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1000 results found for “F-Box Protein”

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  • View Data Sheet

    Description:

    Biogenesis of Lysosomal Organelles Complex-1, Subunit 2 Human Recombinant

    Biogenesis of lysosomal organelles complex-1 subunit 2, BLOS2, BLOC-1 subunit 2, Centrosome-associated protein, centrosome protein oncogene, centrosomal 10 kDa protein, RP11-316M21.4, CEAP, FLJ30135, MGC10120.

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    PRO-1094

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    Description

    BLOC1S2 Human Recombinant produced in E. coli is a single polypeptide chain containing 166 amino acids (1-142) and having a molecular mass of 18.5kDa.BLOC1S2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BLOC1S2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      BLOC1S2 is a member of the BLOC1S2 family. Biogenesis of lysosome-related organelles complex 1 or BLOC-1 is a universally expressed multisubunit protein complex which is essential for regular biogenesis of specialized organelles of the endosomal-lysosomal system, like melanosomes and platelet dense granules. BLOC1S2 takes part in cell proliferation.

    • Synonyms

      Biogenesis of lysosomal organelles complex-1 subunit 2, BLOS2, BLOC-1 subunit 2, Centrosome-associated protein, centrosome protein oncogene, centrosomal 10 kDa protein, RP11-316M21.4, CEAP, FLJ30135, MGC10120.

    • 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 MGSHMAAAAE GVLATRSDEP ARDDAAVETA EEAKEPAEAD ITELCRDMFS KMATYLTGEL TATSEDYKLL ENMNKLTSLK YLEMKDIAIN ISRNLKDLNQ KYAGLQPYLD QINVIEEQVA ALEQAAYKLD AYSKKLEAKY KKLEKR

    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.

    Bloc1S2 Human
  • View Data Sheet

    Description:

    EPH Receptor B4 Human Recombinant

    Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.

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    PRO-2592

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    Description

    EPHB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (16-539a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 532 amino acids and having a molecular mass of 58.1 kDa. EPHB4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EPHB4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EPHB4 or Ephrin type-B receptor 4 is encoded by the EPHB4 gene in humans. The receptor and its ligands (the ephrins) take part in different developmental stages, mainly in the nervous system. EPHB4 and other Ephrin receptors are the biggest subgroup of the RTK receptors. EPHB4 binds to ephrin B2 and has a crucial part in the development of the vascular system.

    • Synonyms

      Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.

    • 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

      LEETLLNTKL ETADLKWVTF PQVDGQWEEL SGLDEEQHSV RTYEVCDVQR APGQAHWLRT GWVPRRGAVH VYATLRFTML ECLSLPRAGRSCKETFTVFY YESDADTATA LTPAWMENPY IKVDTVAAEH LTRKRPGAEA TGKVNVKTLR LGPLSKAGFY LAFQDQGACM ALLSLHLFYK KCAQLTVNLT RFPETVPREL VVPVAGSCVV DAVPAPGPSP SLYCREDGQW AEQPVTGCSC APGFEAAEGN TKCRACAQGT FKPLSGEGSC QPCPANSHSN TIGSAVCQCR VGYFRARTDP RGAPCTTPPS APRSVVSRLN GSSLHLEWSA PLESGGREDL TYALRCRECR PGGSCAPCGG DLTFDPGPRD LVEPWVVVRG LRPDFTYTFE VTALNGVSSL ATGPVPFEPV NVTTDREVPP AVSDIRVTRS SPSSLSLAWA VPRAPSGAVL DYEVKYHEKG AEGPSSVRFL KTSENRAELR GLKRGASYLV QVRARSEAGY GPFGQEHHSQ TQLDESEGWR EQLAVEHHHH HH.

    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.

    Ephb4 Human
  • View Data Sheet

    Description:

    Epigen Human Recombinant, His Tag

    EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    Product # :

    CYT-794

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    Description

    EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (23-110 a.a) and having a molecular mass of 12.1kDa.EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EPGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

    • Synonyms

      EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    • 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 MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

    • Background

      What is the molecular weight/Mw of EPIGEN Protein?
      EPIGEN Protein has a total Mw of 12.1kDa.

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

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

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

      What is the amino acid sequence of EPIGEN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

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

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

    Epgn Human His
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    Description:

    Zika Envelope Domain-III Recombinant

    Product # :

    ZKV-008

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    Description

    The E.Coli derived Zika Envelope domain-III is a non-glycosylated polypeptide chain having a molecular mass of 11 kDa and fused to a His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Zika virus (ZIKV) belongs to the family Flaviviridae and the genus Flavivirus, it is transmitted by daytime-active Aedes mosquitoes, such as A. aegypti and A. albopictus. The Zika virus is related to the dengue, yellow fever, Japanese encephalitis, and West Nile viruses. Much like the other flaviviruses, Zika virus is enveloped and icosahedral and has a nonsegmented, single-stranded, positive-sense RNA genome. Zika fever is an infection, which often causes no symptoms or only mild ones, like a mild form of dengue fever, and it is treated by rest. As of February 2016, there has been mounting evidence that Zika fever in pregnant women can cause abnormal brain development in their fetuses by mother-to-child transmission, which may result in miscarriage or microcephaly, however it is not yet known whether Zika virus causes microcephaly. Furthermore, a connection has been established with neurologic conditions in infected adults, including Guillain–Barre syndrome.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Zika Envelope between 2-8°C, do not freeze. Upon reconstitution Zika Envelope should be stored at 4°C for 6 months and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Zika Envelope Domain-3 protein in sterile 18M-cm H2O at 1mg/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.

    Zika Envelope Domain 3
  • View Data Sheet

    Description:

    Dickkopf-Related Protein 3 Human Recombinant

    Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    Product # :

    PRO-1175

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    Description

    DKK3 Human Recombinant produced in E. coli is a single polypeptide chain containing 353 amino acids (22-350) and having a molecular mass of 38.8 kDa.DKK3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DKK3 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

    • Synonyms

      Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    • 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

      MGSSHHHYHH SSGLVPRGSH MGSMAPAPTA TSAPVKPGPA LSYPQEEATL NEMFREVEEL MEDTQHKLRS AVEEMEAEEA AAKASSEVNL ANLPPSYHNE TNTDTKVGNN TIHVHREIHK ITNNQTGQMV FSETVITSVG DEEGRRSHEC IIDEDCGPSM YCQFASFQYT CQPCRGQRML CTRDSECCGD QLCVWGHCTK MATRGSNGTI CDNQRDCQPG LCCAFQRGLL FPVCTPLPVE GELCHDPASR LLDLITWELE PDGALDRCPC ASGLLCQPHS HSLVYVCKPT FVGSRDQDGE ILLPREVPDE YEVGSFMEEV RQELEDLERS LTEEMALREP AAAAAALLGG EEI

    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.

    Dkk3 Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-23 Human Recombinant, Sf9

    Fibroblast growth factor 23, FGF-23, Phosphatonin, Tumor-derived hypophosphatemia-inducing factor, HYPF.

    Product # :

    CYT-1102

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    • sds-page

    Description

    FGF23 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 236 amino acids (25-251a.a.) and having a molecular mass of 26.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).FGF23 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    FGF23 protein solution (0.25mg/ml) containsPhosphate Buffered Saline (pH 7.4), 2mM DTT, 1mM EDTA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, tissue repair, morphogenesis, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. a high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism.

    • Synonyms

      Fibroblast growth factor 23, FGF-23, Phosphatonin, Tumor-derived hypophosphatemia-inducing factor, HYPF.

    • 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

      ADPYPNASPL LGSSWGGLIH LYTATARNSY HLQIHKNGHV DGAPHQTIYS ALMIRSEDAG
      FVVITGVMSR RYLCMDFRGN IFGSHYFDPE NCRFQHQTLE NGYDVYHSPQ YHFLVSLGRA
      KRAFLPGMNP PPYSQFLSRR NEIPLIHFNT PIPRRHTRSA EDDSERDPLN VLKPRARMTP
      APASCSQELP SAEDNSPMAS DPLGVVRGGR VNTHAGGTGP EGCRPFAKFI HHHHHH.

    • Background

      What is the molecular weight/Mw of FGF23 HUMAN, SF9 Protein?
      FGF23 HUMAN, SF9 Protein has a total Mw of 26.4kDa.

      What is the source or expression system of FGF23 HUMAN, SF9 Protein?
      Sf9, Insect cells.
      What is the Purity of FGF23 HUMAN, SF9 Protein?
      FGF23 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF23 HUMAN, SF9 Protein?
      The biological functionality of FGF23 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of FGF23 HUMAN, SF9 Protein?
      ADPYPNASPL LGSSWGGLIH LYTATARNSY HLQIHKNGHV DGAPHQTIYS ALMIRSEDAG
      FVVITGVMSR RYLCMDFRGN IFGSHYFDPE NCRFQHQTLE NGYDVYHSPQ YHFLVSLGRA
      KRAFLPGMNP PPYSQFLSRR NEIPLIHFNT PIPRRHTRSA EDDSERDPLN VLKPRARMTP
      APASCSQELP SAEDNSPMAS DPLGVVRGGR VNTHAGGTGP EGCRPFAKFI HHHHHH.
      What applications can FGF23 HUMAN, SF9 Protein be used in?
      FGF23 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF23 HUMAN, SF9 Protein?
      The endotoxin level is minimal, FGF23 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

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

    Fgf 23 Protein
  • View Data Sheet

    Description:

    Kallikrein-13 Human Recombinant, sf9

    Kallikrein-Related Peptidase 13, KLKL4, Kallikrein-Like Protein 4, Kallikrein 13, KLK-L4, Kallikrein-Like Gene 4, Kallikrein-13, EC 3.4.21.-, EC 3.4.21, Kallikrein-13.

    Product # :

    ENZ-911

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    Description

    KLK13 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (17-277a.a.) and having a molecular mass of 29.7kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). KLK13 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK13 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 8,000 pmol/min/ug. One unit will hydrolyze 1.0 pmole of BAEE to Na-Benzoyl-L-arginine per minute at pH8.0 at 25C.

    More Info

    • Introduction

      Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.

    • Synonyms

      Kallikrein-Related Peptidase 13, KLKL4, Kallikrein-Like Protein 4, Kallikrein 13, KLK-L4, Kallikrein-Like Gene 4, Kallikrein-13, EC 3.4.21.-, EC 3.4.21, Kallikrein-13.

    • 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

      GGVSQESSKV LNTNGTSGFL PGGYTCFPHS QPWQAALLVQ GRLLCGGVLV HPKWVLTAAH CLKEGLKVYL GKHALGRVEA GEQVREVVHS IPHPEYRRSP THLNHDHDIM LLELQSPVQL TGYIQTLPLS HNNRLTPGTT CRVSGWGTTT SPQVNYPKTL QCANIQLRSD EECRQVYPGK ITDNMLCAGT KEGGKDSCEG DSGGPLVCNR TLYGIVSWGD FPCGQPDRPG VYTRVSRYVL WIRETIRKYE TQQQKWLKGP QHHHHHH.

    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.

    Klk13 Human Sf9
  • View Data Sheet

    Description:

    Sprouty-Related EVH1 Domain Containing 1 Human Recombinant

    Sprouty-Related EVH1 Domain Containing 1, SPRED1, Spred-1, hSpred1, NFLS.

    Product # :

    PRO-2107

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    Description

    SPRED1 Human Recombinant produced in E. coli is a single polypeptide chain containing 467 amino acids (1-444) and having a molecular mass of 52.9kDa.SPRED1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPRED1 solution (0.5mg/1ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sprouty-Related EVH1 Domain Containing 1, also known as SPRED1, is a part of the Sprouty family of proteins and is phosphorylated by tyrosine kinase. SPRED1 inhibits growth-factor-mediated activation of MAP kinase. SPRED1 plays a role as a homodimer or as a heterodimer with SPRED2 to regulate activation of the MAP kinase cascade. SPRED1 is a negative regulator of hematopoiesis of bone marrow.

    • Synonyms

      Sprouty-Related EVH1 Domain Containing 1, SPRED1, Spred-1, hSpred1, NFLS.

    • 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 MGSMSEETAT SDNDNSYARV RAVVMTRDDS SGGWLPLGGS GLSSVTVFKV PHQEENGCAD FFIRGERLRD KMVVLECMLK KDLIYNKVTP TFHHWKIDDK KFGLTFQSPA DARAFDRGIR RAIEDISQGC PESKNEAEGA DDLQANEEDS SSSLVKDHLF QQETVVTSEP YRSSNIRPSP FEDLNARRVY MQSQANQITF GQPGLDIQSR SMEYVQRQIS KECGSLKSQN RVPLKSIRHV SFQDEDEIVR INPRDILIRR YADYRHPDMW KNDLERDDAD SSIQFSKPDS KKSDYLYSCG DETKLSSPKD SVVFKTQPSS LKIKKSKRRK EDGERSRCVY CQERFNHEEN VRGKCQDAPD PIKRCIYQVS CMLCAESMLY HCMSDSEGDF SDPCSCDTSD DKFCLRWLAL VALSFIVPCM CCYVPLRMCH RCGEACGCCG GKHKAAG.

    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.

    Spred1 Human
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    Description:

    EPH Receptor B4 Mouse Recombinant

    Ephrin type-B receptor 4 (EC:2.7.10.1), Developmental kinase 2, mDK-2, Hepatoma transmembrane kinase, Tyrosine kinase MYK-1, Ephb4, Htk, Mdk2, Myk1.

    Product # :

    PRO-2344

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    Description

    EPHB4 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 532 amino acids (16-539 a.a.) and having a molecular mass of 58.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).EPHB4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EPHB4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      Ephrin type-B receptor 4 isoform b (Ephb4) belongs to the Eph receptor tyrosine kinase family which functions in neuronal guidance and mediate venal/arterial separation. EPHB4-mediated forward signaling regulates cellular repulsion and segregation form EFNB2-expressing cells. Furthermore, Ephb4 has a role in postnatal blood vessel remodeling, morphogenesis and permeability and is therefore essential in the context of tumor angiogenesis.

    • Synonyms

      Ephrin type-B receptor 4 (EC:2.7.10.1), Developmental kinase 2, mDK-2, Hepatoma transmembrane kinase, Tyrosine kinase MYK-1, Ephb4, Htk, Mdk2, Myk1.

    • 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

      LEETLLNTKLETADLKWVTYPQAEGQWEELSGLDEEQHSVRTYEVCDMKRPGGQAHWLRT
      GWVPRRGAVHVYATIRFTMMECLSLPRASRSCKETFTVFYYESEADTATAHTPAWMENPY
      IKVDTVAAEHLTRKRPGAEATGKVNIKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYK
      KCSWLITNLTYFPETVPRELVVPVAGSCVANAVPTANPSPSLYCREDGQWAEQQVTGCSC
      APGYEAAESNKVCRACGQGTFKPQIGDESCLPCPANSHSNNIGSPVCLCRIGYYRARSDP
      RSSPCTTPPSAPRSVVHHLNGSTLRLEWSAPLESGGREDLTYAVRCRECRPGGSCLPCGG
      DMTFDPGPRDLVEPWVAIRGLRPDVTYTFEVAALNGVSTLATGPPPFEPVNVTTDREVPP
      AVSDIRVTRSSPSSLILSWAIPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELR
      GLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESESWREQLAVEHHHHHH.

    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.

    Ephb4 Mouse
  • View Data Sheet

    Description:

    TNF Ligand Receptor Superfamily Member 12A Human Recombinant, Sf9

    Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

    Product # :

    CYT-1021

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    Description

    TNFRSF12A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (28-80a.a.) and having a molecular mass of 32.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). TNFRSF12A is expressed with a 239 amino acids hIgG- His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF12A protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The gene for TNFRSF12A was initially recognized as a fibroblast growth factor inducible immediate early response gene Fn14 in mouse NIH 3T3 fibroblasts. Human TNFRSF12A cDNA encodes a 129 amino acid residue type I transmembrane protein with a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. Human and mouse TNFRSF12A hold 82% aa sequence identity. TNFRSF12 is the tiniest member of the TNF receptor superfamily and has only one cysteine rich region in its extracellular domain. The TNFRSF12A cytoplasmic domain holds one TRAF binding motif which binds TRAFs 1, 2, and 3. TNFRSF12A binds its ligand TWEAK/TNFSF12A with high affinity to initiate a signal transduction cascade which subject to the cell type, causes different cellular responses such as cell death, cell proliferation, and angiogenesis.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

    • 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

      EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWPLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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    Tnfrsf12A Protein
  • View Data Sheet

    Description:

    MOB1, Mps One Binder Kinase Activator-Like 1B Human Recombinant

    Mps one binder kinase activator-like 1B, Mob1 alpha, Mob1A, Mob1 homolog 1B, Protein Mob4B, MOBKL1B, C2orf6, MOB4B, MOBK1B, MOB1, MATS1, FLJ10788, FLJ11595.

    Product # :

    PRO-068

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    Description

    MOBKL1B Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 27.2kDa. The MOBKL1B is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MOBKL1B solution (0.5mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MOBKL1B is a member of the MOB1/phocein family. MOBKL1B stimulates the kinase activity of STK38 and STK38L. MOBKL1B also binds to and regulates downstream targets such as the NDR-family protein kinases and LATS1 kinase. Thus, MOBKL1B participates in cell cycle checkpoint control and tumor inhibition.

    • Synonyms

      Mps one binder kinase activator-like 1B, Mob1 alpha, Mob1A, Mob1 homolog 1B, Protein Mob4B, MOBKL1B, C2orf6, MOB4B, MOBK1B, MOB1, MATS1, FLJ10788, FLJ11595.

    • 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 MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG EDLNEWIAVN TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG TNIKKPIKCS APKYIDYLMT WVQDQLDDET LFPSKIGVPF PKNFMSVAKT ILKRLFRVYA HIYHQHFDSV MQLQEEAHLN TSFKHFIFFV QEFNLIDRRE LAPLQELIEK LGSKDR.

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    Mobkl1B Human
  • View Data Sheet

    Description:

    EGF Like Domain Multiple 6 Mouse Recombinant

    Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.

    Product # :

    CYT-1105

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    Description

    EGFL6 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 273 amino acids (287-550a.a.) and having a molecular mass of 31.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EGFL6 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    EGFL6 protein solution ( 0.5mg/ml ) contains Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Epidermal Growth Factor­like Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

    • Synonyms

      Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.

    • 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

      ADLTMKKKVK LKMVTPRPAS TRVPKVNLPY SSEEGVSRGR NYDGEQKKKE EGKRERLEEE
      KGEKTLRNEV EQERTLRGDV FSPKVNEAED LDLVYVQRKE LNSKLKHKDL NISVDCSFDL
      GVCDWKQDRE DDFDWHPADR DNDVGYYMAV PALAGHKKNI GRLKLLLPNL TPQSNFCLLF
      DYRLAGDKVG KLRVFVKNSN NALAWEETKN EDGRWRTGKI QLYQGIDTTK SVIFEAERGK GKTGEIAVDG VLLVSGLCPD DFLSVEGHHH HHH.

    • Background

      Title: EGF-Like Domain Multiple 6 Mouse Recombinant: Insights into its Biological Significance and Potential Applications

      Abstract:


      EGF-Like Domain Multiple 6 (EGFL6) is a critical protein involved in various biological processes, including development, tissue homeostasis, and cancer progression. This research paper provides a comprehensive analysis of mouse recombinant EGFL6, focusing on its production, characterization, and potential applications in studying its biological functions. The paper highlights the significance of EGFL6 in cellular processes and its role in disease pathogenesis. Furthermore, it discusses ongoing research and potential therapeutic applications of recombinant EGFL6 in cancer and regenerative medicine. The information presented in this paper aims to enhance our understanding of mouse recombinant EGFL6 and its utility as a research tool and a potential therapeutic agent.

      Introduction:


      EGF-Like Domain Multiple 6 (EGFL6) is a secreted protein that belongs to the epidermal growth factor (EGF) family. Mouse recombinant EGFL6, produced through genetic engineering techniques, provides a valuable tool for investigating its biological functions and potential therapeutic applications.

      Production and Characterization:


      Recombinant EGFL6 is typically generated using expression systems such as bacteria or mammalian cells. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EGFL6.

      Biological Significance:


      EGFL6 plays a crucial role in diverse cellular processes, including angiogenesis, tissue regeneration, and cell proliferation. It is involved in the modulation of signaling pathways, such as the Wnt/β-catenin pathway, and interacts with extracellular matrix components. Recombinant EGFL6 offers a valuable tool for investigating the molecular mechanisms underlying its biological functions and its involvement in disease pathogenesis.

      Role in Cancer:


      EGFL6 is implicated in cancer progression and metastasis. It promotes tumor angiogenesis, invasion, and resistance to chemotherapy. Studies utilizing recombinant EGFL6 can contribute to a better understanding of its role in tumor microenvironment remodeling and the development of targeted therapeutic strategies.

      Therapeutic Implications:


      Given its involvement in various cellular processes and disease pathogenesis, EGFL6 has emerged as a potential therapeutic target. Recombinant EGFL6-based therapies, such as antibody-based approaches or small molecule inhibitors, hold promise for cancer treatment and regenerative medicine. Ongoing research is focused on developing strategies to modulate EGFL6 activity for therapeutic benefit.

      Conclusion:


      Mouse recombinant EGFL6 serves as a valuable research tool for studying its biological functions and exploring its therapeutic potential. Its production, characterization, and applications in understanding cellular processes and disease pathogenesis contribute to our knowledge of EGFL6 biology and the development of targeted interventions. Continued research and clinical investigations exploring the therapeutic applications of recombinant EGFL6 offer promising avenues for improving outcomes in cancer and regenerative medicine.

      What is the molecular weight/Mw of EGFL6 MOUSE Protein?
      EGFL6 MOUSE Protein has a total Mw of 31.1kDa.

      What is the source or expression system of EGFL6 MOUSE Protein?
      Sf9, Insect cells.

      What is the Purity of EGFL6 MOUSE Protein?
      EGFL6 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of EGFL6 MOUSE Protein?
      The biological functionality of EGFL6 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of EGFL6 MOUSE Protein?
      EGFL6 MOUSE Protein is composed from 273 amino acids.

      What applications can EGFL6 MOUSE Protein be used in?
      EGFL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EGFL6 MOUSE Protein?
      The endotoxin level is minimal, EGFL6 MOUSE Protein was purified using conventional chromatography techniques.

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

    Egfl6 Mouse
  • View Data Sheet

    Description:

    Mucin-16 (CA125) Human

    Product # :

    PRO-2746

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    Description

    The Human Mucin-16 (CA125) was purified from Human carcinoma cell line.

    Source

    Human carcinoma cell line.

    Formulation

    MUC16 is supplied in a 0.05M sodium phosphate buffer, pH 7.5, 0.09% NaN3 and 0.15M NaCl.

    Purity

    Greater than 60%.

    More Info

    • Introduction

      MUC16, aka CA125, is a mucin protein that might be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.
      The CA125 molecule is heterogeneous with regard to both size and charge, almost certainly due to continuous deglycosylation of side chains during its life-span in bodily fluids.
      MUC16 is most likely a glycoprotein with a predominance of O-linkages.

    • Physical Appearance

      Clear colorless to pale blue frozen solution.

    • Stability

      Human MUC16 although stable at 4°C for 1 week, should be stored at -20°C.

    • Human Virus Test

      Tissue sample tested and found negative for HIV-1 & 2 antibodies, HBsAg, and Hepatitis-C antibodies.

    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.

    Ca125 Muc16 Human
  • View Data Sheet

    Description:

    Allergenic Isoflavone Reductase-Like Protein Bet v 6.0102 Recombinant

    Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.

    Product # :

    ALR-018

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    Description

    Recombinant BETV6.0102 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 36,636 Dalton. BETV6.0102 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    BETV6.0102 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BETV6.0102 allergen is one of Isoflavone reductases which were found in pear, orange, apple, mango, lychee and other plants. Isoflavone reductases are plant defense proteins which induced by plant stress, e.g. high salinity, freeze or drought.

    • Synonyms

      Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

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    Betv60102
  • View Data Sheet

    Description:

    Angiotensin Converting Enzyme Human Recombinant

    Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143

    Product # :

    ENZ-1156

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    Description

    ACE Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1235 amino acids (30-1256 a.a.) and having a molecular mass of 142kDa. ACE is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACE 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.

    Biological Activity

    Specific activity is > 1,000 pmol/min/mg. Defined by the amount of enzyme that cleaves 1pmol of McaRPPGFSAFK(Dnp)-OH per minute at 25C˚.

    More Info

    • Introduction

      Angiotensin Converting Enzyme (ACE) is a zinc metallopeptidase vital for blood pressure control and salt and water metabolism.ACE converts angiotensin I to angiotensin II by release of the terminal His-Leu which causes the vasoconstrictor activity of angiotensin to increase.ACE inactivates bradykinin, a potent vasodilator and has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.

    • Synonyms

      Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143

    • 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

      LDPGLQPGNF SADEAGAQLF AQSYNSSAEQ VLFQSVAASW AHDTNITAEN ARRQEEAALL SQEFAEAWGQ KAKELYEPIW QNFTDPQLRR IIGAVRTLGS ANLPLAKRQQ YNALLSNMSR IYSTAKVCLP NKTATCWSLD PDLTNILASS RSYAMLLFAW EGWHNAAGIP LKPLYEDFTA LSNEAYKQDG FTDTGAYWRS WYNSPTFEDD LEHLYQQLEP LYLNLHAFVR RALHRRYGDR YINLRGPIPA HLLGDMWAQS WENIYDMVVP FPDKPNLDVT STMLQQGWNA THMFRVAEEF FTSLELSPMP PEFWEGSMLE KPADGREVVC HASAWDFYNR KDFRIKQCTR VTMDQLSTVH HEMGHIQYYL QYKDLPVSLR RGANPGFHEA IGDVLALSVS TPEHLHKIGL LDRVTNDTES DINYLLKMAL EKIAFLPFGY LVDQWRWGVF SGRTPPSRYN FDWWYLRTKY QGICPPVTRN ETHFDAGAKF HVPNVTPYIR YFVSFVLQFQ FHEALCKEAG YEGPLHQCDI YRSTKAGAKL RKVLQAGSSR PWQEVLKDMV GLDALDAQPL LKYFQPVTQW LQEQNQQNGE VLGWPEYQWH PPLPDNYPEG IDLVTDEAEA SKFVEEYDRT SQVVWNEYAE ANWNYNTNIT TETSKILLQK NMQIANHTLK YGTQARKFDV NQLQNTTIKR IIKKVQDLER AALPAQELEE YNKILLDMET TYSVATVCHP NGSCLQLEPD LTNVMATSRK YEDLLWAWEG WRDKAGRAIL QFYPKYVELI NQAARLNGYV DAGDSWRSMY ETPSLEQDLE RLFQELQPLY LNLHAYVRRA LHRHYGAQHI NLEGPIPAHL LGNMWAQTWS NIYDLVVPFP SAPSMDTTEA MLKQGWTPRR MFKEADDFFT SLGLLPVPPE FWNKSMLEKP TDGREVVCHA SAWDFYNGKD FRIKQCTTVN LEDLVVAHHE MGHIQYFMQY KDLPVALREG ANPGFHEAIG DVLALSVSTP KHLHSLNLLS SEGGSDEHDI NFLMKMALDK IAFIPFSYLV DQWRWRVFDG SITKENYNQE WWSLRLKYQG LCPPVPRTQG DFDPGAKFHI PSSVPYIRYF VSFIIQFQFH EALCQAAGHT GPLHKCDIYQ SKEAGQRLAT AMKLGFSRPW PEAMQLITGQ PNMSASAMLS YFKPLLDWLR TENELHGEKL GWPQYNWTPN SARSEGPLPD SGRVSFLGLD LDAQQARVEH HHHHH

    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.

    Ace Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-Basic Human Recombinant

    Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

    Product # :

    CYT-218

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    Description

    Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.The FGF-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH7.4 and 1M NaCl.

    Purity

    Greater than 98.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.

    More Info

    • Introduction

      Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The HPR -binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

    • Background

      FGF 2 HUMAN: Insights into Fibroblast Growth Factor-2

      Basic Fibroblast Growth Factor or FGF 2 HUMAN is a protein with crucial roles in cell growth, tissue repair, and embryonic development. This is part of the larger fibroblast growth factor family and is vital for various biological processes, including the modulation of cell survival activities.

      Production and Properties

      Produced in E. coli, FGF 2 is a non-glycosylated polypeptide chain possessing 154 amino acids with a molecular weight of about 17.2 kDa. It is purified through advanced chromatographic techniques, ensuring high purity and activity for laboratory use.

      Physical Characteristics and Preparation

      The physical form of FGF 2 HUMAN is a sterile, white lyophilized powder. For experimental use, it is reconstituted with sterile water to at least 100µg/ml. This reconstitution is crucial for maintaining the integrity and effectiveness of the protein in various research applications.

      Storage and Handling

      To maintain stability, lyophilized FGF 2 should be stored at -18°C and used within three weeks if kept at room temperature. Once reconstituted, it should be kept at 4°C and used within 2-7 days or stored at -18°C for longer-term storage.

      Proper handling and avoiding repeated freeze-thaw cycles are essential to preserve the protein's functionality.

      Purity and Biological Activity

      FGF 2 is characterized by a purity greater than 98%, verified by SDS-PAGE analysis. Its biological activity is primarily defined by its efficacy in promoting the proliferation of specific cell lines, with an effective dose (ED50) typically below 0.1 ng/ml.

      Research Applications and Impact

      In the research context, FGF 2 is used extensively to study its effects on cell migration, proliferation, and angiogenesis. Moreover, its role in disease models, particularly in cancer and tissue repair studies, makes it a valuable resource for developing new therapeutic approaches.

      Usage Guidelines

      FGF 2 HUMAN is strictly for laboratory research use and is not suitable for drug development, food production, or cosmetic applications. Researchers are advised to comply with safety and handling guidelines to ensure that experiments are conducted under optimal conditions.

      The Broad Impact on Development and Disease

      FGF-2 is known for its multifunctional role across numerous biological processes such as tissue repair, embryonic development, angiogenesis, and even tumorigenesis.

      This growth factor, existing in various synonymous forms such as Basic FGF, FGF-b, and HBGF-2, is essential in cellular processes that underpin both health and disease.

      Furthermore, FGF-2's ability to bind to cellular receptors triggers a cascade of signaling pathways, including PI3K/Akt, MAPK/ERK, and PLCγ, which in turn influence cell growth, migration, and survival.

      These pathways are pivotal in mediating the factor's diverse effects on cell behavior, contributing to its critical roles in wound healing, angiogenesis, and tissue remodeling.

      What is the molecular weight/Mw of FGF 2 Protein?
      FGF 2 Protein has a total Mw of 17.2kDa.

      What is the source or expression system of FGF 2 Protein?
      Escherichia Coli.

      What is the Purity of FGF 2 Protein?
      FGF 2 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 2 Protein?
      The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.

      What is the amino acid sequence of FGF 2 Protein?
      AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

      What applications can FGF 2 Protein be used in?
      FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 2 Protein?
      The endotoxin level is minimal, FGF 2 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.

    Fgf 2 Human
  • View Data Sheet

    Name :

    GDNF Rat

    Description:

    Glial-Derived Neurotrophic Factor Rat Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-403

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    Description

    Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.

    Biological Activity

    Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

    • Background

      What is the molecular weight/Mw of GDNF RAT Protein?
      GDNF RAT Protein has a total Mw of 29.8kDa.

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

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

      What is the Biological Activity of GDNF RAT Protein?
      Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

      What is the amino acid sequence of GDNF RAT Protein?
      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

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

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

    Gdnf Rat
  • View Data Sheet

    Description:

    Ubiquilin 2 Human Recombinant

    UBQLN2, Ubiquilin 2, CHAP1, PLIC2, Protein Linking IAP With Cytoskeleton 2, Ubiquitin-Like Product Chap1/Dsk2, ALS15, N4BP4, NEDD4 Binding Protein 4, Nedd4 Binding Protein 4, DSK2 Homolog, Ubiquilin-2, HRIHFB2157, HPLIC-2, PLIC-2, DSK2.

    Product # :

    PRO-2228

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    Description

    UBQLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 647 amino acids (1-624 a.a) and having a molecular mass of 68.1kDa. UBQLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBQLN2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquilin-2, also known as UBQLN2 contains an N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. UBQLN2 is physically linked with proteasomes as well as ubiquitin ligases, and therefore is considered to functionally connect the ubiquitination machinery to the proteasome in order to affect in vivo protein degradation. Furthermore, UBQLN2 binds the ATPase domain of the Hsp70-like Stch protein. Among the diseases which are associated with UBQLN2: Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia as well as Amyotrophic lateral sclerosis type 15.

    • Synonyms

      UBQLN2, Ubiquilin 2, CHAP1, PLIC2, Protein Linking IAP With Cytoskeleton 2, Ubiquitin-Like Product Chap1/Dsk2, ALS15, N4BP4, NEDD4 Binding Protein 4, Nedd4 Binding Protein 4, DSK2 Homolog, Ubiquilin-2, HRIHFB2157, HPLIC-2, PLIC-2, DSK2.

    • 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 MGSMAENGES SGPPRPSRGP AAAQGSAAAP AEPKIIKVTV KTPKEKEEFA VPENSSVQQF KEAISKRFKS QTDQLVLIFA GKILKDQDTL IQHGIHDGLT VHLVIKSQNR PQGQSTQPSN AAGTNTTSAS TPRSNSTPIS TNSNPFGLGS LGGLAGLSSL GLSSTNFSEL QSQMQQQLMA SPEMMIQIME NPFVQSMLSN PDLMRQLIMA NPQMQQLIQR NPEISHLLNN PDIMRQTLEI ARNPAMMQEM MRNQDLALSN LESIPGGYNA LRRMYTDIQE PMLNAAQEQF GGNPFASVGS SSSSGEGTQP SRTENRDPLP NPWAPPPATQ SSATTSTTTS TGSGSGNSSS NATGNTVAAA NYVASIFSTP GMQSLLQQIT ENPQLIQNML SAPYMRSMMQ SLSQNPDLAA QMMLNSPLFT ANPQLQEQMR PQLPAFLQQM QNPDTLSAMS NPRAMQALMQ IQQGLQTLAT EAPGLIPSFT PGVGVGVLGT AIGPVGPVTP IGPIGPIVPF TPIGPIGPIG PTGPAAPPGS TGSGGPTGPT VSSAAPSETT SPTSESGPNQ QFIQQMVQAL AGANAPQLPN PEVRFQQQLE QLNAMGFLNR EANLQALIAT GGDINAAIER LLGSQPS.

    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.

    Ubqln2 Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor 16 Human Recombinant

    Fibroblast Growth Factor 16, Metacarpal 4-5 Fusion, FGF-16, MF4, FGF16.

    Product # :

    CYT-939

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    Description

    FGF16 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 206 amino acids and having a molecular mass of 23.6kDa.The FGF-16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-16 0.2µm filtered solution containing 20mM Tris-HCl, 1M NaCl, pH 9.0, 0.2% Tween-20 and 10% Glycerol.

    Purity

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

    Biological Activity

    The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.

    More Info

    • Introduction

      Fibroblast growth factor 16 (FGF16) is a member of the large FGF family, whose members are heparin-binding growth factors with a core 120 amino acid (a.a.) FGF domain which allows for a common tertiary structure. Human FGF16 cDNA is a 207 aa precursor protein with one N-linked glycosylation site. FGF16 though lacking a typical signal peptide, is efficiently produced by mechanisms other than the classical protein secretion pathway. FGF16 is expressed in cardiac cells and is required for proper heart development. FGF16 gene mutation was also observed in individuals with metacarpal 4-5 fusion. FGF16 has an imperative role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development.

    • Synonyms

      Fibroblast Growth Factor 16, Metacarpal 4-5 Fusion, FGF-16, MF4, FGF16.

    • 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

      AEVGGVFASL DWDLHGFSSS LGNVPLADSP GFLNERLGQI EGKLQRGSPT DFAHLKGILR RRQLYCRTGF HLEIFPNGTV HGTRHDHSRF GILEFISLAV GLISIRGVDS GLYLGMNERG ELYGSKKLTR ECVFREQFEE NWYNTYASTL YKHSDSERQY YVALNKDGSP REGYRTKRHQ KFTHFLPRPV DPSKLPSMSR DLFHYR.

    • Background

      What is the molecular weight/Mw of FGF16 Protein?
      FGF16 Protein has a total Mw of 23.6kDa.

      What is the source or expression system of FGF16 Protein?
      Escherichia Coli.

      What is the Purity of FGF16 Protein?
      FGF16 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF16 Protein?
      The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.

      What is the amino acid sequence of FGF16 Protein?
      AEVGGVFASL DWDLHGFSSS LGNVPLADSP GFLNERLGQI EGKLQRGSPT DFAHLKGILR RRQLYCRTGF HLEIFPNGTV HGTRHDHSRF GILEFISLAV GLISIRGVDS GLYLGMNERG ELYGSKKLTR ECVFREQFEE NWYNTYASTL YKHSDSERQY YVALNKDGSP REGYRTKRHQ KFTHFLPRPV DPSKLPSMSR DLFHYR.

      What applications can FGF16 Protein be used in?
      FGF16 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF16 Protein?
      The endotoxin level is minimal, FGF16 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.

    Fgf16 Human
  • View Data Sheet

    Description:

    S100 Calcium Binding Protein A11 Human Recombinant

    Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.

    Product # :

    PRO-385

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    Description

    S100A11 Human Recombinant is expressed in E. coli having a molecular weight of 17kDa fused to an amino terminal hexahistidine tag.

    Source

    Escherichia Coli.

    Formulation

    S100A11 is supplied in PBS and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    2 bands on Western blot at 17 and 34 kDa, respectively representing monomeric and dimeric form.

    More Info

    • Introduction

      S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.

    • Synonyms

      Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      S100A11 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    S100A11 Human
  • View Data Sheet

    Description:

    Lymphocyte Antigen 6 Complex Locus G6F Human Recombinant

    Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.

    Product # :

    PRO-1782

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    Description

    LY6G6F Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (17-235) and having a molecular mass of 26.2kDa.LY6G6F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LY6G6F solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The human Lymphocyte Antigen 6 Complex Locus G6F (LY6G6F) protein is a type I transmembrane protein belonging to the immunoglobin (Ig) superfamily, which contains cell-surface proteins involved in the immune system and cellular recognition. The LY6G6F protein has a role in the downstream signal transduction pathways involving GRB2 and GRB7.

    • Synonyms

      Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.

    • 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 MGSADNMQAI YVALGEAVEL PCPSPPTLHG DEHLSWFCSP AAGSFTTLVA QVQVGRPAPD PGKPGRESRL RLLGNYSLWL EGSKEEDAGR YWCAVLGQHH NYQNWRVYDV LVLKGSQLSA RAADGSPCNV LLCSVVPSRR MDSVTWQEGK GPVRGRVQSF WGSEAALLLV CPGEGLSEPR SRRPRIIRCL MTHNKGVSFS LAASIDASPA LCAPSTGWDM PW

    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.

    Ly6G6F Human
  • View Data Sheet

    Name :

    C9 Human

    Description:

    Complement C9 Human

    Product # :

    PRO-2696

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    Description

    Human Complement C9 produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 71kDa.

    Source

    Human Plasma.

    Formulation

    C9 protein 1mg/ml solution contains PBS pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C9 binds to the C5b-8 complex and formson cell membranes the mature membrane attack complex. Each pathway of complement activation generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing the anaphylatoxin C5a and activating C5b. This is the only proteolytic step in the assembly of the C5b-9 complex. Although C5b is unstable it remains bound to the activating complex for a few minutes during which it binds a single C6 from the surrounding fluid or it decays and is no longer capable of forming MAC.The C5b,6 complex may also remain connected to the C3/C5 convertase where the binding of a single C7 exposes a membrane-binding region and C5b,6,7 can enter into the bilipid layer of the target cell. Each C5b-7 complex can bind 1 molecule of C8 causing the complex to enter more firmly into the membrane. The C5b-8 complex can cause lysis without C9,though it will take longer andwill require many more complexes per cell than with C9. The main role of C8 is to catalyze the binding of C9 and each can bind another C9 initiating formation of a ring structure containing up to 18 C9molecules.C5b-9 complexes with 1 or more C9 are called the Membrane Attack Complex of complement.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C9 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

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

    C9 Protein
  • View Data Sheet

    Description:

    Insulin Like Growth Factor-1, Mutant E3R Human Recombinant

    Insulin-Like Growth Factor-1.

    Product # :

    CYT-1217

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Insulin-Like Growth Factor-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

    • Background

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

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

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

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

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

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

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

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

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

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

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

      What is the endotoxin level for IGF1 E3R HUMAN Protein?
      The endotoxin level is minimal, IGF1 E3R HUMAN Protein was purified using conventional chromatography techniques.


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

    Igf1 Mutant
  • View Data Sheet

    Description:

    Embryonic Ectoderm Development Human Recombinant

    Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.

    Product # :

    PRO-1503

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    Description

    EED Human Recombinant produced in E. coli is a single polypeptide chain containing 464 amino acids (1-441) and having a molecular mass of 52.6kDa. EED is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EED solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      EED is a part of the Polycomb-group family whose members form multimeric protein complexe that are involved in preserving the transcriptional repressive state of genes over successive cell generations. EED mediates repression of gene activity through histone deacetylation, and acts as a specific regulator of integrin function. EED protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin ?7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins.

    • Synonyms

      Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.

    • 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 MGSMSEREVS TAPAGTDMPA AKKQKLSSDE NSNPDLSGDE NDDAVSIESG TNTERPDTPT NTPNAPGRKS WGKGKWKSKK CKYSFKCVNS LKEDHNQPLF GVQFNWHSKE GDPLVFATVG SNRVTLYECH SQGEIRLLQS YVDADADENF YTCAWTYDSN TSHPLLAVAG SRGIIRIINP ITMQCIKHYV GHGNAINELK FHPRDPNLLL SVSKDHALRL WNIQTDTLVA IFGGVEGHRD EVLSADYDLL GEKIMSCGMD HSLKLWRINS KRMMNAIKES YDYNPNKTNR PFISQKIHFP DFSTRDIHRN YVDCVRWLGD LILSKSCENA IVCWKPGKME DDIDKIKPSE SNVTILGRFD YSQCDIWYMR FSMDFWQKML ALGNQVGKLY VWDLEVEDPH KAKCTTLTHH KCGAAIRQTS FSRDSSILIA VCDDASIWRW DRLR.

    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.

    Eed Human