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Search results

1000 results found for “serum amyloid a”

Name

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  • View Data Sheet

    Name :

    Cyclophilin A E.Coli

    Description:

    Cyclophilin A E.Coli Recombinant

    Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, CypA, rot, rotA.

    Product # :

    ENZ-859

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    Description

    Cyclophilin A E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (25-190a.a.) and having a molecular mass of 20.5kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    Cyclophilin A protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, CypA, rot, rotA.

    • 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 MGSAKGDPHV LLTTSAGNIE LELDKQKAPV SVQNFVDYVN SGFYNNTTFH RVIPGFMIQG GGFTEQMQQK KPNPPIKNEA DNGLRNTRGT IAMARTADKD SATSQFFINV ADNAFLDHGQ RDFGYAVFGK VVKGMDVADK ISQVPTHDVG PYQNVPSKPV VILSAKVLP.

    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.

    Cyclophilin A Ecoli
  • View Data Sheet

    Name :

    Adiponectin Human, Sf9

    Description:

    Adiponectin Human Recombinant, Sf9

    Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    Product # :

    CYT-1002

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    • sds-page
    • Citations

    Description

    Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Acrp30 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    Adiponectin-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
      Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
      The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
      Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

    • Synonyms

      Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    • 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

      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.9kDa.

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

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

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

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

    Acrp30 Human Sf9
  • View Data Sheet

    Name :

    NAA30 Human

    Description:

    N Alpha-Acetyltransferase 30, NatC Catalytic Subunit Human Recombinant

    N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.

    Product # :

    ENZ-720

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    Description

    NAA30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362 a.a) and having a molecular mass of 41.7kDa.NAA30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAA30 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      N-alpha-acetyltransferase 30 (NAA30) is catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. NAA30 catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. In addition, NAA30 is essential for the lysosomal localization and function of ARL8B. The disease Eastern equine encephalitis has been associated with NAA30.

    • Synonyms

      N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.

    • 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 MGSMAEVPPG PSSLLPPPAP PAPAAVEPRC PFPAGAALAC CSEDEEDDEE HEGGGSRSPA GGESATVAAK GHPCLRCPQP PQEQQQLNGL ISPELRHLRA AASLKSKVLS VAEVAATTAT PDGGPRATAT KGAGVHSGER PPHSLSSNAR TAVPSPVEAA AASDPAAARN GLAEGTEQEE EEEDEQVRLL SSSLTADCSL RSPSGREVEP GEDRTIRYVR YESELQMPDI MRLITKDLSE PYSIYTYRYF IHNWPQLCFL AMVGEECVGA IVCKLDMHKK MFRRGYIAML AVDSKYRRNG IGTNLVKKAI YAMVEGDCDE VVLETEITNK SALKLYENLG FVRDKRLFRY YLNGVDALRL KLWLR

    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.

    Naa30 Human
  • View Data Sheet

    Name :

    ANKRA2 Human

    Description:

    Ankyrin Repeat Family A2 Human Recombinant

    Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.

    Product # :

    PRO-2062

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    Description

    ANKRA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313a.a) and having a molecular mass of 36.7kDa. ANKRA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANKRA2 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ankyrin Repeat Family A2, also known as ANKRA2 contains 5 ANK repeats. ANKRA2 assist endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.

    • Synonyms

      Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.

    • 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 MGSMDTSTNL DIGAQLIVEE CPSTYSLTGM PDIKIEHPLD PNSEEGSAQG VAMGMKFILP NRFDMNVCSR FVKSLNEEDS KNIQDQVNSD LEVASVLFKA ECNIHTSPSP GIQVRHVYTP STTKHFSPIK QSTTLTNKHR GNEVSTTPLL ANSLSVHQLA AQGEMLYLAT RIEQENVINH TDEEGFTPLM WAAAHGQIAV VEFLLQNGAD PQLLGKGRES ALSLACSKGY TDIVKMLLDC GVDVNEYDWN GGTPLLYAVH GNHVKCVKML LESGADPTIE TDSGYNSMDL AVALGYRSVQ QVIESHLLKL LQNIKE.

    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.

    Ankra2 Human
  • View Data Sheet

    Name :

    SIT1 Human

    Description:

    Signaling Threshold Regulating Transmembrane Adaptor 1 Human Recombinant

    Signaling threshold-regulating transmembrane adapter 1, SHP2-interacting transmembrane adapter protein, Suppression-inducing transmembrane adapter 1, gp30/40, SIT1, SIT, RP11-331F9.5, MGC125908, MGC125909, MGC125910.

    Product # :

    PRO-928

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    Description

    SIT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (62-196 a.a.) and having a molecular mass of 16.9kDa (Molecular weight on SDS-PAGE will appear higher).SIT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SIT1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Signaling threshold-regulating transmembrane adapter 1 (SIT1) negatively regulates T-cell antigen receptor (TCR)-mediated signaling in T-cells. SIT1 is involved in positive selection of T-cells. SIT1 is specifically expressed in T- and B-cells. SIT1 is also present in plasma cells but not in germinal center B-cells (at protein level). SIT1 is expressed in T- and B-cell lymphoma.

    • Synonyms

      Signaling threshold-regulating transmembrane adapter 1, SHP2-interacting transmembrane adapter protein, Suppression-inducing transmembrane adapter 1, gp30/40, SIT1, SIT, RP11-331F9.5, MGC125908, MGC125909, MGC125910.

    • 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 MHLSQWTRGR SRSHPGQGRS GESVEEVPLY GNLHYLQTGR LSQDPEPDQQ DPTLGGPARA AEEVMCYTSL QLRPPQGRIP GPGTPVKYSE VVLDSEPKSQ ASGPEPELYA SVCAQTRRAR ASFPDQAYAN SQPAAS.

    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.

    Sit1 Human
  • View Data Sheet

    Name :

    SOS1 Human

    Description:

    Son Of Sevenless Homolog 1 Human Recombinant

    SOS Ras/Rac Guanine Nucleotide Exchange Factor 1, Gingival Fibromatosis, Hereditary, 1, SOS-1, Son Of Sevenless Homolog 1 (Drosophila), Guanine Nucleotide Exchange Factor, Son Of Sevenless Homolog 1, GINGF, GGF1, GF1, HGF, NS4, Son of sevenless homolog 1.

    Product # :

    PRO-2507

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    Description

    SOS1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 495 amino acids (564-1049a.a.) and having a molecular mass of 58.0kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).SOS1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SOS1 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 7.5), 30% glycerol, 0.1M NaCl, 1mM DTT & 0.2mM MgCl2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SOS1, also known as Gingival Fibromatosis, is a Ras & Rac guanine nucleotide exchange factor. SOS1 is comprised of a number of significant domains. The REM and CDC25 domains provide the catalytic activity of SOS1 towards Ras and the histone fold DH/PH (Dbl homology & Pleckstrin homology) domains function, in tandem, to stimulate GTP/GDP exchange for Rac. Moreover, binding of GTP activates Ras proteins, and subsequent hydrolysis of the bound GTP to GDP and phosphate inactivates signaling by these proteins. GTP binding can be catalyzed by guanine nucleotide exchange factors for RAS, and GTP hydrolysis can be enhanced by GTPase-activating proteins.

    • Synonyms

      SOS Ras/Rac Guanine Nucleotide Exchange Factor 1, Gingival Fibromatosis, Hereditary, 1, SOS-1, Son Of Sevenless Homolog 1 (Drosophila), Guanine Nucleotide Exchange Factor, Son Of Sevenless Homolog 1, GINGF, GGF1, GF1, HGF, NS4, Son of sevenless homolog 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

      ADPEEQMRLP SADVYRFAEP DSEENIIFEE NMQPKAGIPI IKAGTVIKLI ERLTYHMYAD PNFVRTFLTT YRSFCKPQEL LSLIIERFEI PEPEPTEADR IAIENGDQPL SAELKRFRKE YIQPVQLRVL NVCRHWVEHH FYDFERDAYL LQRMEEFIGT VRGKAMKKWV ESITKIIQRK KIARDNGPGH NITFQSSPPT VEWHISRPGH IETFDLLTLH PIEIARQLTL LESDLYRAVQ PSELVGSVWT KEDKEINSPN LLKMIRHTTN LTLWFEKCIV ETENLEERVA VVSRIIEILQ VFQELNNFNG VLEVVSAMNS SPVYRLDHTF EQIPSRQKKI LEEAHELSED HYKKYLAKLR SINPPCVPFF GIYLTNILKT EEGNPEVLKR HGKELINFSK RRKVAEITGE IQQYQNQPYC LRVESDIKRF FENLNPMGNS MEKEFTDYLF NKSLEIEPRN PKPLPRFPKK YSYPLKSPGV RPSNPRPGTH 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.

    Sos1 Human
  • View Data Sheet

    Name :

    TPA (36-310) Human

    Description:

    Tissue Plasminogen Activator (36-310 a.a.) Human Recombinant

    Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA, Alteplase, Reteplase, Plasminogen Activator, Tissue, Plasminogen/Activator Kringle. 

    Product # :

    ENZ-1050

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    Description

    TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 284 amino acids (36-310a.a.) and having a molecular mass of 32.0kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).TPA is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TPA protein solution (0.25mg/ml) contains 50mM MES(pH5.5),10% glycerol, 100mM NaCl and 5mM CaCl2.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
      This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

    • Synonyms

      Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA, Alteplase, Reteplase, Plasminogen Activator, Tissue, Plasminogen/Activator Kringle.

    • 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

      ADPSYQVICR DEKTQMIYQQ HQSWLRPVLR SNRVEYCWCN SGRAQCHSVP VKSCSEPRCF NGGTCQQALY FSDFVCQCPE GFAGKCCEID TRATCYEDQG ISYRGTWSTA ESGAECTNWN SSALAQKPYS GRRPDAIRLG LGNHNYCRNP DRDSKPWCYV FKAGKYSSEF CSTPACSEGN SDCYFGNGSA YRGTHSLTES GASCLPWNSM ILIGKVYTAQ NPSAQALGLG KHNYCRNPDG DAKPWCHVLK NRRLTWEYCD VPSCSTCGLR QYSQPQFRHH HHHH.

    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.

    Tpa Protein
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

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    Description

    Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

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

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

    Leptin Ta Human
  • View Data Sheet

    Name :

    LIF Human, Sf9

    Description:

    Leukemia Inhibitory Factor Human Recombinant, Sf9

    Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

    Product # :

    CYT-1003

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    Description

    LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LIF 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

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.

    Citations

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

    • 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

      ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
      QAFHHHHHH.

    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 Sf9
  • View Data Sheet

    Name :

    YOD1 Human

    Description:

    YOD1 Human Recombinant

    DUBA8, OTUD2, PRO0907, RP11-164O23.1, Ubiquitin thioesterase OTU1, DUBA-8, HIN-7, HsHIN7, OTU domain-containing protein 2.

    Product # :

    ENZ-696

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    Description

    YOD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (1-348) and having a molecular mass of 40.7kDa.YOD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YOD1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      YOD1 is a Hydrolase which removes conjugated ubiquitin from proteins and takes part in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. YOD1 is a highly conserved deubiquitinating enzyme belonging to the ovarian tumor (otubain) family, whose function has yet to be determined in mammalian cells. YOD1 is a component of a multiprotein complex with p97 as its nucleus, proposing a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. YOD1 variant xpression deprived of its deubiquitinating activity compels a halt on the dislocation reaction, as concluded by the stabilization of various dislocation substrates.

    • Synonyms

      DUBA8, OTUD2, PRO0907, RP11-164O23.1, Ubiquitin thioesterase OTU1, DUBA-8, HIN-7, HsHIN7, OTU domain-containing protein 2.

    • 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 MGSMFGPAKG RHFGVHPAPG FPGGVSQQAA GTKAGPAGAW PVGSRTDTMW RLRCKAKDGT HVLQGLSSRT RVRELQGQIA AITGIAPGGQ RILVGYPPEC LDLSNGDTIL EDLPIQSGDM LIIEEDQTRP RSSPAFTKRG ASSYVRETLP VLTRTVVPAD NSCLFTSVYY VVEGGVLNPA CAPEMRRLIA QIVASDPDFY SEAILGKTNQ EYCDWIKRDD TWGGAIEISI LSKFYQCEIC VVDTQTVRID RFGEDAGYTK RVLLIYDGIH YDPLQRNFPD PDTPPLTIFS SNDDIVLVQA LELADEARRR RQFTDVNRFT LRCMVCQKGL TGQAEAREHA KETGHTNFGE V.

    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.

    Yod1 Human
  • View Data Sheet

    Name :

    YWHAE Human, His

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein, Epsilon Human Recombinant, His Tag

    YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.

    Product # :

    PKA-095

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    Description

    YWHAE Human Recombinant produced in E. coli is a single polypeptide chain containing 275 amino acids (1-255) and having a molecular mass of 31.3kDa. YWHAE is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YWHAE solution (1mg/1ml) contains phosphate buffered Saline (pH7.4), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 epsilon, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.

    • Synonyms

      YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.

    • 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 MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ.

    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.

    Ywhae Human His
  • View Data Sheet

    Name :

    STYX Human (26-223)

    Description:

    Serine/Threonine/Tyrosine Interacting Protein (26-223 a.a.) Human Recombinant

    Serine/threonine/tyrosine-interacting protein.

    Product # :

    ENZ-590

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    Description

    STYX Human Recombinant produced in E. coli is a single polypeptide chain containing 221 amino acids (26-223) and having a molecular mass of 25.0kDa.STYX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The STYX solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STYX is a member of the protein-tyrosine phosphatase family. STYX has a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. Nevertheless, the binding pocket is adequately preserved to bind phosphorylated substrates, and possibly protect them from phosphatases. STYX takes part in spermiogenesis.

    • Synonyms

      Serine/threonine/tyrosine-interacting protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH SHMRREMQEI LPGLFLGPYS SAMKSKLPVL QKHGITHIIC IRQNIEANFI KPNFQQLFRY LVLDIADNPV ENIIRFFPMT KEFIDGSLQM GGKVLVHGNA GISRSAAFVI AYIMETFGMK YRDAFAYVQE RRFCINPNAG FVHQLQEYEA IYLAKLTIQM MSPLQIERSL SVHSGTTGSL KRTHEEEDDF GTMQVATAQN G

    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.

    Styx Human 26 223
  • View Data Sheet

    Name :

    SYT1 Human

    Description:

    Synaptotagmin I Human Recombinant

    Synaptotagmin-1, Synaptotagmin I, SytI, p65, SYT1, SVP65, SYT.

    Product # :

    PRO-239

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    Description

    SYT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (136-382 a.a) and having a molecular mass of 29.5kDa.SYT1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SYT1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptotagmin-1(SYT1) is a member of the synaptotagmin family, which contains two C2 domains. The synaptotagmins are integral membrane proteins of synaptic vesicles assumed to function as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SYT1 is the principal regulator responsible for allowing the human brain to release neurotransmitters. SYT1 may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. SYT1 binds acidic phospholipids with a specificity which entails the presence of both an acidic head group and a diacyl backbone. SYT1 can also bind to at least 3 additional proteins in a Ca2+-independent manner; these being neurexins, syntaxin and AP2.

    • Synonyms

      Synaptotagmin-1, Synaptotagmin I, SytI, p65, SYT1, SVP65, SYT.

    • 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

      MEPKEEEKLG KLQYSLDYDF QNNQLLVGII QAAELPALDM GGTSDPYVKV FLLPDKKKKF ETKVHRKTLN PVFNEQFTFK VPYSELGGKT LVMAVYDFDR FSKHDIIGEF KVPMNTVDFG HVTEEWRDLQ SAEKEEQEKL GDICFSLRYV PTAGKLTVVI LEAKNLKKMD VGGLSDPYVK IHLMQNGKRL KKKKTTIKKN TLNPYYNESF SFEVPFEQIQ KVQVVVTVLD YDKIGKNDAI GKVFVGYNLE HHHHHH.

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

    Syt1 Human
  • View Data Sheet

    Name :

    LY9 Human

    Description:

    Lymphocyte Antigen 9 Human Recombinant

    Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.

    Product # :

    PRO-2338

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    Description

    LY9 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 416 amino acids (48-454 aa) and having a molecular mass of 45.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).LY9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LY9 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lymphocyte Antigen 9, also known as LY9 is a member of the SLAM family of immunomodulatory receptors, LY9 interacts with the adaptor molecule SAP . LY9 plays a part in adhesion reactions between T lymphocytes and accessory cells via homophilic interaction. LY9 promotes T-cell differentiation into a helper T-cell Th17 phenotype which leads to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Furthermore it also promotes recruitment of RORC to the IL-17 promoter. LY9 is implicated in the maintenance of peripheral cell tolerance through serving as a negative regulator of the immune response. LY9 disables autoantibody responses as well as inhibits IFN-gamma secretion by CD4(+) T-cells. Moreover, LY9 negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells. Systemic Lupus Erythematosus is one of the diseases which are associated with LY9.

    • Synonyms

      Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.

    • 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

      ADLKDSAPTV VSGILGGSVT LPLNISVDTE IENVIWIGPK NALAFARPKE NVTIMVKSYL GRLDITKWSY SLCISNLTLN DAGSYKAQIN QRNFEVTTEE EFTLFVYEQL QEPQVTMKSV KVSENFSCNI TLMCSVKGAE KSVLYSWTPR EPHASESNGG SILTVSRTPC DPDLPYICTA QNPVSQRSSL PVHVGQFCTD PGASRGGTTG ETVVGVLGEP VTLPLALPAC RDTEKVVWLF NTSIISKERE EAATADPLIK SRDPYKNRVW VSSQDCSLKI SQLKIEDAGP YHAYVCSEAS SVTSMTHVTL LIYRRLRKPK ITWSLRHSED GICRISLTCS VEDGGNTVMY TWTPLQKEAV VSQGESHLNV SWRSSENHPN LTCTASNPVS RSSHQFLSEN ICSGPERNTK HHHHHH

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

    Ly9 Human
  • View Data Sheet

    Name :

    CD105 Human, Sf9

    Description:

    Endoglin Human Recombinant, Sf9

    CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    Product # :

    CYT-389

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    Description

    CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

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

    Biological Activity

    Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

    Citations

    More Info

    • Introduction

      Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
      The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

    • Synonyms

      CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

    • Background

      What is the molecular weight/Mw of CD105 Protein?
      CD105 Protein has a total Mw of 90kDa.

      What is the source or expression system of CD105 Protein?
      Sf9 Insect Cells.

      What is the Purity of CD105 Protein?
      CD105 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD105 Protein?
      Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

      What is the amino acid sequence of CD105 Protein?
      MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

      What applications can CD105 Protein be used in?
      CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD105 Protein?
      The endotoxin level is minimal, CD105 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.

    Endoglin Human Sf9
  • View Data Sheet

    Name :

    CX3CL1 Human, Sf9

    Description:

    Fractalkine (CX3CL1) Human Recombinant, Sf9

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-042

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    Description

    Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Fractalkine solution (1 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CX3CL1 Human, Sf9-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • 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

      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.

      What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
      The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

      What applications can CX3CL1 HUMAN, SF9 Protein be used in?
      CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
      The endotoxin level is minimal, CX3CL1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CX3CL1 HUMAN, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CX3CL1 HUMAN, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Cx3Cl1 Human
  • View Data Sheet

    Name :

    LMO1 Human

    Description:

    LIM Domain Only 1 Human Recombinant

    Rhombotin-1, Cysteine-rich protein TTG-1, LIM domain only protein 1, T-cell translocation protein 1, RBTN1, RHOM1, TTG1, LMO-1, LMO1.

    Product # :

    PRO-1457

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    Description

    LMO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (1-156 a.a) and having a molecular mass of 20.2kDa.LMO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LMO1protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      LIM domain only 1 (LMO1) is a protein-coding gene. LMO1 encodes a transcriptional regulator which contains two cysteine-rich LIM domains but lacks a DNA-binding domain. LIM domains might play a part in protein interactions; hence the protein may regulate transcription by competitively binding to specific DNA-binding transcription factors.

    • Synonyms

      Rhombotin-1, Cysteine-rich protein TTG-1, LIM domain only protein 1, T-cell translocation protein 1, RBTN1, RHOM1, TTG1, LMO-1, LMO1.

    • 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 MGSMMVLDKE DGVPMLSVQP KGKQKGCAGC NRKIKDRYLL KALDKYWHED CLKCACCDCR LGEVGSTLYT KANLILCRRD YLRLFGTTGN CAACSKLIPA FEMVMRARDN VYHLDCFACQ LCNQRFCVGD KFFLKNNMIL CQMDYEEGQL NGTFESQVQ

    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.

    Lmo1 Human
  • View Data Sheet

    Name :

    GDF3 Human

    Description:

    Growth Differentiation Factor-3 Human Recombinant

    Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    Product # :

    CYT-694

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    Description

    GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.

    • Synonyms

      Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 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 GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

    • Background

      What is the molecular weight/Mw of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein has a total Mw of 14.15XkDa.

      What is the source or expression system of GDF3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF3 HUMAN Protein?
      The biological functionality of GDF3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GDF3 HUMAN Protein?
      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

      What applications can GDF3 HUMAN Protein be used in?
      GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF3 HUMAN Protein?
      The endotoxin level is minimal, GDF3 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.

    Gdf3 Human
  • View Data Sheet

    Name :

    Influenza-A H3N2 Antibody

    Description:

    H3N2/HA1, Mouse Anti-Human

    Product # :

    ANT-080

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    • More Info
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    Formulation

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

    Citations

    More Info

    • Introduction

      H3N2 is a subtype of the influenza A virus. Its name derives from the forms of the two kinds of proteinson the surface of its coat, hemagglutinin(H) and neuraminidase(N). H3N2 exchanges genes for internal proteins with other influenza subtypes. H3N2 has tended to dominate in prevalence over H1N1, H1N2, and influenza B. H3N2 strain descended from H2N2by antigenic shift, in which genes from multiple subtypes re-assorted to form a new virus. Both the H2N2and H3N2 strains contained genesfrom avian influenzaviruses.

    • Immunogen

      Anti-human Influenza-A H3N2 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human H3N2/HA1 amino acids 17-345 purified from Baculovirus.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1B7AT.

    • Applications

      Influenza-A H3N2 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      H3N2/HA1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Influenza A H3N2 Antibody Pat1B7At
  • View Data Sheet

    Name :

    TNF a Rat

    Description:

    Tumor Necrosis Factor-Alpha Rat Recombinant

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

    Product # :

    CYT-393

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    Description

    Tumor Necrosis Factor-a Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17339.44 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The concentrated protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer and 0.1M NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 IU/mg.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLIY SQVLFKGQGC PDYVLLTHTV SRFATSYQEK VSLLSAIKSP CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV YFGVIAL.

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

    Tnf Alpha Rat
  • View Data Sheet

    Name :

    C3a Human

    Description:

    Complement C3a Human

    Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    Product # :

    PRO-2685

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    Description

    Human Complement C3a produced in Human plasma is an non glycosylated polypeptide chain containing 77 amino acids having a molecular weight of 9,089 daltons.

    Source

    Human Plasma.

    Formulation

    C3a solution contains Phosphate buffered saline, pH 7.2.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Native human C3a is created by cleavage of human C3 protein by a human C3 convertase. C3a is a member of the anaphylatoxin family of three proteins (C3a, C4a and C5a) created by the activation of complement. C3a mediates various inflammatory responses including smooth muscle contraction, increased vascular permeability, vasodilation and release of histamine from mast cells and basophils. C3a (In contrast to C5a) does not exhibit significant neutrophil stimulating activities and does not induce chemotaxis, granule release or superoxide production. C3a acts through the C3a Receptor which is a G-protein coupled receptor found mainly on peripheral tissues, lymphoid cells and in the central nervous system. These activities of C3a are inactivated by removal of the C-terminal arginine which happens rapidly in plasma due to the action of carboxypeptidase N.

    • Synonyms

      Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      C3a 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, HTLV-I &II 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.

    C3A Human
  • View Data Sheet

    Name :

    Thyroglobulin Human, Biotin

    Description:

    Thyroglobulin Human, Biotinylated

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2563

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    Description

    Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).

    Source

    Native, Isolated from human thyroid glands.

    Formulation

    Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
      Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.

    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered 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 IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

    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.

    Thyroglobulin Protein
  • View Data Sheet

    Name :

    S.Typhi OMP 52kDa

    Description:

    Salmonella Typhi Outer Membrane Protein 52kDa Recombinant

    Product # :

    STY-003

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    Description

    Recombinant S.Typhi OMP produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 52 kDa and fused to a His tag at C-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.

    Citations

    More Info

    • Introduction

      Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized S.Typhi OMP between 2-8°C, do not freeze. Upon reconstitution S.Typhi OMP should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

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

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

    Styphi Omp 52Kda
  • View Data Sheet

    Name :

    Cys-Protein-A/G/L

    Description:

    Cys-Protein A/G/L Recombinant

    Product # :

    PRO-1935

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    Citations

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE EPRARPGSGS GKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.

    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.

    Cys Protein A G L
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