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Search results

1000 results found for “gliadin”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    OCM Human

    Description:

    Oncomodulin-1 Human Recombinant

    Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    Product # :

    PRO-143

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    • More Info

    Description

    The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.

    • Synonyms

      Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.

    • Applications

      Western blotting.

    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.

    Ocm Human
  • View Data Sheet

    Name :

    STMN3 Human

    Description:

    Stathmin Like-3 Human Recombinant

    Stathmin-3, SCG10-like protein, STMN3, SCLIP

    Product # :

    PRO-838

    Price :

    Quantity :

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    • More Info

    Description

    STMN3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (39-180 a.a.) and having a molecular mass of 18.9 kDa. The STMN3 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STMN3 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STMN3 is a neuronal specific protein which belongs to the stathmin/oncoprotein 18 family of microtubule-destabilizing phosphoproteins. It is similar to the SCG10 protein and is involved in signal transduction and regulation of microtubule dynamics.

    • Synonyms

      Stathmin-3, SCG10-like protein, STMN3, SCLIP

    • 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 MDMEVKQLDK RASGQSFEVI LKSPSDLSPE SPMLSSPPKK KDTSLEELQK RLEAAEERRK TQEAQVLKQL AERREHEREV LHKALEENNN FSRQAEEKLN YKMELSKEIR EAHLAALRER LREKELHAAE VRRNKEQREE MSG.

    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.

    Stmn3 Human
  • View Data Sheet

    Name :

    C1GALT1 Human

    Description:

    Core 1 Beta3-Gal-T1 Human Recombinant

    Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.

    Product # :

    ENZ-721

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    • More Info

    Description

    C1GALT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (30-363 a.a) and having a molecular mass of 41.4kDa.C1GALT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    C1GALT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.

    • Synonyms

      Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 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 MGSLLGEKVD TQPNVLHNDP HARHSDDNGQ NHLEGQMNFN ADSSQHKDEN TDIAENLYQK VRILCWVMTG PQNLEKKAKH VKATWAQRCN KVLFMSSEEN KDFPAVGLKT KEGRDQLYWK TIKAFQYVHE HYLEDADWFL KADDDTYVIL DNLRWLLSKY DPEEPIYFGR RFKPYVKQGY MSGGAGYVLS KEALKRFVDA FKTDKCTHSS SIEDLALGRC MEIMNVEAGD SRDTIGKETF HPFVPEHHLI KGYLPRTFWY WNYNYYPPVE GPGCCSDLAV SFHYVDSTTM YELEYLVYHL RPYGYLYRYQ PTLPERILKE ISQANKNEDT KVKLGNP.

    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.

    C1Galt1 Human
  • View Data Sheet

    Name :

    Periostin Human, HEK

    Description:

    Periostin Human Recombinant, HEK

    OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    Product # :

    CYT-835

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.

    Purity

    Greater than 38.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
      Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.

    • Synonyms

      OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH H.

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

    Periostin Human Hek
  • View Data Sheet

    Name :

    PFN2 Human

    Description:

    Profilin-2 Human Recombinant

    Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    Product # :

    PRO-809

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    Description

    PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.

    • Synonyms

      Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    • 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 MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.

    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.

    Pfn2 Human
  • View Data Sheet

    Name :

    Follistatin Human, Sf9

    Description:

    Follistatin Human Recombinant, Sf9

    Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.

    Product # :

    CYT-865

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    • sds-page

    Description

    FST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (30-317a.a.) and having a molecular mass of 32.5kDa.FST is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    FST protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    Follistatin Human, Sf9-sds-page - Product image 1

    More Info

    • Introduction

      Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.

    • 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

      MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN, SF9 Protein?
      FOLLISTATIN HUMAN, SF9 Protein has a total Mw of 32.5kDa.

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

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

      What is the amino acid sequence of FOLLISTATIN HUMAN, SF9 Protein?
      MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH.

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

      What is the endotoxin level for FOLLISTATIN HUMAN, SF9 Protein?
      The endotoxin level is minimal, FOLLISTATIN 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.

    Fst Human Sf9
  • View Data Sheet

    Name :

    G CSF Human, His

    Description:

    Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-476

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    Description

    Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment (31-204) and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.G-CSF-His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Granulocyte Colony Stimulating Factor His is supplied in 1x PBS and 50% glycerol.

    Purity

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

    More Info

    • Introduction

      Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Background

      What is the molecular weight/Mw of G CSF Protein?
      G CSF Protein has a total Mw of 23.19kDa.

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

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

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

      What is the amino acid sequence of G CSF Protein?
      G CSF Protein is composed from 174 amino acids.

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

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

    G Csf Human His
  • View Data Sheet

    Name :

    KLK10 Human, Sf9

    Description:

    Kallikrein-10 Human Recombinant, Sf9

    Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    Product # :

    ENZ-1090

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    Description

    KLK10 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 252 amino acids (34-276 a.a) and having a molecular mass of 27.8kDa. KLK10 protein is fused to a 6 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK10 protein solution (0.5mg/ml) contains 30% glycerol, 20mM Tris-HCl (pH 8.0), 0.15M NaCl & 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.

    • Synonyms

      Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    • 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

      ADPALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSNHHHH 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.

    Kallikrein 10
  • View Data Sheet

    Name :

    PPIL2 Human

    Description:

    Cyclophilin-60 Human Recombinant

    CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.

    Product # :

    ENZ-497

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    Description

    PPIL2 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 547 amino acids (1-527 a.a.) and having a molecular mass of 61.6 kDa. The PPIL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPIL2 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 290 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

      PPIL2 is part of the cyclophilin family of peptidylprolyl isomerases which are highly conserved ubiquitous proteins that play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL2 interacts with the proteinase inhibitor eglin c and is localized in the nucleus. PPIL2 increases folding of proteins andcatalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

    • Synonyms

      CYC4, Cyp-60, CYP60, hCyP-60, Peptidyl-prolyl cis-trans isomerase-like 2, PPIase, Rotamase PPIL2, Cyclophilin-60, Cyclophilin-like protein Cyp-60, PPIL2, MGC787, FLJ39930, MGC33174.

    • 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 MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT NAETRETLQE YKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF TSTAMVPETT EAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH.

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    Ppil2 Human
  • View Data Sheet

    Name :

    LIF Human, GST

    Description:

    Leukemia Inhibitory Factor, GST tag Human Recombinant

    D factor, MLPLI, HILDA, Emfilermin, Leukemia Inhibitory factor, Differentiation-stimulating factor, Melanoma-derived LPL inhibitor.

    Product # :

    CYT-001

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    Description

    LIF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (23-202a.a.) and having a molecular mass of 47.2kDa.LIF is fused to a 236 amino acid His-GST tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIF GST protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leukemia inhibitory factor, is a pleiotropic cytokine which is expressed by numerous cells including activated T lymphocytes, monocytes, mast cells and neuronal cells. LIF takes part in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and is a key player in immune tolerance at the maternal-fetal interface.

    • Synonyms

      D factor, MLPLI, HILDA, Emfilermin, Leukemia Inhibitory factor, Differentiation-stimulating factor, Melanoma-derived LPL inhibitor.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MHHHHHHMSP ILGYWKIKGL VQPTRLLLEY LEEKYEEHLY ERDEGDKWRN KKFELGLEFP NLPYYIDGDV KLTQSMAIIR YIADKHNMLG GCPKERAEIS MLEGAVLDIR YGVSRIAYSK DFETLKVDFL SKLPEMLKMF EDRLCHKTYL NGDHVTHPDF MLYDALDVVL YMDPMCLDAF PKLVCFKKRI EAIPQIDKYL KSSKYIAWPL QGWQATFGGG DHPPKSDLVP RGSHMSPLPI TPVNATCAIR HPCHNNLMNQ IRSQLAQLNG SANALFILYY TAQGEPFPNN LDKLCGPNVT DFPPFHANGT EKAKLVELYR IVVYLGTSLG NITRDQKILN PSALSLHSKL NATADILRGL LSNVLCRLCS KYHVGHVDVT YGPDTSGKDV FQKKKLGCQL LGKYKQIIAV LAQAF

    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.

    Lif Human Gst
  • View Data Sheet

    Name :

    CHGB Human

    Description:

    Chromogranin B Human Recombinant

    SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    Product # :

    PRO-824

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    Description

    CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.

    • Synonyms

      SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    • 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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.

    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.

    Chgb Human
  • View Data Sheet

    Name :

    LYG2 Human

    Description:

    Lysozyme G-Like 2 Human Recombinant

    Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.

    Product # :

    PRO-1245

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    Description

    LYG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (20-212) and having a molecular mass of 23.9 kDa. LYG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The LYG2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      lysozyme G-like 2 and LYGH (LYG2), is a member of the glycosyl hydrolase 23 family. Lysozyme takes part in human innate immunity by causing bacterial cell lysis. LYG2 contains a SLT domain, a protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc).

    • Synonyms

      Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.

    • 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 MGSSYPFSHS MKPHLHPRLY HGCYGDIMTM KTSGATCDAN SVMNCGIRGS EMFAEMDLRA IKPYQTLIKE VGQRHCVDPA VIAAIISRES HGGSVLQDGW DHRGLKFGLM QLDKQTYHPV GAWDSKEHLS QATGILTERI KAIQKKFPTW SVAQHLKGGL SAFKSGIEAI ATPSDIDNDF VNDIIARAKF YKRQSF.

    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.

    Lyg2 Human
  • View Data Sheet

    Name :

    Resistin Human

    Description:

    Resistin Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-456

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    Description

    Resistin Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 93 amino acids and having a total molecular weight of 19.7kDa.The Resistin Human Recombinant protein is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.1% Trifluoroacetic Acis (TFA).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppresses the ability to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP

    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.

    Resistin Human
  • View Data Sheet

    Name :

    CRYM Human

    Description:

    Crystallin, Mu Human Recombinant

    Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    Product # :

    PRO-2291

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    Description

    CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CYRM 1mg/ml solution containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.

    • Synonyms

      Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CRYM although stable at 4°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK

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    Crym Human
  • View Data Sheet

    Name :

    MOG Human

    Description:

    Myelin Oligodendrocyte Glycoprotein Human Recombinant

    Myelin Oligodendrocyte Glycoprotein, MOG, MOGIG-2, MGC26137.

    Product # :

    PRO-466

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    Description

    Myelin Oligodendrocyte Glycoprotein produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 132 amino acids (Met + 30-154 a.a. + 6x His tag at C-terminus) and having a total molecular mass of 15.2 kDa.

    Source

    Escherichia Coli.

    Formulation

    The Myelin Oligodendrocyte Glycoprotein was lyophilized from a 0.2µm filtered solution in 20mM HAc-NaAc and 150mM NaCl pH-4.5

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myelin Oligodendrocyte Glycoprotein is a membrane protein expressed on the oligodendrocyte cell surface and the outermost surface of myelin sheaths. Due to this localization, it is a prime target antigen that plays a role in immune-mediated demyelination. Myelin Oligodendrocyte Glycoprotein is involved in completion and maintenance of the myelin sheath and in cell-cell communication. MOG protein was found to differentially expressed in the dorsolateral prefrontal cortex and in the temporal lobe from patients with schizophrenia. MOG-specific antibody is crucial to the initiation of MOG-induced murine experimental autoimmune encephalomyelitis.

    • Synonyms

      Myelin Oligodendrocyte Glycoprotein, MOG, MOGIG-2, MGC26137.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MOG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MOG 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 MOG in sterile 50mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGQFRVIGPRHPIRALVGDEVELPCRISPGKNATGMEVGWYRPPFSRVVHLYRN
      GKDQDGDQAPEYRGRTELLKDAIGEGKVTLRIRNVRFSDEGGFTCFFRDHSYQE
      EAAMELKVEDPFYWVSPGHHHHHH.

    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.

    Mog Human
  • View Data Sheet

    Name :

    SDC1 Human

    Description:

    Syndecan-1 Human Recombinant

    Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.

    Product # :

    PRO-1065

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    Description

    SDC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (18-254) and having a molecular mass of 27kDa (molecular size on SDS-PAGE will appear higher).SDC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SDC1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD138 takes a part in cell adhesion. CD138 is expressed on the surface of pre-B cells and plasma cells but is absent from mature B cells. SDC1 is a selective marker for B cell lymphoblastic leukemia and lymphoplasmacytoid leukemia. SDC1 is missing from the apoptotic myeloma cells; therefore is a valuable marker for plasma cell and myeloma cells.

    • Synonyms

      Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.

    • 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 MGSHMQPALP QIVATNLPPE DQDGSGDDSD NFSGSGAGAL QDITLSQQTP STWKDTQLLT AIPTSPEPTG LEATAASTST LPAGEGPKEG EAVVLPEVEP GLTAREQEAT PRPRETTQLP TTHQASTTTA TTAQEPATSH PHRDMQPGHH ETSTPAGPSQ ADLHTPHTED GGPSATERAA EDGASSQLPA AEGSGEQDFT FETSGENTAV VAVEPDRRNQ SPVDQGATGA SQGLLDRKEV LG.

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    Sdc1 Human
  • View Data Sheet

    Name :

    DEFB118 Human

    Description:

    Beta Defensin 118 Human Recombinant

    Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    Product # :

    CYT-714

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    • sds-page

    Description

    DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    DEFB118-sds-page - Product image 1

    More Info

    • Introduction

      Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.

    • Synonyms

      Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    • 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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

    • Background

      Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications

      Abstract:


      Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. 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 BD118.

      Role in Innate Immunity:


      BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.

      Therapeutic Implications:


      Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.

      Conclusion:


      Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.

      What is the molecular weight/Mw of DEFB118 Protein?
      DEFB118 Protein has a total Mw of 13.8kDa.

      What is the source or expression system of DEFB118 Protein?
      Escherichia Coli.

      What is the Purity of DEFB118 Protein?
      DEFB118 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB118 Protein?
      The biological functionality of DEFB118 Protein will be determined in the future.

      What is the amino acid sequence of DEFB118 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

      What applications can DEFB118 Protein be used in?
      DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB118 Protein?
      The endotoxin level is minimal, DEFB118 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.

    Defb118 Human
  • View Data Sheet

    Name :

    SERPING1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1401

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    Description

    SERPING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 499 amino acids (23-500a.a) and having a molecular mass of 55.1kDa. SERPING1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SERPING1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • 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 MNPNATSSSS QDPESLQDRG EGKVATTVIS KMLFVEPILE VSSLPTTNST TNSATKITAN TTDEPTTQPT TEPTTQPTIQ PTQPTTQLPT DSPTQPTTGS FCPGPVTLCS DLESHSTEAV LGDALVDFSL KLYHAFSAMK KVETNMAFSP FSIASLLTQV LLGAGENTKT NLESILSYPK DFTCVHQALK GFTTKGVTSV SQIFHSPDLA IRDTFVNASR TLYSSSPRVL SNNSDANLEL INTWVAKNTN NKISRLLDSL PSDTRLVLLN AIYLSAKWKT TFDPKKTRME PFHFKNSVIK VPMMNSKKYP VAHFIDQTLK AKVGQLQLSH NLSLVILVPQ NLKHRLEDME QALSPSVFKA IMEKLEMSKF QPTLLTLPRI KVTTSQDMLS IMEKLEFFDF SYDLNLCGLT EDPDLQVSAM QHQTVLELTE TGVEAAAASA ISVARTLLVF EVQQPFLFVL WDQQHKFPVF MGRVYDPRA.

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    Serping1 Human
  • View Data Sheet

    Name :

    SH3BGRL3 Human

    Description:

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 3 Human Recombinant

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.

    Product # :

    PRO-1216

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    Description

    SH3BGRL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 116 amino acids (1-93) and having a molecular mass of 12.8 kDa.SH3BGRL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SH3BGRL3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SH3 domain-binding glutamic acid-rich-like protein 3 (SH3BGRL3) which is located on chromosome 1p34.3-35, encodes for a small 93 amino acids protein. SH3BGRL3 is the newest member of thioredoxin super family, whose posttranslational altered form was recognized as TNF-alpha inhibitory protein. SH3BGRL3 may act as a regulator in all-trans retinoic acid-induced pathway and also as a modulator of glutaredoxin biological activity.

    • Synonyms

      SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.

    • 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 MGSMSGLRVY STSVTGSREI KSQQSEVTRI LDGKRIQYQL VDISQDNALR DEMRALAGNP KATPPQIVNG DQYCGDYELF VEAVEQNTLQ EFLKLA

    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.

    Sh3Bgrl3 Human
  • View Data Sheet

    Name :

    EED Human

    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.

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    Eed Human
  • View Data Sheet

    Name :

    AZGP1

    Description:

    Alpha-2-Glycoprotein 1 Zinc-Binding Human Recombinant

    Zinc-alpha-2-glycoprotein, ZA2G, ZAG, Zn-alpha-2-GP, Zn-alpha-2-glycoprotein.

    Product # :

    PRO-2169

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    Description

    AZGP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (21-298 a.a) and having a molecular mass of 34.5kDa.AZGP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AZGP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Zinc-alpha-2-glycoprotein (AZGP1) protein stimulates lipid degradation in adipocytes and causes the massive fat losses linked with various advanced cancers. AZGP1 may bind polyunsaturated fatty acids.

    • Synonyms

      Zinc-alpha-2-glycoprotein, ZA2G, ZAG, Zn-alpha-2-GP, Zn-alpha-2-glycoprotein.

    • 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 MGSQENQDGR YSLTYIYTGL SKHVEDVPAF QALGSLNDLQ FFRYNSKDRK SQPMGLWRQV EGMEDWKQDS QLQKAREDIF METLKDIVEY YNDSNGSHVL QGRFGCEIEN NRSSGAFWKY YYDGKDYIEF NKEIPAWVPF DPAAQITKQK WEAEPVYVQR AKAYLEEECP ATLRKYLKYS KNILDRQDPP SVVVTSHQAP GEKKKLKCLA YDFYPGKIDV HWTRAGEVQE PELRGDVLHN GNGTYQSWVV VAVPPQDTAP YSCHVQHSSL AQPLVVPWEA S.

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    Azgp1 Human
  • View Data Sheet

    Name :

    BGN Human

    Description:

    Biglycan Human Recombinant

    DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.

    Product # :

    PRO-1382

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    • More Info

    Description

    BGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (38-368a.a) and having a molecular mass of 39.5kDa. BGN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

    • Synonyms

      DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.

    • 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 MDEEASGADT SGVLDPDSVT PTYSAMCPFG CHCHLRVVQC SDLGLKSVPK EISPDTTLLD LQNNDISELR KDDFKGLQHL YALVLVNNKI SKIHEKAFSP LRKLQKLYIS KNHLVEIPPN LPSSLVELRI HDNRIRKVPK GVFSGLRNMN CIEMGGNPLE NSGFEPGAFD GLKLNYLRIS EAKLTGIPKD LPETLNELHL DHNKIQAIEL EDLLRYSKLY RLGLGHNQIR MIENGSLSFL PTLRELHLDN NKLARVPSGL PDLKLLQVVY LHSNNITKVG VNDFCPMGFG VKRAYYNGIS LFNNPVPYWE VQPATFRCVT DRLAIQFGNY KK.

    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.

    Bgn Human
  • View Data Sheet

    Name :

    STARD5 Human

    Description:

    StAR-Related Lipid Transfer Domain Containing 5 Human Recombinant

    StAR-Related Lipid Transfer (START) Domain Containing 5, START Domain-Containing Protein 5, StARD5.

    Product # :

    PRO-1775

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    STARD5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 236 amino acids (1-213 a.a) and having a molecular mass of 26.2kDa. STARD5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STARD5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STARD5 is a member of the STARD family of proteins. This family of proteins has 15 different members, all of which hold the distinctive START domain and have a vital part in the metabolism and transport of lipids. The STARD family of proteins has six subfamilies based on their START domain sequences. STARD5 constitute one subfamily, sharing approximately 30% amino acid identity with each other. Even though STARD5 is not sterol-regulated it is induced by endomplasmic reticulum (ER) stress.

    • Synonyms

      StAR-Related Lipid Transfer (START) Domain Containing 5, START Domain-Containing Protein 5, StARD5.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDPALAA QMSEAVAEKM LQYRRDTAGW KICREGNGVS VSWRPSVEFP GNLYRGEGIV YGTLEEVWDC VKPAVGGLRV KWDENVTGFE IIQSITDTLC VSRTSTPSAA MKLISPRDFV DLVLVKRYED GTISSNATHV EHPLCPPKPG FVRGFNHPCG CFCEPLPGEP TKTNLVTFFH TDLSGYLPQN VVDSFFPRSM TRFYANLQKA VKQFHE

    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.

    Stard5 Human
  • View Data Sheet

    Name :

    STMN1 Human

    Description:

    Stathmin-1 Human Recombinant

    Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.

    Product # :

    PRO-676

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    Description

    Recombinant Human Stathmin-1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149 a.a) and having a molecular mass of 19.4 kDa. STMN1 is fused to 20 amino acid His Tga at N-Terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The STMN1 protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STMN1 takes part in the regulation of the microtubule filament structure by destabilizing microtubules. STMN1 promotes the disassembly of microtubules and prevents assembly. STMN1 is a ubiquitous cytosolic phosphoprotein which functions as an intracellular relay integrating regulatory signals of the cellular environment. Stathmin functions as an Oncoprotein in regulation of the cell cycle. Stathmin mutation results in uncontrolled cell proliferation. Stathmin expression associates with cervical carcinogenesis and tumor progression, thus Stathmin is an important prognostic marker in cervical carcinoma. STMN1, takes part in the prevenative progression of ER-positive primary in breast cancer. Somatic mutation in STMN1 effects cell homeostasis that leads to tumorigenicity.

    • Synonyms

      Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.

    • 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 MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL ERLREKDKHI EEVRKNKESK DPADETEAD.

    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.

    Stmn1 Human
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