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Search results

1000 results found for “serum amyloid a”

Name

Description

Product #

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  • View Data Sheet

    Name :

    DFFA Human

    Description:

    DNA Fragmentation Factor Subunit Alpha Human Recombinant

    DNA fragmentation factor subunit alpha, DNA fragmentation factor 45 kDa subunit, DFF-45, Inhibitor of CAD, ICAD, DFFA, DFF1, DFF45.

    Product # :

    PRO-718

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    Description

    DFFA Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 351 amino acids (1- 331 a.a.) and having a molecular mass of 38.7kDa.The DFFA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DFF is a heterodimeric protein of 40kDa (DFFB) and 45kDa (DFFA) subunits. DFFA (DNA fragmentation factor subunit alpha) is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF is activated once DFFA is cleaved by caspase-3. The cleaved fragments of DFFA detach from DFFB (the active component of DFF), which in turn triggers DNA fragmentation as well as chromatin condensation during apoptosis. Apoptosis is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units.
      A reduced level of DFFA detected in ovarian endometriosis may be a part of an apoptosis-resistant mechanism enhancing the disease progression.
      DFFA at chromosome 1 shows rare allelic variants in neuroblastoma tumors.

    • Synonyms

      DNA fragmentation factor subunit alpha, DNA fragmentation factor 45 kDa subunit, DFF-45, Inhibitor of CAD, ICAD, DFFA, DFF1, DFF45.

    • 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 MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL AIDKSLTPVT LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD GGTAWISQES FDVDETDSGA GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV DAPCSDLAQE LRQSCATVQR LQHTLQQVLD QREEVRQSKQ LLQLYLQALE KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH ILTALREKQA PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE WELALRLQQT QSLHSLRSIS ASKASPPGDL QNPKRARQDP T.

    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.

    Dffa Human
  • View Data Sheet

    Name :

    ARL14 Human

    Description:

    ADP-Ribosylation Factor-Like 14 Human Recombinant

    ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.

    Product # :

    PRO-936

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    Description

    ARL14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 23.8kDa (Molecular weight on SDS-PAGE will appear higher).ARL14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARL14 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol, 200mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ADP-ribosylation factor-like 14 (ARL14) is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. ARL14 is GTPase which recruits MYO1E to MHC class II-containing vesicles via the effector protein C11orf46/ARF7EP and thus controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. MHC-II transport was controlled by the GTPase ARL14/ARF7, which recruits the motor myosin 1E via an effector protein ARF7EP.

    • Synonyms

      ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.

    • 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 MGSLGSKNPQ TKQAQVLLLG LDSAGKSTLL YKLKLAKDIT TIPTIGFNVE MIELERNLSL TVWDVGGQEK MRTVWGCYCE NTDGLVYVVD STDKQRLEES QRQFEHILKN EHIKNVPVVL LANKQDMPGA LTAEDITRMF KVKKLCSDRN WYVQPCCALT GEGLAQGFRK LTGFVKSHMK SRGDTLAFFK QN.

    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.

    Arl14 Human
  • View Data Sheet

    Name :

    EDA2R Human

    Description:

    Ectodysplasin A2 Receptor Human Recombinant

    Ectodysplasin A2 Receptor, XEDAR, TNFRSF27, EDA-A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDAA2R, EDA-A2R, Tumor Necrosis Factor Receptor Superfamily Member 27, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, EDAR2.

    Product # :

    PRO-1744

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    Description

    EDA2R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-138 a.a) and having a molecular mass of 17.7kDa.EDA2R is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EDA2R protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EDA2R (ectodysplasin A2 receptor) mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated through binding to TRAF3 and TRAF6. In addition, Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA2R specifically binds to EDA-A2 isoform. This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain however it lacks an N-terminal signal peptide. Alternatively spliced transcript variants have been found for this gene. Among the diseases associated with EDA2R are ectodermal dysplasia 1, hypohidrotic, x-linked, and hypohidrotic ectodermal dysplasia.

    • Synonyms

      Ectodysplasin A2 Receptor, XEDAR, TNFRSF27, EDA-A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDAA2R, EDA-A2R, Tumor Necrosis Factor Receptor Superfamily Member 27, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, EDAR2.

    • 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 MGSMDCQENE YWDQWGRCVT CQRCGPGQEL SKDCGYGEGG DAYCTACPPR RYKSSWGHHR CQSCITCAVI NRVQKVNCTA TSNAVCGDCL PRFYRKTRIG GLQDQECIPC TKQTPTSEVQ CAFQLSLVEA DAPTVPPQEA T

    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.

    Eda2R Human
  • View Data Sheet

    Name :

    KRT5 Human

    Description:

    Cytokeratin 5 Human Recombinant

    Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.

    Product # :

    PRO-1940

    Price :

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    Description

    KRT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 613 amino acids (1-590) and having a molecular mass of 64.8 kDa.KRT5 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The KRT5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytokeratin 5 (KRT5) belongs to the keratin gene family. The type II cytokeratins are comprised of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed throughout differentiation of simple and stratified epithelial tissues. The type II cytokeratins are clustered in a region of chromosome 12q12-q13. The KRT5 type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. Mutations in these genes are linked with a complex of diseases termed epidermolysis bullosa simplex.

    • Synonyms

      Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.

    • 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 MGSMSRQSSV SFRSGGSRSF STASAITPSV SRTSFTSVSR SGGGGGGGFG RVSLAGACGV GGYGSRSLYN LGGSKRISIS TSGGSFRNRF GAGAGGGYGF GGGAGSGFGF GGGAGGGFGL GGGAGFGGGF GGPGFPVCPP GGIQEVTVNQ SLLTPLNLQI DPSIQRVRTE EREQIKTLNN KFASFIDKVR FLEQQNKVLD TKWTLLQEQG TKTVRQNLEP LFEQYINNLR RQLDSIVGER GRLDSELRNM QDLVEDFKNK YEDEINKRTT AENEFVMLKK DVDAAYMNKV ELEAKVDALM DEINFMKMFF DAELSQMQTH VSDTSVVLSM DNNRNLDLDS IIAEVKAQYE EIANRSRTEA ESWYQTKYEE LQQTAGRHGD DLRNTKHEIS EMNRMIQRLR AEIDNVKKQC ANLQNAIADA EQRGELALKD ARNKLAELEE ALQKAKQDMA RLLREYQELM NTKLALDVEI ATYRKLLEGE ECRLSGEGVG PVNISVVTSS VSSGYGSGSG YGGGLGGGLG GGLGGGLAGG GSGSYYSSSS GGVGLSGGLS VGGSGFSASS GRGLGVGFGS GGGSSSSVKF VSTTSSSRKS FKS.

    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.

    Krt5 Human
  • View Data Sheet

    Name :

    PSMA1 Human

    Description:

    Proteasome Subunit Alpha Type 1 Human Recombinant

    Proteasome (prosome macropain) subunit alpha type 1, PROS30, HC2, NU, Macropain subunit C2, Multicatalytic endopeptidase complex subunit C2, Proteasome component C2, Proteasome nu chain, 30 kDa prosomal protein, protein P30-33K, PROS-30, PSC2, EC 3.4.25.1.

    Product # :

    ENZ-178

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    Description

    PSMA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 32.0 kDa.PSMA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PSMA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PSMA1 is a prosomal protein who takes part in a nonlysosomal ATP/ubiquitin-dependent proteolytic pathway. PSMA1 is a multicatalytic proteinase complex that is characterized by its capacity to cleave peptides with Arg, Phe, Tyr, Leu, and Glu next to the leaving group at neutral or slightly basic pH. PSMA1 is vastly expressed in prostate epithelium.

    • Synonyms

      Proteasome (prosome macropain) subunit alpha type 1, PROS30, HC2, NU, Macropain subunit C2, Multicatalytic endopeptidase complex subunit C2, Proteasome component C2, Proteasome nu chain, 30 kDa prosomal protein, protein P30-33K, PROS-30, PSC2, EC 3.4.25.1.

    • 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 MGSMFRNQYD NDVTVWSPQG RIHQIEYAME AVKQGSATVG LKSKTHAVLV ALKRAQSELA AHQKKILHVD NHIGISIAGL TADARLLCNF MRQECLDSRF VFDRPLPVSR LVSLIGSKTQ IPTQRYGRRP YGVGLLIAGY DDMGPHIFQT CPSANYFDCR AMSIGARSQS ARTYLERHMS EFMECNLNEL VKHGLRALRE TLPAEQDLTT KNVSIGIVGK DLEFTIYDDD DVSPFLEGLE ERPQRKAQPA QPADEPAEKA DEPMEH

    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.

    Psma1 Human
  • View Data Sheet

    Name :

    RCHY1 Human

    Description:

    Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant

    ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    Product # :

    PRO-1536

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    Description

    RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.

    • Synonyms

      ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    • 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 MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.

    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.

    Rchy1 Human
  • View Data Sheet

    Name :

    YWHAE Human

    Description:

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

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

    Product # :

    PKA-253

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    Description

    YWHAE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids (1-255) and having a molecular mass of 29 kDa. YWHAE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAE solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% 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 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.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      YWHAE Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASWRIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVFYYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVFYYEILNSPDR 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
  • View Data Sheet

    Name :

    Ara h 2.0201

    Description:

    Allergen Ara h 2.0201 (Conglutin-7) Recombinant

    Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.

    Product # :

    ALR-007

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    Description

    Recombinant Allergen Ara h 2.0201 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 20,000 Dalton. Ara h 2.0201 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Ara h 2.0201 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ara h 2 comprises of 2 isoforms: Ara h 2.0101 and Ara h 2.0201. Ara h 2.0201 is the most important peanut allergen which binds IgE. Ara h 2.0201 is a Weak inhibitor of trypsin and is a conglutin storage protein which accounts together with Ara h 6.0101 for the majority of the IgE immune response.

    • Synonyms

      Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

    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.

    Ara H 20201
  • View Data Sheet

    Name :

    GDF11 Human, His

    Description:

    Growth and Differentiation factor 11 Human Recombinant, His Tag

    Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

    Product # :

    CYT-887

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    Description

    GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.

    • Synonyms

      Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

    • 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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

    • Background

      What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
      GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.

      What is the source or expression system of GDF11 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF11 HUMAN, HIS Protein?
      GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF11 HUMAN, HIS Protein?
      The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

      What applications can GDF11 HUMAN, HIS Protein be used in?
      GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF11 HUMAN, HIS Protein?
      The endotoxin level is minimal, GDF11 HUMAN, HIS 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.

    Gdf11 Human His
  • View Data Sheet

    Name :

    SARS Human

    Description:

    Seryl-tRNA Synthetase Human Recombinant

    Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    Product # :

    ENZ-229

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    Description

    SARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (1-514) and having a molecular mass of 61.2kDa.SARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SARS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Seryl-tRNA synthetase, cytoplasmic (SARS) is a member of the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases’ role is to catalyze the aminoacylation of tRNAs by their corresponding amino acids, as a result linking amino acids with tRNA-contained nucleotide triplets. The SARS enzyme catalyzes the attachment of serine to tRNA (Ser). SARS enzyme is probably able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be then converted into selenocysteinyl-tRNA (Sec).

    • Synonyms

      Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    • 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 MGSMVLDLDL FRVDKGGDPA LIRETQEKRF KDPGLVDQLV KADSEWRRCR FRADNLNKLK NLCSKTIGEK MKKKEPVGDD ESVPENVLSF DDLTADALAN LKVSQIKKVR LLIDEAILKC DAERIKLEAE RFENLREIGN LLHPSVPISN DEDVDNKVER IWGDCTVRKK YSHVDLVVMV DGFEGEKGAV VAGSRGYFLK GVLVFLEQAL IQYALRTLGS RGYIPIYTPF FMRKEVMQEV AQLSQFDEEL YKVIGKGSEK SDDNSYDEKY LIATSEQPIA ALHRDEWLRP EDLPIKYAGL STCFRQEVGS HGRDTRGIFR VHQFEKIEQF VYSSPHDNKS WEMFEEMITT AEEFYQSLGI PYHIVNIVSG SLNHAASKKL DLEAWFPGSG AFRELVSCSN CTDYQARRLR IRYGQTKKMM DKVEFVHMLN ATMCATTRTI CAILENYQTE KGITVPEKLK EFMPPGLQEL IPFVKPAPIE QEPSKKQKKQ HEGSKKKAAA RDVTLENRLQ NMEVTDA.

    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.

    Sars Human
  • View Data Sheet

    Name :

    SHH (C24II) Human

    Description:

    Sonic HedgeHog (C24II) Human Recombinant

    Sonic Hedgehog, MCOPCB5, SMMCI, HLP3, HPE3, Sonic Hedgehog (Drosophila) Homolog, Sonic Hedgehog Homolog (Drosophila), Sonic Hedgehog Homolog, Sonic Hedgehog Protein, TPTPS, HHG-1, HHG1, TPT, SHH (C24II).

    Product # :

    CYT-888

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    Description

    SHH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (24-197 a.a.) and having a molecular mass of 19.8kDa (The Cys at position 24 has been replaced with 2 Ile).The SHH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SHH protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sonic Hedgehog is part of a small group of secreted proteins which are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      Sonic Hedgehog, MCOPCB5, SMMCI, HLP3, HPE3, Sonic Hedgehog (Drosophila) Homolog, Sonic Hedgehog Homolog (Drosophila), Sonic Hedgehog Homolog, Sonic Hedgehog Protein, TPTPS, HHG-1, HHG1, TPT, SHH (C24II).

    • 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

      MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG

    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.

    Shh C24Ii Human
  • View Data Sheet

    Name :

    OCM Human

    Description:

    Oncomodulin-1 Human Recombinant

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

    Product # :

    PRO-143

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    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.

    Citations

    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 :

    TCEAL3 Human

    Description:

    Transcription Elongation Factor A (SII)-Like 3 Human Recombinant

    Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.

    Product # :

    PRO-1128

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    Description

    TCEAL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 224 amino acids (1-200) and having a molecular mass of 25.0 kDa.TCEAL3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TCEAL3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TCEAL3 belongs to the transcription elongation factor A (SII)-like (TCEAL) gene family. TCEAL family members hold TFA domains and operate as nuclear phosphoproteins which control transcription in a promoter context-dependent fashion. Various family members are situated in the X chromosome.

    • Synonyms

      Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.

    • 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 MGSHMEKPYN KNEGNLENEG KPEDEVEPDD EGKSDEEEKP DVEGKTECEG KREDEGEPGD EGQLEDEGSQ EKQGRSEGEG KPQGEGKPAS QAKPESQPRA AEKRPAEDYV PRKAKRKTDR GTDDSPKDSQ EDLQERHLSS EEMMRECGDV SRAQEELRKK QKMGGFHWMQ RDVQDPFAPR GQRGVRGVRG GGRGQRGLHD IPYL

    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.

    Tceal3 Human
  • View Data Sheet

    Name :

    TGFB1 (113 a.a.) Human

    Description:

    Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

    Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

    Product # :

    CYT-679

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    Description

    TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    • Synonyms

      Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 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

      MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.

    • Background

      Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential

      Abstract:


      Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.

      Introduction:


      TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.

      Production Process and Characteristics:


      TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.

      Therapeutic Applications:


      TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.

      Advantages and Challenges:


      The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.

      Conclusion:


      TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

    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.

    Tgf Beta 1 Human 113 Aa
  • View Data Sheet

    Name :

    CENPA Human

    Description:

    Centromere Protein A Human Recombinant

    Histone H3-like centromeric protein A, Centromere protein A, CENP-A, Centromere autoantigen A, CENPA.

    Product # :

    PRO-389

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    Description

    CENPA Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 17,015 Dalton. CENPA is expressed with a -6x His tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    CENPA is supplied in 20mM HEPES buffer pH-8, 100mM sodium chloride, and 6M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Centromere proteins are a group of proteins which form and/or mediate the function of centromeres, the central structures of chromosomes to which spindle fibers/microtubuli attach and pull the chromosomes apart in cell division. Currently, 9 centromere proteins are known and designated CENPA to CENP-I. Most of the centromere proteins are targets of autoantibodies, the anti-centromere antibodies.
      CENPA is another important centromeric autoantigen in addition to CENPB: it has a molecular weight of approx. 20 kDa and is incorporated into centromeric chromatin due to its histone-like properties. CENPA antibodies are an important marker for correct diagnosis of Scleroderma / CREST syndrome in CENPB-autoantibody negative patients.

    • Synonyms

      Histone H3-like centromeric protein A, Centromere protein A, CENP-A, Centromere autoantigen A, CENPA.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • 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. Standard ELISA test (checker-board analysis of positive/negative sera panels including CDC international reference sera).

    • coating concentration

      0.15-0.4 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    • Applications

      Western-Blot with monoclonal anti-hexa-His-tag antibody & Scleroderma patient sera.

    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.

    Cenpa Human
  • View Data Sheet

    Name :

    PTP4A2 Human

    Description:

    Protein Tyrosine Phosphatase Type IVA Member 2 Human Recombinant

    HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, ptp-IV1a, ptp-IV1b, PTP4A, PTPCAAX2.

    Product # :

    ENZ-558

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    Description

    Recombinant Human PTP4A2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-167 a.a.) and having a molecular mass of 23.2 kDa. PTP4A2 is fused to a 36 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTP4A2 (0.5mg/ml) protein solution contains 20mM Tris-HCl, pH-8, 1mM EDTA and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PTP4A2 is part of a small class of the protein tyrosine phosphatase (PTP) family. PTP4A2 is localized to the early endosome that take part in a variety of cellular activities. PTP4A2 protein interacts with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), therefore has a role as a regulator of GGT II activity. Overexpression of PTP4A2 in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis.

    • Synonyms

      HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, ptp-IV1a, ptp-IV1b, PTP4A, PTPCAAX2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNRP APVEISYENM RFLITHNPTN ATLNKFTEEL KKYGVTTLVR VCDATYDKAP
      VEKEGIHVLD WPFDDGAPPP NQIVDDWLNL LKTKFREEPG CCVAVHCVAG LGRAPVLVAL ALIECGMKYE DAVQFIRQKR RGAFNSKQLL
      YLEKYRPKMR LRFRDTNGHC CVQ.

    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.

    Ptp4A2 Human
  • View Data Sheet

    Name :

    HBG1 Human

    Description:

    Hemoglobin Gamma A Human Recombinant

    HBGA, HBGR, HSGGL1, PRO2979, Hemoglobin subunit gamma-1, Gamma-1-globin, Hb F Agamma, Hemoglobin gamma-1 chain, Hemoglobin gamma-A chain, HBG1.

    Product # :

    PRO-1502

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    Description

    HBG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 170 amino acids (1-147) and having a molecular mass of 18kDa. HBG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HBG1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The gamma globin genes which are HBG1 and HBG2, usually expressed in the fetal liver, spleen and bone marrow. 2 gamma chains together along with 2 alpha chains comprise fetal hemoglobin (HbF) which is normally replaced by mature hemoglobin (HbA) at birth. Gamma chain production continues into adulthood in several beta-thalassemias and linked situations. The two types of gamma chains differ at residue 136 where glycine is found in the G-gamma product (HBG2) and alanine is found in the A-gamma product (HBG1). The former is predominant at birth.

    • Synonyms

      HBGA, HBGR, HSGGL1, PRO2979, Hemoglobin subunit gamma-1, Gamma-1-globin, Hb F Agamma, Hemoglobin gamma-1 chain, Hemoglobin gamma-A chain, HBG1.

    • 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 MGSMGHFTEE DKATITSLWG KVNVEDAGGE TLGRLLVVYP WTQRFFDSFG NLSSASAIMG NPKVKAHGKK VLTSLGDATK HLDDLKGTFA QLSELHCDKL HVDPENFKLL GNVLVTVLAI HFGKEFTPEV QASWQKMVTA VASALSSRYH.

    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.

    Hbg1 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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    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

    Citations

    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 :

    APRIL Human

    Description:

    APRIL Human Recombinant

    Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

    Product # :

    CYT-815

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    Description

    APRIL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (105-247) and having a molecular mass of 17.6kDa.APRIL is fused to a 16 amino acid T7-tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    APRIL protein solution (1mg/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.

    sds-page

    APRIL-sds-page - Product image 1

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

    • Background

      APRIL Human Recombinant: Expanding the Horizons of Immunotherapy

      Abstract:


      APRIL (A Proliferation-Inducing Ligand) is a promising molecule within the tumor necrosis factor (TNF) superfamily that plays a pivotal role in immune regulation. This research paper provides an overview of APRIL human recombinant, exploring its potential applications in immunotherapy. Understanding the mechanisms and therapeutic implications of APRIL holds promise in the field of immune-related disorders. This article presents a concise analysis of APRIL, highlighting its potential as a therapeutic target.

      Introduction:


      Immunotherapy has revolutionized the treatment of various diseases by harnessing the power of the immune system. APRIL, a member of the TNF superfamily, has emerged as a potential candidate for immunotherapeutic interventions. This paper provides an overview of APRIL, shedding light on its structure, function, and potential applications in immunotherapy.

      APRIL Structure and Function:


      APRIL is a transmembrane protein that can be proteolytically cleaved, leading to the generation of soluble forms. It interacts with its receptors, such as BCMA and TACI, to regulate immune responses. APRIL influences B-cell activation, proliferation, and antibody production, making it a compelling target for immunotherapeutic strategies.

      Immunotherapeutic Applications of APRIL Human Recombinant:


      APRIL human recombinant holds great potential in immunotherapy. By modulating APRIL activity, it may be possible to enhance immune responses against cancer cells or dampen immune dysregulation in autoimmune disorders. Additionally, APRIL-based therapeutics could be developed to target specific immune cell populations or enhance the efficacy of existing immunotherapies.

      Challenges and Future Directions:


      Although APRIL shows promise, there are challenges to overcome. Further research is needed to elucidate the precise mechanisms of APRIL-mediated immune regulation and identify optimal therapeutic approaches. Additionally, safety considerations and potential side effects must be thoroughly evaluated.

      Conclusion:


      APRIL human recombinant represents a valuable tool for advancing immunotherapy. Understanding the structure, function, and therapeutic potential of APRIL opens up new avenues for treating immune-related disorders. Continued research and development in this field have the potential to revolutionize the landscape of immunotherapy, improving patient outcomes and expanding the possibilities for personalized medicine.

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

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

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

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

      What is the amino acid sequence of APRIL Protein?
      MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

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

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

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

    April Human
  • View Data Sheet

    Name :

    SRI Human

    Description:

    Sorcin Human Recombinant

    Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.

    Product # :

    PRO-166

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    Description

    SRI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-198 a.a.) and having a molecular mass of 24.1kDa. The SRI is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SRI solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.

    • Synonyms

      Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.

    • 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 MGSMAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS 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.

    Sri Human
  • View Data Sheet

    Name :

    Stratifin Human

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Sigma Human Recombinant

    14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.

    Product # :

    PKA-357

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    Description

    Stratifin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-248) and having a molecular mass of 27.7 kDa. Stratifin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Stratifin solution containing 20mM Tris-HCl pH-8, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Stratifin is part of the 14-3-3 family. The 14-3-3 family of proteins plays an important regulatory function in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are 7 isoforms, beta, gamma, epsilon, sigma, zeta, tau and eta that have been identified in mammals. Stratifin is an epithelial cell marker that functions as a tumor suppressor whose expression can be down regulated via methylation. Failure of Stratifin expression results in a defective G2/M phase checkpoint and results in epithelial and non-epithelial tumorigenesis.

    • Synonyms

      14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.

    • 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

      MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS.

    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.

    Stratifin Human
  • View Data Sheet

    Name :

    CHMP2A Human

    Description:

    Chromatin Modifying Protein 2A Human Recombinant

    Charged multivesicular body protein 2a, Chromatin-modifying protein 2a, Vacuolar protein-sorting-associated protein 2-1, Putative breast adenocarcinoma marker BC-2, Vps2-1, hVps2-1, CHMP2A, BC2, CHMP2, BC-2, VPS2, VPS2A.

    Product # :

    PRO-503

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    Description

    CHMP2A Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 242 amino acids (1-222 a.a.) and having a molecular mass of 27.2 kDa.The CHMP2A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CHMP2A solution contains 20mM Tris-HCl buffer (pH8.0) , 0.1M NaCl 1mM DTT, and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chromatin modifying protein 2A (CHMP2A) is a member of the SNF7 family and it is a component of the ESCRT III complex, which is required for MVBs (multivesicular bodies) formation and sorting of endosomal cargo proteins into MVBs.
      The MVB pathway mediates release of transmembrane proteins into the lumen of the lysosome for degradation. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins generally detach from the invaginating membrane before the ILV (intraluminal vesicles) is released. ESCRT-III proteins are thought to mediate the basic vesicle extrusion and/or membrane fission activities, probably in conjunction with the AAA ATPase VPS4.

    • Synonyms

      Charged multivesicular body protein 2a, Chromatin-modifying protein 2a, Vacuolar protein-sorting-associated protein 2-1, Putative breast adenocarcinoma marker BC-2, Vps2-1, hVps2-1, CHMP2A, BC2, CHMP2, BC-2, VPS2, VPS2A.

    • 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 MDLLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLETQE KKIIADIKKM AKQGQMDAVR IMAKDLVRTR RYVRKFVLMR ANIQAVSLKI QTLKSNNSMA QAMKGVTKAM GTMNRQLKLP QIQKIMMEFE RQAEIMDMKE EMMNDAIDDA MGDEEDEEES DAVVSQVLDE LGLSLTDELS NLPSTGGSLS VAAGGKKAEA AASALADADA DLEERLKNLR RD.

    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.

    Chmp2A Human
  • View Data Sheet

    Name :

    Clusterin Human, His

    Description:

    Apolipoprotein-J Human Recombinant, His Tag

    CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.

    Product # :

    CYT-814

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    • sds-page
    • Citations

    Description

    Clusterin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 463 amino acids (23-449 a.a.) and having a molecular mass of 54.1kDa. Clusterin is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Clusterin protein solution (0.5mg/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.

    sds-page

    Clusterin-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 54.1kDa.

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

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

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

      What is the amino acid sequence of CLUSTERIN Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.

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

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

    Clusterin Human His
  • View Data Sheet

    Name :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MNAAQHDEAQ 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 TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.

    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.

    Protein A G His
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