta (TGF-beta) signaling pathway. The structure, biological implications, and signaling pathway of ACVR2A are all extensively reviewed. The potential for ACVR2A as a therapeutic target in various pathological conditions is also explored.

      2. Introduction

      The ACVR2A, a receptor protein vital to the TGF-beta signaling pathway, plays a significant role in a multitude of biological processes, including embryogenesis, cell differentiation, and homeostasis. Understanding the intricate operations of ACVR2A could open the door to innovative therapeutic strategies.

      3. Structure and Signaling of ACVR2A

      As a transmembrane serine/threonine kinase receptor, ACVR2A is characterized by a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Upon binding of specific ligands like activin, ACVR2A interacts with type I receptors to trigger phosphorylation events, leading to the activation of downstream SMAD signaling pathways.

      4. Biological Functions of ACVR2A

      ACVR2A plays a substantial role in a wide range of biological processes. These include embryonic development, cell differentiation, bone growth, immune responses, and homeostasis. Furthermore, ACVR2A is instrumental in follicle-stimulating hormone (FSH) regulation, highlighting its importance in reproduction.

      5. ACVR2A in Disease Pathology

      Impairments in ACVR2A signaling have been linked to several diseases, including various cancers and reproductive disorders. Mutations in the ACVR2A gene have been implicated in tumor progression, underscoring the receptor's role in cell proliferation and differentiation.

      6. Therapeutic Potential of ACVR2A

      The centrality of ACVR2A in critical biological processes and disease pathology suggests its therapeutic potential. By modulating ACVR2A signaling, it may be possible to intervene in diseases characterized by aberrant TGF-beta signaling. Additionally, ACVR2A antagonists are being studied for their potential in cancer treatment.

      7. Conclusion and Future Perspectives

      Our comprehension of ACVR2A's functions has substantially increased in recent years, yet much remains to be discovered. Further research into ACVR2A's precise molecular mechanisms and involvement in disease will undoubtedly yield new therapeutic strategies.

      What is the molecular weight / Mw of ACVR2A Protein?
      ACVR2A Protein has a total Mw of 14.4kDa.
      What is the source or expression system of ACVR2A Protein?
      Sf9, Baculovirus cells.

      What is the Purity of ACVR2A Protein?
      ACVR2A Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ACVR2A Protein?
      The biological functionality of ACVR2A Protein will be determined in the future.

      What is the amino acid sequence of ACVR2A Protein?
      AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

      What applications can ACVR2A Protein be used in?
      ACVR2A Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ACVR2A Protein?
      The endotoxin level is minimal, ACVR2A 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.

    Acvr2A Human
  • View Data Sheet

    Name :

    TNFRSF10C Antibody

    Description:

    TRAIL Receptor-3, Mouse Anti Human

    Tumor Necrosis Factor Receptor Superfamily, Member 10c, Decoy Without An , Intracellular Domain, TRAILR3, DCR1, TRID, TNF-Related Apoptosis-Inducing Ligand Receptor, Antagonist Decoy Receptor For TRAIL/Apo-2L, Decoy TRAIL Receptor Without Death Domain, Lymphocyte Inhibitor Of TRAIL, Decoy Receptor,TRAIL-R, LIT,Tumor Necrosis Factor Receptor Superfamily Member 10C, TRAIL Receptor Without an Intracellular Domain, Cytotoxic TRAIL Receptor, TRAIL Receptor, CD263 Antigen, DCR1-TNFR, CD263.

    Product # :

    ANT-741

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      TRAIL Receptor-3, also known as TNFRSF10C belongs to theTNF-receptor super family. TNFRSF10C contains an extracellular TRAIL-binding domain as well as a transmembranedomain, however no cytoplasmic death domain. Furthermore, TNFRSF10C is not capable of inducing apoptosis, and is considered toact as an antagonistic receptor which protects cells from TRAIL-induced apoptosis.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 10c, Decoy Without An , Intracellular Domain, TRAILR3, DCR1, TRID, TNF-Related Apoptosis-Inducing Ligand Receptor, Antagonist Decoy Receptor For TRAIL/Apo-2L, Decoy TRAIL Receptor Without Death Domain, Lymphocyte Inhibitor Of TRAIL, Decoy Receptor,TRAIL-R, LIT,Tumor Necrosis Factor Receptor Superfamily Member 10C, TRAIL Receptor Without an Intracellular Domain, Cytotoxic TRAIL Receptor, TRAIL Receptor, CD263 Antigen, DCR1-TNFR, CD263.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human TNFRSF10C mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human TNFRSF10C amino acids 26-236 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT1E12AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      TNFRSF10C antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Tnfrsf10C Antibody
  • View Data Sheet

    Name :

    APRIL Mouse

    Description:

    APRIL Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, CD256, Tnfsf13, April.

    Product # :

    CYT-803

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    Description

    APRIL Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.4 kDa. The APRIL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4, with 0.02 % Tween-20.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    Determined by a cell proliferation assay using activated T cells.

    More Info

    • Introduction

      APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines. APRIL stimulates proliferation of tumor cell lines and intensifies tumorigenicity in nude mice.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, CD256, Tnfsf13, April.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AVLTQKHKKK HSVLHLVPVN ITSKADSDVT EVMWQPVLRR GRGLEAQGDI VRVWDTGIYL LYSQVLFHDV TFTMGQVVSR EGQGRRETLF RCIRSMPSDP DRAYNSCYSA GVFHLHQGDI ITVKIPRANA KLSLSPHGTF LGFVKL.

    • Background

      What is the molecular weight/Mw of APRIL Protein?
      APRIL Protein has a total Mw of 16.4kDa.

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

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

      What is the Biological Activity of APRIL Protein?
      Determined by a cell proliferation assay using activated T cells.

      What is the amino acid sequence of APRIL Protein?
      AVLTQKHKKK HSVLHLVPVN ITSKADSDVT EVMWQPVLRR GRGLEAQGDI VRVWDTGIYL LYSQVLFHDV TFTMGQVVSR EGQGRRETLF RCIRSMPSDP DRAYNSCYSA GVFHLHQGDI ITVKIPRANA KLSLSPHGTF LGFVKL.

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

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

    April Mouse
  • View Data Sheet

    Name :

    Leptin tA Human, PEG

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant, Pegylated

    Product # :

    CYT-702

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    Description

    Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant pegylated Human Recombinant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Human Pegylated
  • View Data Sheet

    Name :

    SPP1 Human

    Description:

    Osteopontin Human Recombinant

    Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    Product # :

    CYT-635

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    Description

    Secreted Phosphoprotein-1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 321 amino acids fragment (17-314) and having a total molecular mass of 36.2 kDa(molecular weight on SDS-PAGE will shift up). The SPP1 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Osteopontin is supplied in 20mM Tris-HCl buffer pH-7.5, 1mM DTT, 2mM EDTA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
      Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

    • Synonyms

      Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.

    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.

    Spp1 Human
  • View Data Sheet

    Name :

    KLK5 Human, Sf9

    Description:

    Kallikrein-5 Human Recombinant, Sf9

    Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    Product # :

    ENZ-1021

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    Description

    Kallikrein-5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 236 amino acids (67-293 a.a.) and having a molecular mass of 26.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.

    • Synonyms

      Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    • 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

      ADLIINGSDC DMHTQPWQAA LLLRPNQLYC GAVLVHPQWL LTAAHCRKKV FRVRLGHYSL SPVYESGQQM FQGVKSIPHP GYSHPGHSND LMLIKLNRRI RPTKDVRPIN VSSHCPSAGT KCLVSGWGTT KSPQVHFPKV LQCLNISVLS QKRCEDAYPR QIDDTMFCAG DKAGRDSCQG DSGGPVVCNG SLQGLVSWGD YPCARPNRPG VYTNLCKFTK WIQETIQANS HHHHHH.

    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.

    Klk5 Human Sf9
  • View Data Sheet

    Name :

    RANGRF Human

    Description:

    RAN Guanine Nucleotide Release Factor Human Recombinant

    Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.

    Product # :

    PRO-1149

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    Description

    RANGRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-186 a.a) and having a molecular mass of 23kDa.RANGRF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RANGRF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      RANGRF is a protein which acts as a guanine nucleotide release factor in mouse and regulates the expression and function of the Nav1.5 cardiac sodium channel in human. RANGRF also controls the intracellular trafficking of RAN. In cardiac cells, the RANGRF appears to regulate the cell surface localization of SCN5A.

    • Synonyms

      Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.

    • 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 MGSHMEPTRD CPLFGGAFSA ILPMGAIDVS DLRPVPDNQE VFCHPVTDQS LIVELLELQA HVRGEAAARY HFEDVGGVQG ARAVHVESVQ PLSLENLALR GRCQEAWVLS GKQQIAKENQ QVAKDVTLHQ ALLRLPQYQT DLLLTFNQPP PDNRSSLGPE NLSPAPWSLG DFEQLVTSLT LHDPNIFGPQ.

    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.

    Rangrf Human
  • View Data Sheet

    Name :

    IL 6 Rhesus Macaque

    Description:

    Interleukin-6 Rhesus Macaque Recombinant

    IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, IFN beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    Product # :

    CYT-174

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    Description

    IL 6 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 186 amino acids and having a molecular mass of 21.1kDa.The IL 6 Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 determined by a cell proliferation assay using IL-6-dependent murine 7TD1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.

    More Info

    • Introduction

      Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.

    • Synonyms

      IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, IFN beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-6 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL-6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPVLPGEDS KNVAAPHSQP LTSSERIDKH IRYILDGISA LRKETCNRSN MCESSKEALA ENNLNLPKMA EKDGCFQSGF NEDTCLVKII TGLLEFEVYL EYLQNRFESS EEQARAVQMS TKVLIQFLQK KAKNLDAITT PEPTTNASLL TKLQAQNQWL QDMTTHLILR SFKEFLQSNL RALRQM

    • Background

      Research Paper on Interleukin-6 Rhesus Macaque Recombinant

      Abstract:

      Interleukin-6 (IL-6) Rhesus Macaque Recombinant holds a significant role in the realm of immunological exploration. This research paper delves into the molecular intricacies and implications of IL-6 Rhesus Macaque Recombinant in immune modulation. Through an investigation of its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its contribution to understanding immune responses.

      Introduction:

      IL-6 Rhesus Macaque Recombinant is a key player in immunological studies. This paper aims to provide a comprehensive understanding of its molecular attributes and its impact on immune mechanisms.

      Molecular Structure and Insights:

      Examining the molecular composition of IL-6 Rhesus Macaque Recombinant, we uncover its role in immune signaling. Its interactions and functions contribute to the fine-tuning of immune responses.

      Exploring Immune Dynamics:

      IL-6's influence on immune cell activation and inflammation is well-acknowledged. IL-6 Rhesus Macaque Recombinant provides a tool to delve deeper into these immune processes, enriching our comprehension of cytokine-mediated functions.

      Synonyms and Network Connections:

      Understanding IL-6's synonyms, such as DIF, TNFA, and TNFSF2, adds depth to our understanding of immune signaling networks. IL-6 Rhesus Macaque Recombinant helps uncover the complexity of these interconnected pathways.

      Potential Applications in Research and Beyond:

      Beyond research settings, IL-6 Rhesus Macaque Recombinant holds potential in deciphering immune-related diseases. Its significance extends to possible therapeutic interventions and diagnostic applications.

      Clinical Implications and Future Prospects:

      The clinical relevance of IL-6 Rhesus Macaque Recombinant is underlined by its role in diseases characterized by altered IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies in disease management.

      Conclusion:

      In the realm of immunology, IL-6 Rhesus Macaque Recombinant stands as a pivotal tool. Its molecular insights, pivotal functions, and potential implications position it as a valuable asset for advancing our understanding of immune regulation.

    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.

    Il 6 Rhesus Macaque
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